ID Q10929_CAEEL Unreviewed; 469 AA. AC Q10929; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 2. DT 27-MAR-2024, entry version 169. DE SubName: Full=SH3 domain-containing protein {ECO:0000313|EMBL:CCD61521.1}; GN Name=abi-1 {ECO:0000313|EMBL:CCD61521.1, GN ECO:0000313|WormBase:B0336.6}; GN ORFNames=B0336.6 {ECO:0000313|WormBase:B0336.6}, CELE_B0336.6 GN {ECO:0000313|EMBL:CCD61521.1}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD61521.1, ECO:0000313|Proteomes:UP000001940}; RN [1] {ECO:0000313|EMBL:CCD61521.1, ECO:0000313|Proteomes:UP000001940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD61521.1, RC ECO:0000313|Proteomes:UP000001940}; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RA Sulson J.E., Waterston R.; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC -!- INTERACTION: CC Q10929; Q966J6: CELE_F41B4.1; NbExp=5; IntAct=EBI-315750, EBI-327612; CC Q10929; Q95Y95: M04F3.5; NbExp=4; IntAct=EBI-315750, EBI-2315841; CC Q10929; Q9TYX9: M57.1; NbExp=3; IntAct=EBI-315750, EBI-2315745; CC Q10929; P34400: mig-10; NbExp=6; IntAct=EBI-315750, EBI-2315872; CC Q10929; O62203: phm-2; NbExp=6; IntAct=EBI-315750, EBI-320780; CC Q10929; G5EDS1: vab-3; NbExp=6; IntAct=EBI-315750, EBI-319610; CC -!- SIMILARITY: Belongs to the ABI family. {ECO:0000256|ARBA:ARBA00010020}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284603; CCD61521.1; -; Genomic_DNA. DR RefSeq; NP_498224.1; NM_065823.4. DR AlphaFoldDB; Q10929; -. DR SMR; Q10929; -. DR DIP; DIP-25719N; -. DR IntAct; Q10929; 29. DR STRING; 6239.B0336.6.2; -. DR EPD; Q10929; -. DR PaxDb; 6239-B0336-6-1; -. DR PeptideAtlas; Q10929; -. DR EnsemblMetazoa; B0336.6.1; B0336.6.1; WBGene00015146. DR EnsemblMetazoa; B0336.6.2; B0336.6.2; WBGene00015146. DR GeneID; 175789; -. DR KEGG; cel:CELE_B0336.6; -. DR UCSC; B0336.6.1; c. elegans. DR AGR; WB:WBGene00015146; -. DR WormBase; B0336.6; CE29545; WBGene00015146; abi-1. DR eggNOG; KOG2546; Eukaryota. DR GeneTree; ENSGT00940000168654; -. DR HOGENOM; CLU_035421_0_0_1; -. DR InParanoid; Q10929; -. DR OMA; TDHYRSN; -. DR OrthoDB; 3028771at2759; -. DR PhylomeDB; Q10929; -. DR Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-CEL-9013149; RAC1 GTPase cycle. DR Reactome; R-CEL-9013423; RAC3 GTPase cycle. DR Proteomes; UP000001940; Chromosome III. DR Bgee; WBGene00015146; Expressed in germ line (C elegans) and 4 other cell types or tissues. DR GO; GO:0030424; C:axon; IDA:WormBase. DR GO; GO:0005737; C:cytoplasm; IDA:WormBase. DR GO; GO:0030425; C:dendrite; IDA:WormBase. DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase. DR GO; GO:0098793; C:presynapse; IEA:GOC. DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase. DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB. DR GO; GO:0016477; P:cell migration; IGI:WormBase. DR GO; GO:0048858; P:cell projection morphogenesis; IMP:WormBase. DR GO; GO:0001764; P:neuron migration; IMP:WormBase. DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IMP:UniProtKB. DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IGI:WormBase. DR GO; GO:0099140; P:presynaptic actin cytoskeleton organization; IDA:SynGO. DR GO; GO:0097091; P:synaptic vesicle clustering; IDA:SynGO. DR CDD; cd11826; SH3_Abi; 1. DR Gene3D; 6.10.140.1620; -; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR028457; ABI. DR InterPro; IPR028455; ABI3_SH3. DR InterPro; IPR012849; Abl-interactor_HHR_dom. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR10460:SF0; ABELSON INTERACTING PROTEIN, ISOFORM D; 1. DR PANTHER; PTHR10460; ABL INTERACTOR FAMILY MEMBER; 1. DR Pfam; PF07815; Abi_HHR; 1. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:Q10929, KW ECO:0007829|PeptideAtlas:Q10929}; KW Reference proteome {ECO:0000313|Proteomes:UP000001940}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}. FT DOMAIN 412..469 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT REGION 152..184 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 204..309 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 340..378 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 164..184 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 216..231 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 247..262 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 280..297 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 469 AA; 51307 MW; FC66F475CACF2787 CRC64; MSVNDLQELI ERRIPDNRAQ LETSHANLQQ VAAYCEDNYI QSNNKSAALE ESKKFAIQAL ASVAYQINKM VTDLHDMLAL QTDKVNSLTN QVQYVSQVVD VHKEKLARRE IGSLTTNKTL FKQPKIIAPA IPDEKQRYQR TPIDFSVLDG IGHGVRTSDP PRAAPISRAT SSISGSSPSQ FHNESPAYGV YAGERTATLG RTMRPYAPSI APSDYRLPQV TPQSESRIGR QMSHGSEFGD HMSGGGGSGS QHGSSDYNSI YQPDRYGTIR AGGRTTVDGS FSIPRLSSAQ SSAGGPESPT FPLPPPAMNY TGYVAPGSVV QQQQQQQMQQ QNYGTIRKST VNRHDLPPPP NSLLTGMSSR MPTQDDMDDL PPPPESVGGS SAYGVFAGRT ESYSSSQPPS LFDTSAGWMP NEYLEKVRVL YDYDAAKEDE LTLRENAIVY VLKKNDDDWY EGVLDGVTGL FPGNYVVPV //