BAP31_PONAB
ID BAP31_PONAB Reviewed; 246 AA.
AC Q5R8H3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=B-cell receptor-associated protein 31;
DE Short=BCR-associated protein 31;
DE Short=Bap31;
GN Name=BCAP31;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as a chaperone protein. Is one of the most abundant
CC endoplasmic reticulum (ER) proteins. Plays a role in the export of
CC secreted proteins in the ER, the recognition of abnormally folded
CC protein and their targeting to the ER associated-degradation (ERAD) (By
CC similarity). Also serves as a cargo receptor for the export of
CC transmembrane proteins (By similarity). Plays a role in the assembly of
CC the mitochondrial membrane respiratory chain NADH dehydrogenase
CC (Complex I) by stimulating the translocation of NDUFS4 and NDUFB11 from
CC the cytosol to the mitochondria via interaction with TOMM40. In
CC response to ER stress, delocalizes from the ER-mitochondria contact
CC sites and binds BCL2. May be involved in CASP8-mediated apoptosis (By
CC similarity). {ECO:0000250|UniProtKB:P51572,
CC ECO:0000250|UniProtKB:Q61335}.
CC -!- SUBUNIT: Homodimer and heterodimer with BCAP29 (By similarity). Binds
CC CASP8 (isoform 9) as a complex containing BCAP31, BCAP29, BCL2 and/or
CC BCL2L1 (By similarity). Forms a complex (via C-terminus) with TOMM40
CC which mediates the translocation of components of the mitochondrial
CC membrane respiratory chain NADH dehydrogenase (Complex I) from the
CC cytosol to the mitochondria; within the complex BCAP31 interacts
CC directly with unprocessed and processed NDUFS4 and NDUFB11. Interacts
CC with VDAC1 (By similarity). Interacts with VAMP3, VAMP1 and membrane
CC IgD immunoglobulins (By similarity). Interacts with HACD2 (By
CC similarity). {ECO:0000250|UniProtKB:P51572,
CC ECO:0000250|UniProtKB:Q61335}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P51572}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000250|UniProtKB:P51572}; Multi-pass membrane protein
CC {ECO:0000255}. Note=May shuttle between the ER and the intermediate
CC compartment/cis-Golgi complex. Associates with the mitochondria-
CC associated endoplasmic reticulum membrane via interaction with TOMM40.
CC {ECO:0000250|UniProtKB:P51572}.
CC -!- PTM: Cleaved by CASP8 and other caspases. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR859779; CAH91937.1; -; mRNA.
DR RefSeq; NP_001126123.1; NM_001132651.1.
DR AlphaFoldDB; Q5R8H3; -.
DR SMR; Q5R8H3; -.
DR Ensembl; ENSPPYT00000024311; ENSPPYP00000023334; ENSPPYG00000020850.
DR GeneID; 100173079; -.
DR KEGG; pon:100173079; -.
DR CTD; 10134; -.
DR GeneTree; ENSGT00390000011863; -.
DR InParanoid; Q5R8H3; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR InterPro; IPR008417; BAP29/BAP31.
DR InterPro; IPR040463; BAP29/BAP31_N.
DR InterPro; IPR041672; Bap31/Bap29_C.
DR PANTHER; PTHR12701; PTHR12701; 1.
DR Pfam; PF05529; Bap31; 1.
DR Pfam; PF18035; Bap31_Bap29_C; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Coiled coil; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..246
FT /note="B-cell receptor-associated protein 31"
FT /id="PRO_0000142893"
FT TOPO_DOM 1..6
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..102
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 165..237
FT /evidence="ECO:0000250"
FT MOTIF 243..246
FT /note="Di-lysine motif"
FT SITE 164..165
FT /note="Cleavage; by caspase-8"
FT /evidence="ECO:0000255"
FT SITE 238..239
FT /note="Cleavage; by caspase-8"
FT /evidence="ECO:0000255"
SQ SEQUENCE 246 AA; 27947 MW; 1333B1ACEEF96D54 CRC64;
MSLQWTAVAT FLYAEVFVVL LLCIPFISPK RWQKIFKSRL VELVVSYGNT FFVVLIVILV
LLVIDAVREI RKYDDVTEKV NLQNNPGAME HFHMKLFRAQ RNLYIAGFSL LLSFLLRRLV
TLISQQATLL ASNEAFKKQA ESASEAAKKY MEENDQLKKG AAVDGGKLDV GNAEVKLEEE
NRSLKADLQK LKDELASTKQ KLEKAENQVL AMRKQSEGLT KEYDRLLEEH AKLQAAVDGP
TDKKEE
