ID   CED2_CAEBR              Reviewed;         277 AA.
AC   A8XI74;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Cell death abnormality protein 2 {ECO:0000250|UniProtKB:Q9NHC3};
GN   Name=ced-2 {ECO:0000312|EMBL:CAP32348.1}; ORFNames=CBG13568;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1] {ECO:0000312|EMBL:CAP32348.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16 {ECO:0000312|EMBL:CAP32348.1};
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Required for cell migration and engulfment of cell corpses
CC       but not for programmed cell death/apoptosis. Also has a role in the
CC       migration of the 2 gonadal distal tip cells (DTCs) (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NHC3}.
CC   -!- SUBUNIT: Interacts with ced-5 (via C-terminus which contains a
CC       candidate SH3-binding, proline-rich region). Forms a ternary complex
CC       with ced-5 and ced-12. Interacts (via SH-2 domain) with src-1 (when
CC       activated and phosphorylated at 'Tyr-416').
CC       {ECO:0000250|UniProtKB:Q9NHC3}.
CC   -!- SIMILARITY: Belongs to the CRK family. {ECO:0000255}.
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DR   EMBL; HE600980; CAP32348.1; -; Genomic_DNA.
DR   RefSeq; XP_002635024.1; XM_002634978.1.
DR   AlphaFoldDB; A8XI74; -.
DR   SMR; A8XI74; -.
DR   STRING; 6238.CBG13568; -.
DR   EnsemblMetazoa; CBG13568.1; CBG13568.1; WBGene00034318.
DR   GeneID; 8577019; -.
DR   KEGG; cbr:CBG_13568; -.
DR   CTD; 8577019; -.
DR   WormBase; CBG13568; CBP03281; WBGene00034318; Cbr-ced-2.
DR   eggNOG; KOG4792; Eukaryota.
DR   HOGENOM; CLU_060542_0_0_1; -.
DR   InParanoid; A8XI74; -.
DR   OMA; DQMFPDL; -.
DR   OrthoDB; 1414461at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR   GO; GO:0035591; F:signaling adaptor activity; IBA:GO_Central.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR   GO; GO:1902742; P:apoptotic process involved in development; IEA:EnsemblMetazoa.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0043652; P:engulfment of apoptotic cell; ISS:UniProtKB.
DR   GO; GO:1903356; P:positive regulation of distal tip cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IEA:EnsemblMetazoa.
DR   GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF14604; SH3_9; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF50044; SSF50044; 2.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 2.
PE   3: Inferred from homology;
KW   Phagocytosis; Reference proteome; Repeat; SH2 domain; SH3 domain.
FT   CHAIN           1..277
FT                   /note="Cell death abnormality protein 2"
FT                   /id="PRO_0000379933"
FT   DOMAIN          14..112
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          113..173
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          214..275
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          179..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   277 AA;  30797 MW;  6FEBCDB7B563AB82 CRC64;
     MNMNGFDPFE WRSFYFPGMS REDAHKLLGE PRVSIGTFLM RDSSQPGEYS LSVREADEGN
     TVCHYLIVRD VKEDGTAGVK IAEQSFPDIP ALLNHFKMRV LTEASLLSAY KKPIIEVVVG
     TFKFTGERET DLPFEQGERL EILSKTNNDW WEARNALGTT GLVPANYVQV QSGEFANERI
     SKGTSQSSIG SSGNGAERFS STSTSSENAE AHPTLPTTAK VTFDRVPNAY DPTQLRVKKG
     QTVRVLEKMS NGMYRAELDG QIGSVPFTYI RFNTANQ