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 14-DEC-2022, entry version 171. 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, AND 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 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 [9] 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). CC -!- FUNCTION: Uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) CC transporter in the Golgi apparatus. May supply UDP-GlcNAc as substrate CC for Golgi-resident glycosyltransferases that generate branching of CC diantennary oligosaccharides. {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). CC {ECO:0000269|PubMed:23089177, ECO:0000269|PubMed:28167211}. 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:28167211}; Multi-pass CC membrane protein {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 -!- 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}. Note=The disease is caused by CC variants affecting the gene represented in this entry. In Golgi CC vesicles isolated from patient fibroblasts the transport of the CC respective nucleotide sugar is significantly reduced causing a massive CC decrease in the content of cell surface expressed highly branched N- CC glycans and a concomitant sharp increase of lower branched glycoforms. CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35A CC subfamily. {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; 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. [Q9Y2D2-1] 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 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; Q9Y2D2; -. DR PeptideAtlas; Q9Y2D2; -. DR ProteomicsDB; 78874; -. DR ProteomicsDB; 85734; -. [Q9Y2D2-1] DR ProteomicsDB; 85735; -. [Q9Y2D2-2] DR TopDownProteomics; Q9Y2D2-1; -. [Q9Y2D2-1] DR Antibodypedia; 19975; 58 antibodies from 19 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; AFFSVTM; -. DR OrthoDB; 703674at2759; -. 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; 31 hits in 1069 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 199 other tissues. DR ExpressionAtlas; Q9Y2D2; baseline and differential. DR Genevisible; Q9Y2D2; HS. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. 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 PANTHER; PTHR10231; NUCLEOTIDE-SUGAR TRANSMEMBRANE TRANSPORTER; 1. DR Pfam; PF04142; Nuc_sug_transp; 1. DR PIRSF; PIRSF005799; UDP-gal_transpt; 1. PE 1: Evidence at protein level; KW Alternative splicing; Autism spectrum disorder; Epilepsy; Golgi apparatus; KW Intellectual disability; Membrane; Reference proteome; Sugar transport; KW Transmembrane; Transmembrane helix; 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" 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 //