ID   S35A3_HUMAN             Reviewed;         325 AA.
AC   Q9Y2D2; A8K3F8; D3DT54; Q68CR2; Q9BSB7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 177.
DE   RecName: Full=UDP-N-acetylglucosamine transporter;
DE   AltName: Full=Golgi UDP-GlcNAc transporter;
DE   AltName: Full=Solute carrier family 35 member A3;
GN   Name=SLC35A3;
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, TRANSPORTER ACTIVITY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=10393322; DOI=10.1093/oxfordjournals.jbchem.a022437;
RA   Ishida N., Yoshioka S., Chiba Y., Takeuchi M., Kawakita M.;
RT   "Molecular cloning and functional expression of the human Golgi UDP-N-
RT   acetylglucosamine transporter.";
RL   J. Biochem. 126:68-77(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon carcinoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Placenta;
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   [7]
RP   INTERACTION WITH SLC35A2.
RX   PubMed=23089177; DOI=10.1016/j.febslet.2012.10.016;
RA   Maszczak-Seneczko D., Sosicka P., Majkowski M., Olczak T., Olczak M.;
RT   "UDP-N-acetylglucosamine transporter and UDP-galactose transporter form
RT   heterologous complexes in the Golgi membrane.";
RL   FEBS Lett. 586:4082-4087(2012).
RN   [8]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=23766508; DOI=10.1074/jbc.m113.460543;
RA   Maszczak-Seneczko D., Sosicka P., Olczak T., Jakimowicz P., Majkowski M.,
RA   Olczak M.;
RT   "UDP-N-acetylglucosamine transporter (SLC35A3) regulates biosynthesis of
RT   highly branched N-glycans and keratan sulfate.";
RL   J. Biol. Chem. 288:21850-21860(2013).
RN   [9]
RP   INTERACTION WITH SLC35A2, IDENTIFICATION IN A COMPLEX WITH SLC35A2 AND
RP   SLC35A4, AND SUBCELLULAR LOCATION.
RX   PubMed=28167211; DOI=10.1016/j.bbamcr.2017.02.002;
RA   Sosicka P., Maszczak-Seneczko D., Bazan B., Shauchuk Y., Kaczmarek B.,
RA   Olczak M.;
RT   "An insight into the orphan nucleotide sugar transporter SLC35A4.";
RL   Biochim. Biophys. Acta 1864:825-838(2017).
RN   [10]
RP   INVOLVEMENT IN AMRS.
RX   PubMed=24031089; DOI=10.1136/jmedgenet-2013-101753;
RA   Edvardson S., Ashikov A., Jalas C., Sturiale L., Shaag A., Fedick A.,
RA   Treff N.R., Garozzo D., Gerardy-Schahn R., Elpeleg O.;
RT   "Mutations in SLC35A3 cause autism spectrum disorder, epilepsy and
RT   arthrogryposis.";
RL   J. Med. Genet. 50:733-739(2013).
RN   [11]
RP   VARIANT AMRS CYS-25.
RX   PubMed=28328131; DOI=10.1002/ajmg.a.38112;
RG   EuroEPINOMICS consortium AR working group;
RA   Marini C., Hardies K., Pisano T., May P., Weckhuysen S., Cellini E.,
RA   Suls A., Mei D., Balling R., Jonghe P.D., Helbig I., Garozzo D.,
RA   Guerrini R.;
RT   "Recessive mutations in SLC35A3 cause early onset epileptic encephalopathy
RT   with skeletal defects.";
RL   Am. J. Med. Genet. A 173:1119-1123(2017).
RN   [12]
RP   FUNCTION.
RX   PubMed=32938718; DOI=10.1074/jbc.ra119.012362;
RA   Szulc B., Sosicka P., Maszczak-Seneczko D., Skurska E., Shauchuk A.,
RA   Olczak T., Freeze H.H., Olczak M.;
RT   "Biosynthesis of GlcNAc-rich N- and O-glycans in the Golgi apparatus does
RT   not require the nucleotide sugar transporter SLC35A3.";
RL   J. Biol. Chem. 295:16445-16463(2020).
RN   [13]
RP   INTERACTION WITH MGAT4B, O-GLCNACYLATION, AND FUNCTION.
RX   PubMed=34981577; DOI=10.1096/fj.202101520r;
RA   Song W., Isaji T., Nakano M., Liang C., Fukuda T., Gu J.;
RT   "O-GlcNAcylation regulates beta1,4-GlcNAc-branched N-glycan biosynthesis
RT   via the OGT/SLC35A3/GnT-IV axis.";
RL   FASEB J. 36:e22149-e22149(2022).
CC   -!- FUNCTION: Transports diphosphate-N-acetylglucosamine (UDP-GlcNAc) from
CC       the cytosol into the lumen of the Golgi apparatus, functioning as an
CC       antiporter that exchanges UDP-N-acetyl-alpha-D-glucosamine for UMP
CC       (PubMed:10393322). May supply UDP-GlcNAc as substrate for Golgi-
CC       resident glycosyltransferases that generate highly branched,
CC       multiantennary complex N-glycans and keratan sulfate (PubMed:23766508,
CC       PubMed:34981577). However, the exact role of SLC35A3 still needs to be
CC       elucidated, it could be a member of a catalytically more efficient
CC       multiprotein complex rather than function independently as a single
CC       transporter (PubMed:32938718). {ECO:0000269|PubMed:10393322,
CC       ECO:0000269|PubMed:23766508, ECO:0000269|PubMed:32938718,
CC       ECO:0000269|PubMed:34981577}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-N-acetyl-alpha-D-glucosamine(in) + UMP(out) = UDP-N-
CC         acetyl-alpha-D-glucosamine(out) + UMP(in); Xref=Rhea:RHEA:72695,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:57865;
CC         Evidence={ECO:0000269|PubMed:10393322};
CC   -!- SUBUNIT: Interacts with SLC35A2; the interaction is reduced in the
CC       presence of SLC35A4 (PubMed:23089177, PubMed:28167211). Found in a
CC       complex with SLC35A2 and SLC35A4 (PubMed:28167211). Interacts with
CC       MGAT4B (PubMed:34981577). {ECO:0000269|PubMed:23089177,
CC       ECO:0000269|PubMed:28167211, ECO:0000269|PubMed:34981577}.
CC   -!- INTERACTION:
CC       Q9Y2D2; P78381-1: SLC35A2; NbExp=3; IntAct=EBI-3917581, EBI-8101118;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:10393322, ECO:0000269|PubMed:23766508,
CC       ECO:0000269|PubMed:28167211}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Y2D2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y2D2-2; Sequence=VSP_012786;
CC       Name=3;
CC         IsoId=Q9Y2D2-3; Sequence=VSP_054232, VSP_054233;
CC   -!- PTM: O-Glcnacylation regulates the stability of SLC35A3 and the
CC       specific complex formation with MGAT4B. {ECO:0000269|PubMed:34981577}.
CC   -!- DISEASE: Arthrogryposis, impaired intellectual development, and
CC       seizures (AMRS) [MIM:615553]: A disease characterized by
CC       arthrogryposis, intellectual disability, autism spectrum disorder, and
CC       epilepsy. Additional features include limb malformations, distal joint
CC       involvement, microcephaly, retromicrognathia, and general muscle
CC       hypotonia. {ECO:0000269|PubMed:24031089, ECO:0000269|PubMed:28328131}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry. In Golgi vesicles isolated from patient fibroblasts the
CC       transport of the respective nucleotide sugar is significantly reduced
CC       causing a massive decrease in the content of cell surface expressed
CC       highly branched N-glycans and a concomitant sharp increase of lower
CC       branched glycoforms.
CC   -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AB021981; BAA77841.1; -; mRNA.
DR   EMBL; AK290573; BAF83262.1; -; mRNA.
DR   EMBL; CR749816; CAH18676.1; -; mRNA.
DR   EMBL; AC118553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471097; EAW72977.1; -; Genomic_DNA.
DR   EMBL; CH471097; EAW72978.1; -; Genomic_DNA.
DR   EMBL; CH471097; EAW72979.1; -; Genomic_DNA.
DR   EMBL; BC005136; AAH05136.1; -; mRNA.
DR   CCDS; CCDS60204.1; -. [Q9Y2D2-2]
DR   CCDS; CCDS60205.1; -. [Q9Y2D2-3]
DR   CCDS; CCDS762.1; -. [Q9Y2D2-1]
DR   RefSeq; NP_001258613.1; NM_001271684.1. [Q9Y2D2-3]
DR   RefSeq; NP_001258614.1; NM_001271685.1. [Q9Y2D2-2]
DR   RefSeq; NP_036375.1; NM_012243.2. [Q9Y2D2-1]
DR   RefSeq; XP_005270748.1; XM_005270691.4. [Q9Y2D2-1]
DR   RefSeq; XP_011539438.1; XM_011541136.2.
DR   AlphaFoldDB; Q9Y2D2; -.
DR   SMR; Q9Y2D2; -.
DR   BioGRID; 117010; 11.
DR   CORUM; Q9Y2D2; -.
DR   IntAct; Q9Y2D2; 5.
DR   MINT; Q9Y2D2; -.
DR   STRING; 9606.ENSP00000359172; -.
DR   TCDB; 2.A.7.12.7; the drug/metabolite transporter (dmt) superfamily.
DR   GlyGen; Q9Y2D2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y2D2; -.
DR   PhosphoSitePlus; Q9Y2D2; -.
DR   SwissPalm; Q9Y2D2; -.
DR   BioMuta; SLC35A3; -.
DR   DMDM; 9087207; -.
DR   EPD; Q9Y2D2; -.
DR   jPOST; Q9Y2D2; -.
DR   MassIVE; Q9Y2D2; -.
DR   MaxQB; Q9Y2D2; -.
DR   PaxDb; 9606-ENSP00000359172; -.
DR   PeptideAtlas; Q9Y2D2; -.
DR   ProteomicsDB; 78874; -.
DR   ProteomicsDB; 85734; -. [Q9Y2D2-1]
DR   ProteomicsDB; 85735; -. [Q9Y2D2-2]
DR   Pumba; Q9Y2D2; -.
DR   TopDownProteomics; Q9Y2D2-1; -. [Q9Y2D2-1]
DR   Antibodypedia; 19975; 60 antibodies from 20 providers.
DR   DNASU; 23443; -.
DR   Ensembl; ENST00000370153.6; ENSP00000359172.1; ENSG00000117620.15. [Q9Y2D2-2]
DR   Ensembl; ENST00000427993.7; ENSP00000414947.2; ENSG00000117620.15. [Q9Y2D2-1]
DR   Ensembl; ENST00000465289.6; ENSP00000418527.2; ENSG00000117620.15. [Q9Y2D2-1]
DR   Ensembl; ENST00000533028.8; ENSP00000433849.1; ENSG00000117620.15. [Q9Y2D2-1]
DR   Ensembl; ENST00000638336.1; ENSP00000491145.1; ENSG00000117620.15. [Q9Y2D2-3]
DR   GeneID; 23443; -.
DR   KEGG; hsa:23443; -.
DR   MANE-Select; ENST00000533028.8; ENSP00000433849.1; NM_012243.3; NP_036375.1.
DR   UCSC; uc001dsp.3; human. [Q9Y2D2-1]
DR   AGR; HGNC:11023; -.
DR   CTD; 23443; -.
DR   DisGeNET; 23443; -.
DR   GeneCards; SLC35A3; -.
DR   HGNC; HGNC:11023; SLC35A3.
DR   HPA; ENSG00000117620; Low tissue specificity.
DR   MalaCards; SLC35A3; -.
DR   MIM; 605632; gene.
DR   MIM; 615553; phenotype.
DR   neXtProt; NX_Q9Y2D2; -.
DR   OpenTargets; ENSG00000117620; -.
DR   Orphanet; 370943; Autism spectrum disorder-epilepsy-arthrogryposis syndrome.
DR   PharmGKB; PA35891; -.
DR   VEuPathDB; HostDB:ENSG00000117620; -.
DR   eggNOG; KOG2234; Eukaryota.
DR   GeneTree; ENSGT00950000182827; -.
DR   HOGENOM; CLU_024645_1_0_1; -.
DR   InParanoid; Q9Y2D2; -.
DR   OMA; VPAIMYV; -.
DR   OrthoDB; 200085at2759; -.
DR   PhylomeDB; Q9Y2D2; -.
DR   TreeFam; TF315345; -.
DR   PathwayCommons; Q9Y2D2; -.
DR   Reactome; R-HSA-5619083; Defective SLC35A3 causes arthrogryposis, mental retardation, and seizures (AMRS).
DR   Reactome; R-HSA-727802; Transport of nucleotide sugars.
DR   SignaLink; Q9Y2D2; -.
DR   BioGRID-ORCS; 23443; 32 hits in 1148 CRISPR screens.
DR   ChiTaRS; SLC35A3; human.
DR   GenomeRNAi; 23443; -.
DR   Pharos; Q9Y2D2; Tbio.
DR   PRO; PR:Q9Y2D2; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9Y2D2; Protein.
DR   Bgee; ENSG00000117620; Expressed in mucosa of sigmoid colon and 201 other cell types or tissues.
DR   ExpressionAtlas; Q9Y2D2; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0005459; F:UDP-galactose transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005462; F:UDP-N-acetylglucosamine transmembrane transporter activity; TAS:Reactome.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; TAS:ProtInc.
DR   GO; GO:1990569; P:UDP-N-acetylglucosamine transmembrane transport; IMP:UniProtKB.
DR   InterPro; IPR007271; Nuc_sug_transpt.
DR   NCBIfam; TIGR00803; nst; 1.
DR   PANTHER; PTHR10231; NUCLEOTIDE-SUGAR TRANSMEMBRANE TRANSPORTER; 1.
DR   PANTHER; PTHR10231:SF36; UDP-N-ACETYLGLUCOSAMINE TRANSPORTER; 1.
DR   Pfam; PF04142; Nuc_sug_transp; 1.
DR   PIRSF; PIRSF005799; UDP-gal_transpt; 1.
DR   SUPFAM; SSF103481; Multidrug resistance efflux transporter EmrE; 1.
DR   Genevisible; Q9Y2D2; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antiport; Autism spectrum disorder; Disease variant;
KW   Epilepsy; Golgi apparatus; Intellectual disability; Membrane;
KW   Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..325
FT                   /note="UDP-N-acetylglucosamine transporter"
FT                   /id="PRO_0000213357"
FT   TRANSMEM        8..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1
FT                   /note="M -> MSSRSVLSPVVGTDAPDQHLELKKPQELKEMERLPLANEDKTM (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_012786"
FT   VAR_SEQ         212..220
FT                   /note="GFFGSIFGL -> VSFSLEPSL (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054232"
FT   VAR_SEQ         221..325
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054233"
FT   VARIANT         25
FT                   /note="R -> C (in AMRS)"
FT                   /evidence="ECO:0000269|PubMed:28328131"
FT                   /id="VAR_087691"
SQ   SEQUENCE   325 AA;  35985 MW;  69DFD944E37206C8 CRC64;
     MFANLKYVSL GILVFQTTSL VLTMRYSRTL KEEGPRYLSS TAVVVAELLK IMACILLVYK
     DSKCSLRALN RVLHDEILNK PMETLKLAIP SGIYTLQNNL LYVALSNLDA ATYQVTYQLK
     ILTTALFSVS MLSKKLGVYQ WLSLVILMTG VAFVQWPSDS QLDSKELSAG SQFVGLMAVL
     TACFSSGFAG VYFEKILKET KQSVWIRNIQ LGFFGSIFGL MGVYIYDGEL VSKNGFFQGY
     NRLTWIVVVL QALGGLVIAA VIKYADNILK GFATSLSIIL STLISYFWLQ DFVPTSVFFL
     GAILVITATF LYGYDPKPAG NPTKA
//