ID   TRIAB_XENLA             Reviewed;          78 AA.
AC   Q6DD38;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=TP53-regulated inhibitor of apoptosis 1-B;
DE   AltName: Full=p53-inducible cell-survival factor-B;
DE            Short=p53csv-B;
GN   Name=triap1-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000312|EMBL:AAH77791.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary {ECO:0000312|EMBL:AAH77791.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the modulation of the mitochondrial apoptotic
CC       pathway by ensuring the accumulation of cardiolipin (CL) in
CC       mitochondrial membranes. The triap1:prelid1 complex probably functions
CC       as a phosphatidic acid (PA) transporter across the mitochondrion
CC       intermembrane space to provide PA for cardiolipin CL synthesis in the
CC       inner membrane. Likewise, the triap1:prelid3a complex mediates the
CC       transfer of phosphatidic acid (PA) between liposomes (in vitro) and
CC       probably functions as a PA transporter across the mitochondrion
CC       intermembrane space (in vivo). Mediates cell survival by inhibiting
CC       activation of caspase-9 which prevents induction of apoptosis (By
CC       similarity). Required for pronephros development; probably involved at
CC       an early stage in the formation of pronephric components derived from
CC       the somatic layer (By similarity). {ECO:0000250|UniProtKB:A9ULB4,
CC       ECO:0000250|UniProtKB:O43715}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphate(in) = a 1,2-diacyl-sn-
CC         glycero-3-phosphate(out); Xref=Rhea:RHEA:36435, ChEBI:CHEBI:58608;
CC         Evidence={ECO:0000250|UniProtKB:O43715};
CC   -!- SUBUNIT: Monomer. Forms a complex with prelid1 in the mitochondrion
CC       intermembrane space. Interacts with prelid3a.
CC       {ECO:0000250|UniProtKB:O43715}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O43715}.
CC       Mitochondrion intermembrane space {ECO:0000250|UniProtKB:O43715}.
CC   -!- SIMILARITY: Belongs to the TRIAP1/MDM35 family. {ECO:0000255}.
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DR   EMBL; BC077791; AAH77791.1; -; mRNA.
DR   RefSeq; NP_001086934.1; NM_001093465.1.
DR   AlphaFoldDB; Q6DD38; -.
DR   SMR; Q6DD38; -.
DR   DNASU; 446769; -.
DR   GeneID; 446769; -.
DR   KEGG; xla:446769; -.
DR   CTD; 446769; -.
DR   Xenbase; XB-GENE-6255350; triap1.L.
DR   OrthoDB; 1552088at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 446769; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0015914; P:phospholipid transport; ISS:UniProtKB.
DR   GO; GO:0048793; P:pronephros development; ISS:UniProtKB.
DR   InterPro; IPR007918; MDM35_apoptosis.
DR   PANTHER; PTHR46403; PTHR46403; 1.
DR   Pfam; PF05254; UPF0203; 1.
DR   PROSITE; PS51808; CHCH; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Coiled coil; Developmental protein; Disulfide bond;
KW   Lipid transport; Mitochondrion; Reference proteome; Transport.
FT   CHAIN           1..78
FT                   /note="TP53-regulated inhibitor of apoptosis 1-B"
FT                   /id="PRO_0000391695"
FT   DOMAIN          5..55
FT                   /note="CHCH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   COILED          1..52
FT                   /evidence="ECO:0000250|UniProtKB:O43715"
FT   MOTIF           8..18
FT                   /note="Cx9C motif 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   MOTIF           37..47
FT                   /note="Cx9C motif 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   SITE            27
FT                   /note="Important for interaction with prelid3a"
FT                   /evidence="ECO:0000250|UniProtKB:O43715"
FT   SITE            41
FT                   /note="Important for interaction with prelid3a"
FT                   /evidence="ECO:0000250|UniProtKB:O43715"
FT   DISULFID        8..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
FT   DISULFID        18..37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01150"
SQ   SEQUENCE   78 AA;  8882 MW;  275A4002B5C1EAAB CRC64;
     MNSVGEECTD MKREYDQCFN RWFAEKFLKG DGSGDPCTEL FRRYRECVQK AIKDKDIPVD
     GVDFMGPSKS KTEADGSS