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Conserved domains on  [gi|1958752395|ref|XP_038958941|]
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arfaptin-1 isoform X6 [Rattus norvegicus]

Protein Classification

BAR domain-containing protein( domain architecture ID 36964)

BAR (Bin/Amphiphysin/Rvs) domain-containing protein may bind membranes and detect membrane curvature

CATH:  1.20.1270.60
Gene Ontology:  GO:0097753|GO:0140090
PubMed:  19379681|16524918|14993925|15649145|30456600
SCOP:  4001895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAR super family cl12013
The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects ...
 134-211 3.03e-30

The Bin/Amphiphysin/Rvs (BAR) domain, a dimerization module that binds membranes and detects membrane curvature; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Mutations in BAR containing proteins have been linked to diseases and their inactivation in cells leads to altered membrane dynamics. A BAR domain with an additional N-terminal amphipathic helix (an N-BAR) can drive membrane curvature. These N-BAR domains are found in amphiphysins and endophilins, among others. BAR domains are also frequently found alongside domains that determine lipid specificity, such as the Pleckstrin Homology (PH) and Phox Homology (PX) domains which are present in beta centaurins (ACAPs and ASAPs) and sorting nexins, respectively. A FES-CIP4 Homology (FCH) domain together with a coiled coil region is called the F-BAR domain and is present in Pombe/Cdc15 homology (PCH) family proteins, which include Fes/Fes tyrosine kinases, PACSIN or syndapin, CIP4-like proteins, and srGAPs, among others. The Inverse (I)-BAR or IRSp53/MIM homology Domain (IMD) is found in multi-domain proteins, such as IRSp53 and MIM, that act as scaffolding proteins and transducers of a variety of signaling pathways that link membrane dynamics and the underlying actin cytoskeleton. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions. The I-BAR domain induces membrane protrusions in the opposite direction compared to classical BAR and F-BAR domains, which produce membrane invaginations. BAR domains that also serve as protein interaction domains include those of arfaptin and OPHN1-like proteins, among others, which bind to Rac and Rho GAP domains, respectively.


The actual alignment was detected with superfamily member smart01015:

Pssm-ID: 472257  Cd Length: 217  Bit Score: 110.82  E-value: 3.03e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752395  134 NTYKCTRQIISEKLGRGSR----TVDLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQKQLGDAFADLSLKSLE 209
Cdd:smart01015   1 KTYKKTKQVLIEKLGKKEDehvvASDAELDAKLELLRSTQRTYEDLLKLIEKYQQRLCNLSQTENELGDFFRDLSEKDPT 80


                   ..
gi 1958752395  210 LH 211
Cdd:smart01015  81 LK 82
 
Name Accession Description Interval E-value
Arfaptin smart01015
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
 134-211 3.03e-30

Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. The structure of arfaptin shows that upon binding to a small GTPase, arfaptin forms an elongated, crescent-shaped dimer of three-helix coiled-coils. The N-terminal region of ICA69 is similar to arfaptin.


Pssm-ID: 214974  Cd Length: 217  Bit Score: 110.82  E-value: 3.03e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752395  134 NTYKCTRQIISEKLGRGSR----TVDLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQKQLGDAFADLSLKSLE 209
Cdd:smart01015   1 KTYKKTKQVLIEKLGKKEDehvvASDAELDAKLELLRSTQRTYEDLLKLIEKYQQRLCNLSQTENELGDFFRDLSEKDPT 80


                   ..
gi 1958752395  210 LH 211
Cdd:smart01015  81 LK 82
BAR_Arfaptin cd07660
The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin; The BAR domain of Arfaptin-like proteins, ...
 155-211 1.90e-26

The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin; The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization and lipid binding module that can detect and drive membrane curvature. Arfaptins are ubiquitously expressed proteins implicated in mediating cross-talk between Rac, a member of the Rho family GTPases, and Arf (ADP-ribosylation factor) small GTPases. Arfaptins bind to GTP-bound Arf1, Arf5, and Arf6, with strongest binding to GTP-Arf1. Arfaptins also bind to Rac-GTP and Rac-GDP with similar affinities. The Arfs are thought to bind to the same surface as Rac, and their binding is mutually exclusive. Mammals contain at least two isoforms of Arfaptin. Arfaptin 1 has been shown to inhibit the activation of Arf-dependent phospholipase D (PLD) and the secretion of matrix metalloproteinase-9 (MMP-9), an enzyme implicated in cancer invasiveness and metastasis. Arfaptin 2 regulates the aggregation of the protein huntingtin, which is implicated in Huntington disease. Arfaptins are single-domain proteins with a BAR-like structure. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153344  Cd Length: 201  Bit Score: 100.48  E-value: 1.90e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752395 155 DLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQKQLGDAFADLSLKSLELH 211
Cdd:cd07660     1 DLELEAQIEVLRDTQRKYESVLRLARALASQFYQMLQTQKALGDAFADLSQKSPELQ 57
Arfaptin pfam06456
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
 153-211 1.23e-16

Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. The structure of arfaptin shows that upon binding to a small GTPase, arfaptin forms an elongated, crescent-shaped dimer of three-helix coiled-coils. The N-terminal region of ICA69 is similar to arfaptin.


Pssm-ID: 399453  Cd Length: 207  Bit Score: 74.70  E-value: 1.23e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752395 153 TVDLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQKQLGDAFADLSL--KSLELH 211
Cdd:pfam06456   8 TSDDELDAKLEVLRSIQRTYLGLVKLARNYSKRLYDLSQTQKELGDFFKDLGKheKQQAAG 68
 
Name Accession Description Interval E-value
Arfaptin smart01015
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
 134-211 3.03e-30

Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. The structure of arfaptin shows that upon binding to a small GTPase, arfaptin forms an elongated, crescent-shaped dimer of three-helix coiled-coils. The N-terminal region of ICA69 is similar to arfaptin.


Pssm-ID: 214974  Cd Length: 217  Bit Score: 110.82  E-value: 3.03e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958752395  134 NTYKCTRQIISEKLGRGSR----TVDLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQKQLGDAFADLSLKSLE 209
Cdd:smart01015   1 KTYKKTKQVLIEKLGKKEDehvvASDAELDAKLELLRSTQRTYEDLLKLIEKYQQRLCNLSQTENELGDFFRDLSEKDPT 80


                   ..
gi 1958752395  210 LH 211
Cdd:smart01015  81 LK 82
BAR_Arfaptin cd07660
The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin; The BAR domain of Arfaptin-like proteins, ...
 155-211 1.90e-26

The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin; The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization and lipid binding module that can detect and drive membrane curvature. Arfaptins are ubiquitously expressed proteins implicated in mediating cross-talk between Rac, a member of the Rho family GTPases, and Arf (ADP-ribosylation factor) small GTPases. Arfaptins bind to GTP-bound Arf1, Arf5, and Arf6, with strongest binding to GTP-Arf1. Arfaptins also bind to Rac-GTP and Rac-GDP with similar affinities. The Arfs are thought to bind to the same surface as Rac, and their binding is mutually exclusive. Mammals contain at least two isoforms of Arfaptin. Arfaptin 1 has been shown to inhibit the activation of Arf-dependent phospholipase D (PLD) and the secretion of matrix metalloproteinase-9 (MMP-9), an enzyme implicated in cancer invasiveness and metastasis. Arfaptin 2 regulates the aggregation of the protein huntingtin, which is implicated in Huntington disease. Arfaptins are single-domain proteins with a BAR-like structure. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153344  Cd Length: 201  Bit Score: 100.48  E-value: 1.90e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958752395 155 DLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQKQLGDAFADLSLKSLELH 211
Cdd:cd07660     1 DLELEAQIEVLRDTQRKYESVLRLARALASQFYQMLQTQKALGDAFADLSQKSPELQ 57
Arfaptin pfam06456
Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding ...
 153-211 1.23e-16

Arfaptin-like domain; Arfaptin interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules. The structure of arfaptin shows that upon binding to a small GTPase, arfaptin forms an elongated, crescent-shaped dimer of three-helix coiled-coils. The N-terminal region of ICA69 is similar to arfaptin.


Pssm-ID: 399453  Cd Length: 207  Bit Score: 74.70  E-value: 1.23e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958752395 153 TVDLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQKQLGDAFADLSL--KSLELH 211
Cdd:pfam06456   8 TSDDELDAKLEVLRSIQRTYLGLVKLARNYSKRLYDLSQTQKELGDFFKDLGKheKQQAAG 68
BAR_Arfaptin_like cd00011
The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-like proteins, a dimerization module that ...
 155-210 1.58e-07

The Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-like proteins, a dimerization module that binds and bends membranes; The BAR domain of Arfaptin-like proteins, also called the Arfaptin domain, is a dimerization, lipid binding and curvature sensing module present in Arfaptins, PICK1, ICA69, and similar proteins. Arfaptins are ubiquitously expressed proteins implicated in mediating cross-talk between Rac, a member of the Rho family GTPases, and Arf (ADP-ribosylation factor) small GTPases. Arfaptins bind to GTP-bound Arf1, Arf5, and Arf6, with strongest binding to GTP-Arf1. Arfaptins also binds to Rac-GTP and Rac-GDP with similar affinities. The Arfs are thought to bind to the same surface as Rac, and their binding is mutually exclusive. Protein Interacting with C Kinase 1 (PICK1) plays a key role in the trafficking of AMPA receptors, which are critical for regulating synaptic strength and may be important in cellular processes involved in learning and memory. Islet cell autoantigen 69-kDa (ICA69) is a diabetes-associated autoantigen that is involved in membrane trafficking at the Golgi complex in neurosecretory cells. ICA69 associates with PICK1 through their BAR domains to form a heterodimer which is involved in regulating the synaptic targeting and surface expression of AMPA receptors. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153270  Cd Length: 203  Bit Score: 49.92  E-value: 1.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958752395 155 DLELEAQIDILRDNKKKYENILKLAQTLSTQLFQMVHTQKQLGDAFADLSLKSLEL 210
Cdd:cd00011     1 DLELELQLELLRETKRKYESVLQLGRALTAHLYSLSQTQHALGDAFADLSQKDPEL 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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