S35B1_MOUSE
ID S35B1_MOUSE Reviewed; 322 AA.
AC P97858; Q8CF70;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
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=Ugalt2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9010752; DOI=10.1093/oxfordjournals.jbchem.a021523;
RA Ishida N., Miura N., Yoshioka S., Kawakita M.;
RT "Molecular cloning and characterization of a novel isoform of the human
RT UDP-galactose transporter, and of related complementary DNAs belonging to
RT the nucleotide-sugar transporter gene family.";
RL J. Biochem. 120:1074-1078(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P97858-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97858-2; Sequence=VSP_016192;
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}.
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DR EMBL; D87990; BAA13526.1; -; mRNA.
DR EMBL; AK002961; BAC25013.1; -; mRNA.
DR EMBL; AL662875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002029; AAH02029.1; -; mRNA.
DR CCDS; CCDS25277.1; -. [P97858-1]
DR PIR; JC5025; JC5025.
DR RefSeq; NP_058032.1; NM_016752.1. [P97858-1]
DR RefSeq; XP_006532048.1; XM_006531985.1.
DR AlphaFoldDB; P97858; -.
DR SMR; P97858; -.
DR BioGRID; 225355; 1.
DR STRING; 10090.ENSMUSP00000021243; -.
DR SwissPalm; P97858; -.
DR EPD; P97858; -.
DR jPOST; P97858; -.
DR MaxQB; P97858; -.
DR PaxDb; P97858; -.
DR PeptideAtlas; P97858; -.
DR PRIDE; P97858; -.
DR ProteomicsDB; 260772; -. [P97858-1]
DR ProteomicsDB; 260773; -. [P97858-2]
DR Antibodypedia; 17968; 70 antibodies from 19 providers.
DR DNASU; 110172; -.
DR Ensembl; ENSMUST00000021243; ENSMUSP00000021243; ENSMUSG00000020873. [P97858-1]
DR GeneID; 110172; -.
DR KEGG; mmu:110172; -.
DR UCSC; uc007lah.1; mouse. [P97858-1]
DR CTD; 10237; -.
DR MGI; MGI:1343133; Slc35b1.
DR VEuPathDB; HostDB:ENSMUSG00000020873; -.
DR eggNOG; KOG1580; Eukaryota.
DR GeneTree; ENSGT00940000157900; -.
DR HOGENOM; CLU_036019_1_0_1; -.
DR InParanoid; P97858; -.
DR OMA; VCSNMAL; -.
DR OrthoDB; 1220063at2759; -.
DR PhylomeDB; P97858; -.
DR TreeFam; TF105967; -.
DR BioGRID-ORCS; 110172; 24 hits in 72 CRISPR screens.
DR ChiTaRS; Slc35b1; mouse.
DR PRO; PR:P97858; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P97858; protein.
DR Bgee; ENSMUSG00000020873; Expressed in small intestine Peyer's patch and 283 other tissues.
DR ExpressionAtlas; P97858; baseline and differential.
DR Genevisible; P97858; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
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:0005471; F:ATP:ADP antiporter activity; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Antiport; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..322
FT /note="Solute carrier family 35 member B1"
FT /id="PRO_0000213367"
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"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_016192"
SQ SEQUENCE 322 AA; 35883 MW; 3251E99195AAA4A4 CRC64;
MAASRSLVPD RLRLPLCFLG VFVCYFYYGI LQEKITRGKY GEGPKQETFT FALTLVFIQC
VINAMFAKIL IQFFDTARVD RTRTWLYAAC SVSYVGAMVS SNSALQFVNY PTQVLGKSCK
PIPVMLLGVT LLKKKYPLAK YLCVLLIVAG VALFMYKPKK VVGIEEHTVG FGELLLLMSL
TLDGLTGVSQ DHMRAHYQTG SNHMMLNINL WSTFLLGAGI LFTGELWEFL SFAERYPTII
YNILLFGLTS ALGQSFIFMT VVYFGPLTCS IITTTRKFFT ILASVILFAN PISSMQWVGT
VLVFLGLGLD AKFGKGTKKT SH
