S35B1_BOVIN
ID S35B1_BOVIN Reviewed; 322 AA.
AC Q8MII5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Solute carrier family 35 member B1;
DE AltName: Full=ATP/ADP exchanger ER {ECO:0000250|UniProtKB:P78383};
DE Short=AXER {ECO:0000250|UniProtKB:P78383};
DE AltName: Full=Endoplasmic reticulum ATP/ADP translocase {ECO:0000250|UniProtKB:P78383};
DE AltName: Full=UDP-galactose transporter-related protein 1 {ECO:0000250|UniProtKB:P78383};
DE Short=UGTrel1 {ECO:0000250|UniProtKB:P78383};
GN Name=SLC35B1; Synonyms=ERNST;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY.
RX PubMed=12770764; DOI=10.1016/s0300-9084(03)00046-4;
RA Martinez-Duncker I., Mollicone R., Codogno P., Oriol R.;
RT "The nucleotide-sugar transporter family: a phylogenetic approach.";
RL Biochimie 85:245-260(2003).
CC -!- FUNCTION: ATP:ADP antiporter that catalyzes the exchange of ATP and ADP
CC across the endoplasmic reticulum (ER) membrane. Imports ATP from the
CC cytosol to the ER lumen and exports ADP in the opposite direction (By
CC similarity). Regulates ER energy metabolism and protein biogenesis.
CC Appears to be part of a calcium-dependent ER to cytosol low energy
CC response axis, where calcium efflux from ER to the cytosol triggers ATP
CC import into the ER lumen to maintain sufficient ATP supply. Provides
CC ATP to ER chaperone HSPA5 that drives protein folding and trafficking
CC in the ER (By similarity). Can transport UTP or UDP in exchange for
CC ATP, but the physiological relevance of this process remains to be
CC established (By similarity). {ECO:0000250|UniProtKB:P78383}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P78383};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35001;
CC Evidence={ECO:0000250|UniProtKB:P78383};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P78383}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum localization
CC for type I membrane proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD33236.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ489254; CAD33236.1; ALT_INIT; mRNA.
DR RefSeq; NP_851934.1; NM_181338.2.
DR AlphaFoldDB; Q8MII5; -.
DR SMR; Q8MII5; -.
DR STRING; 9913.ENSBTAP00000009034; -.
DR PaxDb; Q8MII5; -.
DR PRIDE; Q8MII5; -.
DR GeneID; 353217; -.
DR KEGG; bta:353217; -.
DR CTD; 10237; -.
DR eggNOG; KOG1580; Eukaryota.
DR HOGENOM; CLU_036019_1_1_1; -.
DR InParanoid; Q8MII5; -.
DR OrthoDB; 1220063at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005459; F:UDP-galactose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005460; F:UDP-glucose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0072334; P:UDP-galactose transmembrane transport; IBA:GO_Central.
DR InterPro; IPR013657; UAA.
DR PANTHER; PTHR10778; PTHR10778; 1.
DR Pfam; PF08449; UAA; 1.
PE 2: Evidence at transcript level;
KW Antiport; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..322
FT /note="Solute carrier family 35 member B1"
FT /id="PRO_0000213365"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 318..322
FT /note="Di-lysine motif"
SQ SEQUENCE 322 AA; 35703 MW; FCD8E266334C81FD CRC64;
MAASSSLVPD RLRLPLCFLG VFVCYFYYGI LQEKITRGKY GEGAKQETFT FALTLVFIQC
VVNAVFAKIL IQFFDTARVD RTRSWLYAAC SVSYLGAMVS SNSALQFVNY PTQVLGKSCK
PIPVMLLGVT LLKKKYPMAK YLCVLLIVAG VALFMYKPKK VVGIEEHTIG YGELLLLLSL
TLDGLTGVSQ DHMRAHYQTG SNHMMLNINL WSTLLLGAGI LFTGELWEFL SFAERYPTIV
YNILLFGLTS ALGQSFIFMT VVYFGPLTCS IITTTRKFFT ILASVILFAN PISPMQWVGT
VLVFLGLGLD AKFGKGAKKT SH
