ID A0A2Y9K5Z9_ENHLU Unreviewed; 604 AA.
AC A0A2Y9K5Z9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Baculoviral IAP repeat-containing protein 3-like {ECO:0000313|RefSeq:XP_022368533.1, ECO:0000313|RefSeq:XP_022368534.1};
GN Name=LOC111153673 {ECO:0000313|RefSeq:XP_022368533.1,
GN ECO:0000313|RefSeq:XP_022368534.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022368533.1};
RN [1] {ECO:0000313|RefSeq:XP_022368533.1, ECO:0000313|RefSeq:XP_022368534.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022368533.1,
RC ECO:0000313|RefSeq:XP_022368534.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000256|ARBA:ARBA00006672}.
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DR RefSeq; XP_022368533.1; XM_022512825.1.
DR RefSeq; XP_022368534.1; XM_022512826.1.
DR STRING; 391180.A0A2Y9K5Z9; -.
DR KEGG; elk:111153673; -.
DR OrthoDB; 383715at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:UniProt.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd00022; BIR; 3.
DR CDD; cd16713; RING-HC_BIRC2_3_7; 1.
DR CDD; cd14394; UBA_BIRC2_3; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR048875; BIRC2-3-like_UBA.
DR InterPro; IPR041933; BIRC2/BIRC3_UBA.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR10044:SF178; BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR10044; INHIBITOR OF APOPTOSIS; 1.
DR Pfam; PF00653; BIR; 3.
DR Pfam; PF21290; BIRC2-3-like_UBA; 1.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00238; BIR; 3.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR SUPFAM; SSF57924; Inhibitor of apoptosis (IAP) repeat; 3.
DR PROSITE; PS01282; BIR_REPEAT_1; 1.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 439..529
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT DOMAIN 557..592
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 102..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..440
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 107..122
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 604 AA; 67500 MW; F5311F34C26AD80D CRC64;
MDLVQESLCL SGLLKSAPAL ELRYDHSCEL YRMSTFSTFP AGVPVSERSL ARAGFYYTGI
NDKVRCFCCG LMLDNWKLGD RPVEKHRKLY PSCAFVRSLS TASEPGARCP PPQPPPAASS
TRPLPPSLET TGFFSGSYAS FPSSPVNFRE NREFAPRRPS PCEGALKTAE DRLLTFQTWP
LTSPPAQDLA RAGFYYVGPG DRVACFACGG KLSNWEPSDS ALSEHLRHFP DCPFVDQQLQ
DALQSTVSNA SMQAHAARLQ TFWSWPSRVP VRPEQLAAAG FYYTGHSDDV KCFCCDGGLR
CWESGDDPWV EHAKWFPRCE YLIRIKGQEF ISRIQASYPH LLEQLLSTSD NTEDENAESP
IVHFGPGEIR SEDAVMMNTP VVTAALEMGF SRSLVRQTVQ SKILSTGENY RTVNEIVSDL
LHAEDELREE EKERAAENRD SDDAALIRKN QTVLLQCLTQ VPPILDSLLT AGVISEHERG
VLEQRARTPL QARMLLDTVL GRGSSAVTVF KNSLQEVDPV LYKRIFVQQD LKYIPPENLS
DLPVEEQLRR LQEERTCKVC MDKEVSVVFI PCGHLVVCQE CAPSLRRCPI CRGTVKGTVR
TFLS
//
