ID A0A3B3U0H0_9TELE Unreviewed; 621 AA.
AC A0A3B3U0H0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Baculoviral IAP repeat containing 2 {ECO:0000313|Ensembl:ENSPLAP00000006172.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000006172.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000006172.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000256|ARBA:ARBA00006672}.
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DR AlphaFoldDB; A0A3B3U0H0; -.
DR Ensembl; ENSPLAT00000006712.1; ENSPLAP00000006172.1; ENSPLAG00000008290.1.
DR GeneTree; ENSGT00940000154175; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10044:SF79; BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 2; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 457..547
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT DOMAIN 574..609
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 156..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 69743 MW; 4FA421FD673D9967 CRC64;
METLVQLKNN QFLMGLCRNG PPPDLQYDNS SELYRISTFA RFPASPVTER SLARAGWFYT
GMGDRVQCFR CNVTAEGWQA GDCPTEKHRQ LSPSCSFIQS LPSTTNLLSS SHSAFSPLRI
AQLPGPGPAA PNPSVSQVED PVGFLNTAFS ALPPSSPLSS RGVEDMSHQR PTCHNPSMRR
EQDRLDSFHS WTLSIITPTE LAKAGFYYLG QGDRVACFSC GGQLNNWEPG DRAVSEHQRH
YPNCRFVRGD RADNVSLSAP ALTSVSNPSM QQSDERLLTF VNWPSRIPVR PEQLAKAGFY
YVGRNDDVKC FCCDGGLRCW ESGDDPWVEH AKWFPRCEYL LQEKGQDFVH QIQARFPRLF
EQLLTTGDTS SREFVDPPVV HLGPGEERSE DAVMMNTPVI KSALEMGFDR SLVKQTVQSK
ILTSGENYRT VQELVSDLLS AEDQKREEER EMLAEAMASD GFTFVKRHQA ALAQRLKSVE
PVLEHLREQN VLSAEDYSGL LAQTTAQQQT ARLIELVLNK GNAAAEVFRN WIQKNDVHLL
RDLMGMTSPQ DTNTDLRNLP MEEQLRRLQE ERTCKVCMDK EVNIVFIPCG HLVVCKECAP
SLRKCPICRG LVKGTVRTFL S
//
