ID   BAP29_PONAB             Reviewed;         241 AA.
AC   Q5R9U7;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=B-cell receptor-associated protein 29;
DE            Short=BCR-associated protein 29;
DE            Short=Bap29;
GN   Name=BCAP29;
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=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in anterograde transport of membrane proteins
CC       from the endoplasmic reticulum to the Golgi. May be involved in CASP8-
CC       mediated apoptosis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer and heterodimer with BCAP31. Binds CASP8 as a
CC       complex containing BCAP31, BCAP29, BCL2 and/or BCL2L1. Interacts with
CC       VAMP3, VAMP1 and membrane IgD immunoglobulins. May interact with ACTG1
CC       and non-muscle myosin II (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family. {ECO:0000305}.
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DR   EMBL; CR858657; CAH90870.1; -; mRNA.
DR   EMBL; CR859285; CAH91463.1; -; mRNA.
DR   RefSeq; NP_001125860.1; NM_001132388.1.
DR   AlphaFoldDB; Q5R9U7; -.
DR   SMR; Q5R9U7; -.
DR   STRING; 9601.ENSPPYP00000020066; -.
DR   Ensembl; ENSPPYT00000060394; ENSPPYP00000045651; ENSPPYG00000032287.
DR   GeneID; 100172790; -.
DR   KEGG; pon:100172790; -.
DR   CTD; 55973; -.
DR   eggNOG; KOG1962; Eukaryota.
DR   GeneTree; ENSGT00390000011863; -.
DR   HOGENOM; CLU_070975_1_0_1; -.
DR   InParanoid; Q5R9U7; -.
DR   OMA; KYSSKEH; -.
DR   OrthoDB; 1514108at2759; -.
DR   TreeFam; TF315310; -.
DR   Proteomes; UP000001595; Chromosome 7.
DR   GO; GO:0005789; C:endoplasmic reticulum 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..241
FT                   /note="B-cell receptor-associated protein 29"
FT                   /id="PRO_0000142890"
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..103
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          193..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          166..233
FT                   /evidence="ECO:0000250"
FT   MOTIF           238..241
FT                   /note="Di-lysine motif"
SQ   SEQUENCE   241 AA;  28319 MW;  825839B12A072274 CRC64;
     MTLQWAAVAT FLYAEIGLIL IFCLPFIPPQ RWQKIFSFNV WGKIATFWNK AFLTIIILLI
     VLFLDAVREV RKYSSVHTIE KSSTSRPDAY EHTQMKLFRS QRNLYISGFS LFFWLVLRRL
     VTLITQLAKE LSNKGVLKTQ AENTNKAAKK FMEENEKLKR ILKSHGKDEE CVLEAENKKL
     VEDQQKLKTE LRKTSDALSK AQNDVMEMKM QSERLSKEYD QLLKEHSELQ DRLERGNKKR
     L