GenomeNet

Database: UniProt
Entry: G1TER3_RABIT
LinkDB: G1TER3_RABIT
Original site: G1TER3_RABIT 
ID   G1TER3_RABIT            Unreviewed;       246 AA.
AC   G1TER3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=B-cell receptor-associated protein {ECO:0000256|RuleBase:RU367026};
DE            Short=BCR-associated protein {ECO:0000256|RuleBase:RU367026};
GN   Name=BCAP31 {ECO:0000313|Ensembl:ENSOCUP00000015397.2};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000015397.2, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000015397.2, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000015397.2}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000015397.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Plays a role in the export of secreted proteins in the ER.
CC       {ECO:0000256|RuleBase:RU367026}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367026}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU367026}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the BCAP29/BCAP31 family.
CC       {ECO:0000256|ARBA:ARBA00007956, ECO:0000256|RuleBase:RU367026}.
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   RefSeq; XP_008248542.1; XM_008250320.2.
DR   AlphaFoldDB; G1TER3; -.
DR   SMR; G1TER3; -.
DR   STRING; 9986.ENSOCUP00000015397; -.
DR   PaxDb; 9986-ENSOCUP00000015397; -.
DR   Ensembl; ENSOCUT00000017921.3; ENSOCUP00000015397.2; ENSOCUG00000017921.3.
DR   GeneID; 100356247; -.
DR   KEGG; ocu:100356247; -.
DR   CTD; 10134; -.
DR   eggNOG; KOG1962; Eukaryota.
DR   GeneTree; ENSGT00390000011863; -.
DR   HOGENOM; CLU_070975_1_0_1; -.
DR   InParanoid; G1TER3; -.
DR   OMA; AGREIWK; -.
DR   OrthoDB; 2882163at2759; -.
DR   TreeFam; TF315310; -.
DR   Proteomes; UP000001811; Unplaced.
DR   Bgee; ENSOCUG00000017921; Expressed in ovary and 16 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
DR   GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0042288; F:MHC class I protein binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IEA:Ensembl.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; IEA:Ensembl.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR   GO; GO:1904294; P:positive regulation of ERAD pathway; IEA:Ensembl.
DR   GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; IEA:Ensembl.
DR   GO; GO:1904154; P:positive regulation of retrograde protein transport, ER to cytosol; IEA:Ensembl.
DR   GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IEA:UniProtKB-UniRule.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; IEA:Ensembl.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   Gene3D; 1.20.5.110; -; 1.
DR   InterPro; IPR008417; BAP29/BAP31.
DR   InterPro; IPR040463; BAP29/BAP31_N.
DR   InterPro; IPR041672; Bap31/Bap29_C.
DR   PANTHER; PTHR12701:SF15; B-CELL RECEPTOR-ASSOCIATED PROTEIN 31; 1.
DR   PANTHER; PTHR12701; BCR-ASSOCIATED PROTEIN, BAP; 1.
DR   Pfam; PF05529; Bap31; 1.
DR   Pfam; PF18035; Bap31_Bap29_C; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU367026};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|RuleBase:RU367026};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367026};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU367026};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU367026};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU367026};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367026}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367026"
FT   TRANSMEM        40..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367026"
FT   TRANSMEM        103..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367026"
FT   DOMAIN          1..135
FT                   /note="BAP29/BAP31 transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF05529"
FT   DOMAIN          199..246
FT                   /note="Bap31/Bap29 cytoplasmic coiled-coil"
FT                   /evidence="ECO:0000259|Pfam:PF18035"
FT   COILED          133..236
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   246 AA;  28085 MW;  BB90AC92ACA0A083 CRC64;
     MSLQWTAVAT FLYAEVFAVL LLCIPFISPK RWQKIFKSRL VELVVTYGNT FFVVLISILV
     LLVIDAVREI RKYDDVTEKV NLQNNPGAME HFHMKLFRAQ RNLYIAGFSL LLSFLLRRLV
     TLISQQATLL ASNEAFKKQA ESASEAAKKY MEENDQLKKG AAVDRRKLDV GDTEVKLEEE
     NRSLKANLKK LKDDLASAKQ KLEKAENEAL AMRKQSEGLT KEYDRLLDEH AKLQASVDGT
     TDKKEE
//
DBGET integrated database retrieval system