CED12_CAEBR
ID CED12_CAEBR Reviewed; 740 AA.
AC A8XEZ1;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 4.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Cell death abnormality protein 12 {ECO:0000250|UniProtKB:Q8STE5};
GN Name=ced-12 {ECO:0000312|WormBase:CBG12216};
GN ORFNames=CBG12216 {ECO:0000312|WormBase:CBG12216};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
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: Involved in apoptosis and necrosis. Required for the cell
CC corpse engulfment process. Has roles in the formation of actin halos
CC and distal tip cell migration. Plays no role in amphid axon outgrowth
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with psr-1. Forms a ternary complex with ced-2 and
CC ced-5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Punctate
CC localization. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAP31213.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAP31213.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; HE600958; CAP31213.2; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A8XEZ1; -.
DR SMR; A8XEZ1; -.
DR STRING; 6238.CBG12216; -.
DR EnsemblMetazoa; CBG12216.1; CBG12216.1; WBGene00033199.
DR WormBase; CBG12216; CBP37981; WBGene00033199; Cbr-ced-12.
DR eggNOG; KOG2999; Eukaryota.
DR HOGENOM; CLU_339579_0_0_1; -.
DR InParanoid; A8XEZ1; -.
DR OrthoDB; 234725at2759; -.
DR Proteomes; UP000008549; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR GO; GO:0070064; F:proline-rich region binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0060097; P:cytoskeletal rearrangement involved in phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0043652; P:engulfment of apoptotic cell; ISS:UniProtKB.
DR GO; GO:0035262; P:gonad morphogenesis; ISS:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024574; ELMO_ARM.
DR InterPro; IPR006816; ELMO_dom.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF11841; DUF3361; 1.
DR Pfam; PF16457; PH_12; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51335; ELMO; 1.
PE 3: Inferred from homology;
KW Apoptosis; Cytoplasm; Phagocytosis; Reference proteome; SH3-binding.
FT CHAIN 1..740
FT /note="Cell death abnormality protein 12"
FT /id="PRO_0000379435"
FT DOMAIN 348..494
FT /note="ELMO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00664"
FT REGION 555..690
FT /note="Required for punctate localization, cell corpse
FT engulfment and distal cell tip migration"
FT /evidence="ECO:0000250"
FT MOTIF 724..727
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
SQ SEQUENCE 740 AA; 83972 MW; D04A3036ED2719B8 CRC64;
MPSTSLPYTQ MAFHMPLKEL QPVDTSLPEH IIKGAVVIDK ELTTWNRRAV IPSTALHTVF
ITINRLEQKQ ADVVKMAARE MNLPEDNTYG LMADAPKRFI TNENIDQLGS GFILTLCASP
DNYVKRITEI LEDGKNIAQM ENAVKTLDEF SLDPALIEAF YRCSSLELLF DLVRDDRVSM
SYTLLSTCLR ALSSILELAV GDVTWKSVPR DVVVSIAALV TGKAKREEVN TLLAALAMIE
QLVIGDDTTR DWVLEEVPIE TLIRHVEKSD ERIALAALSL MNSMIRHCSD KDKRLELIES
LEVVPFRNAV HSSLLRDGSA RDPKALEQLV EVQRSLISAY DTSPASDSEI QKVLDIDSAN
ENSEEDVEIW RTKLAEHRCG RLATVAMVLF GEKSPQDLRM LISENTMRIE GGKWQLIPMW
MRCCDITAEL FGLLPGRDEL DRLISIIFST DSPFPAVFSC IVHLFHRTWR EMQAKGGEMD
KVASFVLEQL RHVLKRKEIH DVEEMSADLE TFSYKAMQEV RREEQLEKEN DQLHSEAVIS
LKAKLRPKIE ELVRINHLNY LKKGDVFRKP MKSKSLAKAA YWFWKLDASE KMLTITACDG
ERFVDDGHRD DIRQVWLKDV ADVTNNDEID RKASSSRFAS SPSTNMLRGV RVQLKPTNDL
KEGEVLMALT PDETQAGIWQ ESLAYLVGNT EMRSKTNAIV ERMLKMELRV RLLNVKLADP
ENEPDVPPIP DDLISFISSF