ID A0A8W8J8D2_MAGGI Unreviewed; 500 AA.
AC A0A8W8J8D2;
DT 14-DEC-2022, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2022, sequence version 1.
DT 28-JAN-2026, entry version 13.
DE RecName: Full=SH3 domain-containing protein {ECO:0000259|PROSITE:PS50002};
OS Magallana gigas (Pacific oyster) (Crassostrea gigas).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Magallana.
OX NCBI_TaxID=29159 {ECO:0000313|EnsemblMetazoa:G17159.23:cds, ECO:0000313|Proteomes:UP000005408};
RN [1] {ECO:0000313|EnsemblMetazoa:G17159.23:cds}
RP IDENTIFICATION.
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EnsemblMetazoa:G17159.23:cds};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
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DR AlphaFoldDB; A0A8W8J8D2; -.
DR EnsemblMetazoa; G17159.23; G17159.23:cds; G17159.
DR EnsemblMetazoa; G17159.7; G17159.7:cds; G17159.
DR Proteomes; UP000005408; Unassembled WGS sequence.
DR GO; GO:0005884; C:actin filament; IEA:TreeGrafter.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0030427; C:site of polarized growth; IEA:TreeGrafter.
DR GO; GO:0051015; F:actin filament binding; IEA:TreeGrafter.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0030833; P:regulation of actin filament polymerization; IEA:TreeGrafter.
DR CDD; cd11959; SH3_Cortactin; 1.
DR FunFam; 2.30.30.40:FF:000398; Hematopoietic cell-specific Lyn substrate 1; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR035716; Cortactin_SH3.
DR InterPro; IPR003134; Hs1_Cortactin.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10829; CORTACTIN AND DREBRIN; 1.
DR PANTHER; PTHR10829:SF23; CORTACTIN, ISOFORM A; 1.
DR Pfam; PF02218; HS1_rep; 5.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51090; CORTACTIN; 6.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005408};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 442..500
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..396
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..423
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 56103 MW; AEF7B7BF8EF8C6A4 CRC64;
QSSIMWKAAA GHSVKTGKPP VNDDDDDWET EADFVNDVSE QEQRWGAKTI EGSGHKGSLN
LDQLRQEVST DDKSVKQKQM EEGPKASYGY GGKFGVQKDR MDKSAVGSNY VADVEKHSSQ
TDAAKGFGGK YGVQKDRQDK AAVGFDYAGK TEKHQSQTDY SKGFGGKYGV QRDRQDKNAV
GWEHHEQVEK HESQKDYSKG FGGKYGVQTD RVDKSALGYE HHEQVDKHES QKDYSRGFGG
KYGVQTDRQD KSALGYDSQE KVALHPSQTD MSKGFGGKFG VDAENKDKSA GSYNDMQGVS
SSYTRTQADA SSEGARNIKA RFENLAKSGE EEAKKKAEEE RKRRQAREER EKEEQRRQQE
ERLNREKLEE EERAASQPEP QPEPEPEPEP EQEDYGDVSY QPEPVHRQVP EEPPAEEPED
AYEDTTPQDA YEDITPEPAK SSGGLTAVAI YDYQAADDDE ITFDPDDIIT DIEQVDEGWW
RGSCRGKNGL FPANYVEIQQ
//