(data stored in ACNUC8465 zone)

HOGENOM: CAEELIV_PE743

ID   CAEELIV_PE743                        STANDARD;      PRT;   191 AA.
AC   CAEELIV_PE743; Q03206; O44463; O44464;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Ras-related protein ced-10;AltName: Full=CErac1;AltName:
DE   Full=Cell death protein 10;AltName: Full=Cell-corpse engulfment protein
DE   ced-10;AltName: Full=Ras-related protein rac-1;Flags: Precursor;
DE   (CAEELIV.PE743).
GN   Name=ced-10; Synonyms=rac-1; ORFNames=C09G12.8;
OS   CAENORHABDITIS ELEGANS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Pseudocoelomata; Nematoda;
OC   Chromadorea; Rhabditida; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CAEELIV.PE743.
CC       Caenorhabditis elegans chromosome IV WS210  sequence 1..17493784
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:RAC1_CAEEL
CC   -!- FUNCTION: Required in engulfing to control the phagocytosis of
CC       apoptotic cell corpses. Involved in hypodermal cell fusion,
CC       together with pak-1 and cdc-42, leading to embryonic body
CC       elongation, which involves dramatic cytoskeletal reorganization.
CC       Ced-2 and ced-5 function to activate ced-10 in a GTPase signaling
CC       pathway that controls the polarized extension of cell surfaces.
CC   -!- SUBUNIT: The GTP-bound, but not the GDP-bound, form binds to the
CC       p21-activated kinase (pak-1).
CC   -!- SUBCELLULAR LOCATION: Cell surface. Cell membrane; Lipid-anchor
CC       (Potential). Note=Preferentially localized at the cell surface and
CC       especially condensed at cell boundaries.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=Q03206-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q03206-2; Sequence=VSP_005711;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Colocalizes with pak-1 to hypodermal cell
CC       boundaries during embryo elongation throughout the second phase of
CC       embryogenesis.
CC   -!- DEVELOPMENTAL STAGE: Most abundant at embryonic stage, its
CC       expression decreases dramatically during development.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC   -!- GENE_FAMILY: HOG000233974 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Caenorhabditis_elegans;C09G12.8;C09G12.8B;C09G12.8B.
DR   EMBL; AF038608; - ;
DR   EMBL; AF226867; - ;
DR   EMBL; L03711; - ;
DR   EMBL; L04287; - ;
DR   EMBL; X68492; - ;
DR   UniProtKB/Swiss-Prot; Q03206; O44463; O44464; -.
DR   EMBL; L03711; AAA28140.1; -; mRNA.
DR   EMBL; L04287; AAA28141.1; -; mRNA.
DR   EMBL; X68492; CAA48506.1; -; mRNA.
DR   EMBL; AF226867; AAF33846.1; -; mRNA.
DR   EMBL; AF038608; AAC25821.1; -; Genomic_DNA.
DR   EMBL; AF038608; AAC25820.1; -; Genomic_DNA.
DR   PIR; A45324; A45324.
DR   PIR; G88650; G88650.
DR   RefSeq; NP_500362.3; NM_067961.3.
DR   RefSeq; NP_500363.1; NM_067962.4.
DR   UniGene; Cel.19354; -.
DR   ProteinModelPortal; Q03206; -.
DR   SMR; Q03206; 1-177.
DR   IntAct; Q03206; 1.
DR   STRING; Q03206; -.
DR   PRIDE; Q03206; -.
DR   EnsemblMetazoa; C09G12.8b.1; C09G12.8b.1; C09G12.8.
DR   EnsemblMetazoa; C09G12.8b.2; C09G12.8b.2; C09G12.8.
DR   GeneID; 177111; -.
DR   KEGG; cel:C09G12.8; -.
DR   NMPDR; fig|6239.3.peg.12868; -.
DR   UCSC; C09G12.8b; c. elegans.
DR   CTD; 177111; -.
DR   WormBase; C09G12.8a; CE16832; WBGene00000424; ced-10.
DR   WormBase; C09G12.8b; CE16833; WBGene00000424; ced-10.
DR   eggNOG; meNOG06607; -.
DR   GeneTree; EMGT00050000000001; -.
DR   InParanoid; Q03206; -.
DR   OMA; PQTVGDT; -.
DR   PhylomeDB; Q03206; -.
DR   Reactome; REACT_29862; Axon guidance.
DR   NextBio; 895384; -.
DR   ArrayExpress; Q03206; -.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:WormBase.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005626; C:insoluble fraction; IDA:WormBase.
DR   GO; GO:0016021; C:integral to membrane; IDA:UniProtKB.
DR   GO; GO:0009898; C:internal side of plasma membrane; IDA:WormBase.
DR   GO; GO:0005625; C:soluble fraction; IDA:WormBase.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0048846; P:axon extension involved in axon guidance; IGI:WormBase.
DR   GO; GO:0031103; P:axon regeneration; IMP:WormBase.
DR   GO; GO:0010171; P:body morphogenesis; IGI:WormBase.
DR   GO; GO:0033563; P:dorsal/ventral axon guidance; IGI:WormBase.
DR   GO; GO:0043652; P:engulfment of apoptotic cell; IMP:WormBase.
DR   GO; GO:0040035; P:hermaphrodite genitalia development; IMP:WormBase.
DR   GO; GO:0040039; P:inductive cell migration; IMP:WormBase.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IMP:WormBase.
DR   GO; GO:0008045; P:motor axon guidance; IGI:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0001764; P:neuron migration; IGI:WormBase.
DR   GO; GO:0040026; P:positive regulation of vulval development; IMP:WormBase.
DR   GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR   GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:UniProtKB.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   InterPro; IPR003578; Small_GTPase_Rho.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00174; RHO; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
DR   HOGENOMDNA; CAEELIV.PE743; -.
KW   C09G12.80110200367fold_1320000031; C09G12.8b412210.62fold_1320000031;
KW   AF038608; AF226867; L03711; L04287; X68492;
KW   Alternative splicing; Apoptosis; Cell membrane; Complete proteome;
KW   Developmental protein; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Phagocytosis; Prenylation;
KW   Reference proteome.
SQ   SEQUENCE   191 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGRP INLGLWDTAG
     QEDYDRLRPL SYPQTDVFLV CFALNNPASF ENVRAKWYPE VSHHCPNTPI ILVGTKADLR
     EDRDTVERLR ERRLQPVSQT QGYVMAKEIK AVKYLECSAL TQRGLKQVFD EAIRAVLTPP
     QRAKKSKCTV L
//

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