ID S35B4_HUMAN Reviewed; 331 AA. AC Q969S0; A4D1P3; A6NNS4; Q53GQ7; Q8TCU7; Q96K33; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 167. DE RecName: Full=Nucleotide sugar transporter SLC35B4; DE AltName: Full=Solute carrier family 35 member B4; DE AltName: Full=UDP-xylose and UDP-N-acetylglucosamine transporter; DE AltName: Full=YEA4 homolog; GN Name=SLC35B4; Synonyms=YEA4; ORFNames=PSEC0055; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORT ACTIVITY RP (ISOFORM 1), AND CAUTION. RX PubMed=15911612; DOI=10.1074/jbc.m504783200; RA Ashikov A., Routier F., Fuhlrott J., Helmus Y., Wild M., Gerardy-Schahn R., RA Bakker H.; RT "The human solute carrier gene SLC35B4 encodes a bifunctional nucleotide RT sugar transporter with specificity for UDP-xylose and UDP-N- RT acetylglucosamine."; RL J. Biol. Chem. 280:27230-27235(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Liver; RA Moriya Y., Ito K., Aburatani H., Suzuki H., Sugiyama Y.; RT "Molecular cloning of full-length cDNA similar to Yeast Yea4p from human RT liver cDNA library."; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Kobayashi T., Burchell B.; RT "Molecular cloning and characterisation of human yea4p."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 41-331 (ISOFORM 3). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Teratocarcinoma; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; 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 [11] RP SUBCELLULAR LOCATION, MOTIF, MUTAGENESIS OF LYS-329 AND LYS-330, AND RP CAUTION. RX PubMed=30458018; DOI=10.1371/journal.pone.0207521; RA Bazan B., Wiktor M., Maszczak-Seneczko D., Olczak T., Kaczmarek B., RA Olczak M.; RT "Lysine at position 329 within a C-terminal dilysine motif is crucial for RT the ER localization of human SLC35B4."; RL PLoS ONE 13:e0207521-e0207521(2018). RN [12] RP FUNCTION (ISOFORMS 1 AND 2), AND TRANSPORT ACTIVITY (ISOFORMS 1 AND 2). RX PubMed=16965264; DOI=10.1042/bj20060429; RA Kobayashi T., Sleeman J.E., Coughtrie M.W., Burchell B.; RT "Molecular and functional characterization of microsomal UDP-glucuronic RT acid uptake by members of the nucleotide sugar transporter (NST) family."; RL Biochem. J. 400:281-289(2006). CC -!- FUNCTION: Antiporter that transports nucleotide sugars across the CC endoplasmic reticulum (ER) membrane in exchange for another nucleotide CC sugar. May couple UDP-alpha-D-glucuronate (UDP-GlcA) or UDP-alpha-D- CC xylose (UDP-Xyl) efflux to UDP-alpha-D-glucuronate (UDP-GlcA) influx CC into the ER lumen, which in turn stimulates glucuronidation and CC excretion of endobiotics and xenobiotics. {ECO:0000269|PubMed:16965264, CC ECO:0000305|PubMed:15911612}. CC -!- FUNCTION: [Isoform 1]: Has UDP-GlcA:UDP-GlcNAc antiporter activity. CC {ECO:0000269|PubMed:16965264}. CC -!- FUNCTION: [Isoform 2]: Has UDP-GlcA:UDP-GlcNAc antiporter activity. CC {ECO:0000269|PubMed:16965264}. CC -!- CATALYTIC ACTIVITY: [Isoform 1]: CC Reaction=UDP-alpha-D-glucuronate(out) + UDP-N-acetyl-alpha-D- CC glucosamine(in) = UDP-alpha-D-glucuronate(in) + UDP-N-acetyl-alpha-D- CC glucosamine(out); Xref=Rhea:RHEA:73703, ChEBI:CHEBI:57705, CC ChEBI:CHEBI:58052; Evidence={ECO:0000269|PubMed:16965264, CC ECO:0000305|PubMed:15911612}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73704; CC Evidence={ECO:0000305|PubMed:15911612, ECO:0000305|PubMed:16965264}; CC -!- CATALYTIC ACTIVITY: [Isoform 1]: CC Reaction=UDP-alpha-D-glucuronate(out) + UDP-alpha-D-xylose(in) = UDP- CC alpha-D-glucuronate(in) + UDP-alpha-D-xylose(out); CC Xref=Rhea:RHEA:74831, ChEBI:CHEBI:57632, ChEBI:CHEBI:58052; CC Evidence={ECO:0000305|PubMed:15911612}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74832; CC Evidence={ECO:0000305|PubMed:15911612}; CC -!- CATALYTIC ACTIVITY: [Isoform 2]: CC Reaction=UDP-alpha-D-glucuronate(out) + UDP-N-acetyl-alpha-D- CC glucosamine(in) = UDP-alpha-D-glucuronate(in) + UDP-N-acetyl-alpha-D- CC glucosamine(out); Xref=Rhea:RHEA:73703, ChEBI:CHEBI:57705, CC ChEBI:CHEBI:58052; Evidence={ECO:0000269|PubMed:16965264}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73704; CC Evidence={ECO:0000305|PubMed:16965264}; CC -!- INTERACTION: CC Q969S0; Q13520: AQP6; NbExp=3; IntAct=EBI-10281213, EBI-13059134; CC Q969S0; P11912: CD79A; NbExp=3; IntAct=EBI-10281213, EBI-7797864; CC Q969S0; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-10281213, EBI-1045797; CC Q969S0; O00501: CLDN5; NbExp=3; IntAct=EBI-10281213, EBI-18400628; CC Q969S0; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-10281213, EBI-18013275; CC Q969S0; Q96BA8: CREB3L1; NbExp=8; IntAct=EBI-10281213, EBI-6942903; CC Q969S0; O00559: EBAG9; NbExp=3; IntAct=EBI-10281213, EBI-8787095; CC Q969S0; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-10281213, EBI-781551; CC Q969S0; P30040: ERP29; NbExp=3; IntAct=EBI-10281213, EBI-946830; CC Q969S0; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10281213, EBI-18304435; CC Q969S0; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-10281213, EBI-18938272; CC Q969S0; O15552: FFAR2; NbExp=3; IntAct=EBI-10281213, EBI-2833872; CC Q969S0; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-10281213, EBI-13345167; CC Q969S0; Q8TED1: GPX8; NbExp=3; IntAct=EBI-10281213, EBI-11721746; CC Q969S0; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-10281213, EBI-18053395; CC Q969S0; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-10281213, EBI-749265; CC Q969S0; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-10281213, EBI-2820517; CC Q969S0; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-10281213, EBI-6163737; CC Q969S0; P15941-11: MUC1; NbExp=3; IntAct=EBI-10281213, EBI-17263240; CC Q969S0; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-10281213, EBI-716063; CC Q969S0; P15151: PVR; NbExp=3; IntAct=EBI-10281213, EBI-3919694; CC Q969S0; Q9NX52-3: RHBDL2; NbExp=3; IntAct=EBI-10281213, EBI-12908426; CC Q969S0; Q6ZMJ2-2: SCARA5; NbExp=3; IntAct=EBI-10281213, EBI-12823227; CC Q969S0; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-10281213, EBI-17595455; CC Q969S0; P27105: STOM; NbExp=3; IntAct=EBI-10281213, EBI-1211440; CC Q969S0; Q0VAB0: TBXA2R; NbExp=3; IntAct=EBI-10281213, EBI-18271435; CC Q969S0; Q8N3G9: TMEM130; NbExp=3; IntAct=EBI-10281213, EBI-19763514; CC Q969S0; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-10281213, EBI-10982110; CC Q969S0; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-10281213, EBI-18178701; CC Q969S0; O43914: TYROBP; NbExp=3; IntAct=EBI-10281213, EBI-2214794; CC Q969S0; Q9H7M9: VSIR; NbExp=3; IntAct=EBI-10281213, EBI-744988; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:30458018}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q969S0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q969S0-2; Sequence=VSP_016197, VSP_016198; CC Name=3; CC IsoId=Q969S0-3; Sequence=VSP_016199, VSP_016200; CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B CC subfamily. {ECO:0000305}. CC -!- CAUTION: It was initially reported to localize to the Golgi apparatus, CC but this was later found to be artifactual mislocalization due to C- CC terminal tagging interfering with the ER retention signal. CC {ECO:0000269|PubMed:15911612, ECO:0000269|PubMed:30458018}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB55325.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AJ971941; CAI98963.1; -; mRNA. DR EMBL; AB052892; BAB61040.1; -; mRNA. DR EMBL; AJ315497; CAC84567.1; -; mRNA. DR EMBL; AJ315498; CAC84568.1; -; mRNA. DR EMBL; AK027603; BAB55225.1; -; mRNA. DR EMBL; AK027726; BAB55325.1; ALT_INIT; mRNA. DR EMBL; AK075368; BAC11573.1; -; mRNA. DR EMBL; AK222874; BAD96594.1; -; mRNA. DR EMBL; AC008154; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236950; EAL24071.1; -; Genomic_DNA. DR EMBL; CH471070; EAW83810.1; -; Genomic_DNA. DR EMBL; BC008413; AAH08413.1; -; mRNA. DR CCDS; CCDS34756.1; -. [Q969S0-1] DR RefSeq; NP_116215.1; NM_032826.4. [Q969S0-1] DR AlphaFoldDB; Q969S0; -. DR BioGRID; 124349; 39. DR IntAct; Q969S0; 34. DR MINT; Q969S0; -. DR STRING; 9606.ENSP00000367770; -. DR TCDB; 2.A.7.10.2; the drug/metabolite transporter (dmt) superfamily. DR iPTMnet; Q969S0; -. DR PhosphoSitePlus; Q969S0; -. DR SwissPalm; Q969S0; -. DR BioMuta; SLC35B4; -. DR DMDM; 74751727; -. DR MassIVE; Q969S0; -. DR MaxQB; Q969S0; -. DR PaxDb; 9606-ENSP00000367770; -. DR PeptideAtlas; Q969S0; -. DR ProteomicsDB; 75824; -. [Q969S0-1] DR ProteomicsDB; 75825; -. [Q969S0-2] DR ProteomicsDB; 75826; -. [Q969S0-3] DR Antibodypedia; 53731; 47 antibodies from 13 providers. DR DNASU; 84912; -. DR Ensembl; ENST00000378509.9; ENSP00000367770.4; ENSG00000205060.11. [Q969S0-1] DR Ensembl; ENST00000470969.2; ENSP00000485857.1; ENSG00000205060.11. [Q969S0-2] DR GeneID; 84912; -. DR KEGG; hsa:84912; -. DR MANE-Select; ENST00000378509.9; ENSP00000367770.4; NM_032826.5; NP_116215.1. DR UCSC; uc003vrn.4; human. [Q969S0-1] DR AGR; HGNC:20584; -. DR CTD; 84912; -. DR DisGeNET; 84912; -. DR GeneCards; SLC35B4; -. DR HGNC; HGNC:20584; SLC35B4. DR HPA; ENSG00000205060; Low tissue specificity. DR MIM; 610923; gene. DR neXtProt; NX_Q969S0; -. DR OpenTargets; ENSG00000205060; -. DR PharmGKB; PA134922110; -. DR VEuPathDB; HostDB:ENSG00000205060; -. DR eggNOG; KOG1583; Eukaryota. DR GeneTree; ENSGT00390000002915; -. DR HOGENOM; CLU_033007_1_0_1; -. DR InParanoid; Q969S0; -. DR OMA; NPFTGWH; -. DR OrthoDB; 128691at2759; -. DR PhylomeDB; Q969S0; -. DR TreeFam; TF312926; -. DR PathwayCommons; Q969S0; -. DR Reactome; R-HSA-727802; Transport of nucleotide sugars. DR SignaLink; Q969S0; -. DR BioGRID-ORCS; 84912; 7 hits in 1151 CRISPR screens. DR ChiTaRS; SLC35B4; human. DR GeneWiki; SLC35B4; -. DR GenomeRNAi; 84912; -. DR Pharos; Q969S0; Tbio. DR PRO; PR:Q969S0; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q969S0; Protein. DR Bgee; ENSG00000205060; Expressed in cerebellar vermis and 175 other cell types or tissues. DR ExpressionAtlas; Q969S0; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005462; F:UDP-N-acetylglucosamine transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0005464; F:UDP-xylose transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW. DR GO; GO:0006111; P:regulation of gluconeogenesis; IEA:Ensembl. DR GO; GO:1990569; P:UDP-N-acetylglucosamine transmembrane transport; IDA:UniProtKB. DR GO; GO:0015790; P:UDP-xylose transmembrane transport; IDA:UniProtKB. DR InterPro; IPR013657; SCL35B1-4/HUT1. DR PANTHER; PTHR10778; SOLUTE CARRIER FAMILY 35 MEMBER B; 1. DR PANTHER; PTHR10778:SF4; UDP-XYLOSE AND UDP-N-ACETYLGLUCOSAMINE TRANSPORTER; 1. DR Pfam; PF08449; UAA; 1. DR Genevisible; Q969S0; HS. PE 1: Evidence at protein level; KW Alternative splicing; Endoplasmic reticulum; Membrane; Reference proteome; KW Sugar transport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..331 FT /note="Nucleotide sugar transporter SLC35B4" FT /id="PRO_0000213385" FT TRANSMEM 4..24 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 30..50 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 59..79 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 92..112 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 117..137 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 153..173 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 201..221 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 229..249 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 251..267 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 268..288 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 291..311 FT /note="Helical" FT /evidence="ECO:0000255" FT MOTIF 326..331 FT /note="Mediates endoplasmic reticulum retention" FT /evidence="ECO:0000269|PubMed:30458018" FT VAR_SEQ 225..231 FT /note="ELYEIPV -> GEFGVRQ (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_016197" FT VAR_SEQ 232..331 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_016198" FT VAR_SEQ 251..253 FT /note="YVC -> TPT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016199" FT VAR_SEQ 254..331 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_016200" FT MUTAGEN 329 FT /note="K->A: Results in loss of ER retention signal and FT relocalization at the Golgi apparatus." FT /evidence="ECO:0000269|PubMed:30458018" FT MUTAGEN 330 FT /note="K->A: Results in loss of ER retention signal and FT relocalization at the Golgi apparatus." FT /evidence="ECO:0000269|PubMed:30458018" FT CONFLICT 21 FT /note="L -> P (in Ref. 6; BAD96594)" FT /evidence="ECO:0000305" FT CONFLICT 119 FT /note="F -> S (in Ref. 6; BAD96594)" FT /evidence="ECO:0000305" FT CONFLICT 179 FT /note="I -> M (in Ref. 6; BAD96594)" FT /evidence="ECO:0000305" FT CONFLICT 205 FT /note="P -> S (in Ref. 6; BAD96594)" FT /evidence="ECO:0000305" SQ SEQUENCE 331 AA; 37424 MW; 8C305DE30EFD4F82 CRC64; MRPALAVGLV FAGCCSNVIF LELLARKHPG CGNIVTFAQF LFIAVEGFLF EADLGRKPPA IPIRYYAIMV TMFFTVSVVN NYALNLNIAM PLHMIFRSGS LIANMILGII ILKKRYSIFK YTSIALVSVG IFICTFMSAK QVTSQSSLSE NDGFQAFVWW LLGIGALTFA LLMSARMGIF QETLYKRFGK HSKEALFYNH ALPLPGFVFL ASDIYDHAVL FNKSELYEIP VIGVTLPIMW FYLLMNIITQ YVCIRGVFIL TTECASLTVT LVVTLRKFVS LIFSILYFQN PFTLWHWLGT LFVFIGTLMY TEVWNNLGTT KSEPQKDSKK N //