ID G3VH13_SARHA Unreviewed; 711 AA.
AC G3VH13;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=SH3 domain binding protein 1 {ECO:0000313|Ensembl:ENSSHAP00000002467.2};
GN Name=SH3BP1 {ECO:0000313|Ensembl:ENSSHAP00000002467.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000002467.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000002467.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000002467.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; G3VH13; -.
DR Ensembl; ENSSHAT00000002494.2; ENSSHAP00000002467.2; ENSSHAG00000002182.2.
DR GeneTree; ENSGT00940000158369; -.
DR HOGENOM; CLU_013806_2_1_1; -.
DR InParanoid; G3VH13; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0005923; C:bicellular tight junction; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000145; C:exocyst; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0001891; C:phagocytic cup; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR GO; GO:0030215; F:semaphorin receptor binding; IEA:Ensembl.
DR GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0034329; P:cell junction assembly; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Ensembl.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0006911; P:phagocytosis, engulfment; IEA:Ensembl.
DR GO; GO:0030834; P:regulation of actin filament depolymerization; IEA:Ensembl.
DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IEA:Ensembl.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR047165; RHG17/44/SH3BP1-like.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR14130; 3BP-1 RELATED RHOGAP; 1.
DR PANTHER; PTHR14130:SF12; BARGIN-RELATED; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648}.
FT DOMAIN 18..260
FT /note="BAR"
FT /evidence="ECO:0000259|PROSITE:PS51021"
FT DOMAIN 274..467
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 489..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..210
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 489..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..607
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..667
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 77609 MW; 81AAC1510170F168 CRC64;
MMKRQLNRMR LQLSQTGGSA RVQETAEFLS EDLLQVEQRL DPAKRAAHNV HKRLQACLQG
QSGADMEKRV KKLPLMALSH TMAESIKELD AESSMGKALE MSCSIQSQLA RVLAEFEMAL
ERDVLQPLNR LSEEELPSIL KHKKNLQKLV LDWNALKSRL SQMAKNSSLG PGVGGPGGHN
PITNKLETLK EEEEELKKKV EQSKDEYLSD LYHFATKEDS YANYFITLLE LQASYHRKSL
SSLDSALAEL KESHGHTESS TRVSDGPSTK VYGVALRTHL QETGRDIALP LEACILMLLS
EGMKEEGLFR LAAGASVLKR LKQAMALNPS SLEEFCSDPH AVAGALKSYL RELPEPIMTF
ELYEDWMRAA NLKDPVARLE GLREVCGKLP QENLCNLRYL IKFLARLAKE QEVNKMTPSN
IAIVLGPNLL WPSIKDGDQA QLDAASVSSI QVVGVVEALI QNSDVLFPGD INFNVSGLFT
SPAILYQSHP QEQDSPKSEE FSATPSPSPV AKESKVELEP PPRPGSPKVS KNLTEAPASA
EDTVRKTKRP APARPMVPPP QILSSRTSPP IVSATASPPT QPQPQPQPQP QPQPQPQPQP
QPQPQPQSQS QSQPQSSTPG SPATPRALPR RQVGSNIKAP SVPPPLPPQP PQPVRRLSRP
SPASPSPLLT PSTETEVPGE ARGPEGDSCA SPGGVTTPPQ PRPRTLASDT D
//
