S35A2_HUMAN
ID S35A2_HUMAN Reviewed; 396 AA.
AC P78381; A8K2L9; A8K9V1; B4DE11; B4DPT2; E7EW45; Q8IV21; Q92553;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=UDP-galactose translocator;
DE AltName: Full=Solute carrier family 35 member A2;
DE AltName: Full=UDP-galactose transporter;
DE Short=UDP-Gal-Tr;
DE Short=UGT;
GN Name=SLC35A2; Synonyms=UGALT, UGT, UGTL;
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).
RX PubMed=8889805; DOI=10.1093/oxfordjournals.jbchem.a021404;
RA Miura N., Ishida N., Hoshino M., Yamauchi M., Hara T., Ayusawa D.,
RA Kawakita M.;
RT "Human UDP-galactose translocator: molecular cloning of a complementary DNA
RT that complements the genetic defect of a mutant cell line deficient in UDP-
RT galactose translocator.";
RL J. Biochem. 120:236-241(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fibroblast;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8128316; DOI=10.1007/bf01233383;
RA Hara T., Yamauchi M., Takahashi E., Hoshino M., Aoki K., Ayusawa D.,
RA Kawakita M.;
RT "The UDP-galactose translocator gene is mapped to band Xp11.23-p11.22
RT containing the Wiskott-Aldrich syndrome locus.";
RL Somat. Cell Mol. Genet. 19:571-575(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ishida N., Miura N., Yamauchi M., Kawakita M.;
RT "Genomic organization of the human UDP-galactose transporter gene.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC TISSUE=Colon, Lymphoblast, and Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Pancreas;
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 [9]
RP INTERACTION WITH SLC35A3.
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 [10]
RP INTERACTION WITH B4GALT4 (ISOFORM 2).
RX PubMed=32827291; DOI=10.1007/s10719-020-09941-z;
RA Shauchuk A., Szulc B., Maszczak-Seneczko D., Wiertelak W., Skurska E.,
RA Olczak M.;
RT "N-glycosylation of the human beta1,4-galactosyltransferase 4 is crucial
RT for its activity and Golgi localization.";
RL Glycoconj. J. 37:577-588(2020).
RN [11]
RP INTERACTION WITH SLC35A3, IDENTIFICATION IN A COMPLEX WITH SLC35A3 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 [12]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-252.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [13]
RP VARIANT CDG2M ILE-331.
RX PubMed=23561849; DOI=10.1016/j.ajhg.2013.03.012;
RG University of Washington Center for Mendelian Genomics;
RA Ng B.G., Buckingham K.J., Raymond K., Kircher M., Turner E.H., He M.,
RA Smith J.D., Eroshkin A., Szybowska M., Losfeld M.E., Chong J.X.,
RA Kozenko M., Li C., Patterson M.C., Gilbert R.D., Nickerson D.A.,
RA Shendure J., Bamshad M.J., Freeze H.H.;
RT "Mosaicism of the UDP-galactose transporter SLC35A2 causes a congenital
RT disorder of glycosylation.";
RL Am. J. Hum. Genet. 92:632-636(2013).
RN [14]
RP INVOLVEMENT IN CDG2M, AND VARIANT CDG2M PHE-213.
RX PubMed=24115232; DOI=10.1002/humu.22446;
RA Kodera H., Nakamura K., Osaka H., Maegaki Y., Haginoya K., Mizumoto S.,
RA Kato M., Okamoto N., Iai M., Kondo Y., Nishiyama K., Tsurusaki Y.,
RA Nakashima M., Miyake N., Hayasaka K., Sugahara K., Yuasa I., Wada Y.,
RA Matsumoto N., Saitsu H.;
RT "De novo mutations in SLC35A2 encoding a UDP-galactose transporter cause
RT early-onset epileptic encephalopathy.";
RL Hum. Mutat. 34:1708-1714(2013).
RN [15]
RP VARIANT MET-258.
RX PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
RA Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
RA Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
RA Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
RA Gyllensten U., Pinto D., Maciel P.;
RT "Identification of novel genetic causes of Rett syndrome-like phenotypes.";
RL J. Med. Genet. 53:190-199(2016).
CC -!- FUNCTION: Transports nucleotide sugars from the cytosol into Golgi
CC vesicles where glycosyltransferases function.
CC -!- SUBUNIT: Interacts with SLC35A3; the interaction is reduced in the
CC presence of SLC35A4 (PubMed:23089177, PubMed:28167211). Found in a
CC complex with SLC35A3 and SLC35A4 (PubMed:28167211).
CC {ECO:0000269|PubMed:23089177, ECO:0000269|PubMed:28167211}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with B4GALT4.
CC {ECO:0000269|PubMed:32827291}.
CC -!- INTERACTION:
CC P78381-1; Q9Y2D2: SLC35A3; NbExp=3; IntAct=EBI-8101118, EBI-3917581;
CC P78381-3; P27658: COL8A1; NbExp=3; IntAct=EBI-13307533, EBI-747133;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:28167211}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=UGT2;
CC IsoId=P78381-1; Sequence=Displayed;
CC Name=2; Synonyms=UGT1;
CC IsoId=P78381-2; Sequence=VSP_003728;
CC Name=3;
CC IsoId=P78381-3; Sequence=VSP_042029;
CC Name=4;
CC IsoId=P78381-4; Sequence=VSP_054335, VSP_003728;
CC Name=5;
CC IsoId=P78381-5; Sequence=VSP_055197, VSP_003728;
CC -!- DISEASE: Congenital disorder of glycosylation 2M (CDG2M) [MIM:300896]:
CC An X-linked dominant, severe neurologic disorder characterized by
CC developmental delay, hypotonia, ocular anomalies, and brain
CC malformations. Othere more variable clinical features included
CC seizures, hypsarrhythmia, poor feeding, microcephaly, recurrent
CC infections, dysmorphic features, shortened limbs, and coagulation
CC defects. Congenital disorders of glycosylation are caused by a defect
CC in glycoprotein biosynthesis and characterized by under-glycosylated
CC serum glycoproteins and a wide variety of clinical features. The broad
CC spectrum of features reflects the critical role of N-glycoproteins
CC during embryonic development, differentiation, and maintenance of cell
CC functions. {ECO:0000269|PubMed:23561849, ECO:0000269|PubMed:24115232}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35A
CC subfamily. {ECO:0000305}.
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DR EMBL; D88146; BAA13545.1; -; mRNA.
DR EMBL; D84454; BAA12673.1; -; mRNA.
DR EMBL; AB042425; BAA95614.1; -; Genomic_DNA.
DR EMBL; AB042425; BAA95615.1; -; Genomic_DNA.
DR EMBL; AK290284; BAF82973.1; -; mRNA.
DR EMBL; AK292816; BAF85505.1; -; mRNA.
DR EMBL; AK293415; BAG56922.1; -; mRNA.
DR EMBL; AK298484; BAG60694.1; -; mRNA.
DR EMBL; AF207550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50733.1; -; Genomic_DNA.
DR EMBL; CH471224; EAW50734.1; -; Genomic_DNA.
DR EMBL; BC035747; AAH35747.1; -; mRNA.
DR CCDS; CCDS14311.1; -. [P78381-1]
DR CCDS; CCDS35247.1; -. [P78381-3]
DR CCDS; CCDS43937.1; -. [P78381-2]
DR CCDS; CCDS65253.1; -. [P78381-5]
DR CCDS; CCDS65254.1; -. [P78381-4]
DR PIR; JC5022; JC5022.
DR RefSeq; NP_001027460.1; NM_001032289.2. [P78381-3]
DR RefSeq; NP_001035963.1; NM_001042498.2. [P78381-2]
DR RefSeq; NP_001269576.1; NM_001282647.1.
DR RefSeq; NP_001269577.1; NM_001282648.1.
DR RefSeq; NP_001269578.1; NM_001282649.1. [P78381-5]
DR RefSeq; NP_001269579.1; NM_001282650.1.
DR RefSeq; NP_001269580.1; NM_001282651.1. [P78381-4]
DR RefSeq; NP_005651.1; NM_005660.2. [P78381-1]
DR AlphaFoldDB; P78381; -.
DR SMR; P78381; -.
DR BioGRID; 113202; 57.
DR CORUM; P78381; -.
DR ELM; P78381; -.
DR IntAct; P78381; 9.
DR MINT; P78381; -.
DR STRING; 9606.ENSP00000416002; -.
DR ChEMBL; CHEMBL3430867; -.
DR TCDB; 2.A.7.12.6; the drug/metabolite transporter (dmt) superfamily.
DR iPTMnet; P78381; -.
DR PhosphoSitePlus; P78381; -.
DR BioMuta; SLC35A2; -.
DR DMDM; 2499228; -.
DR EPD; P78381; -.
DR jPOST; P78381; -.
DR MassIVE; P78381; -.
DR MaxQB; P78381; -.
DR PaxDb; P78381; -.
DR PeptideAtlas; P78381; -.
DR PRIDE; P78381; -.
DR ProteomicsDB; 18770; -.
DR ProteomicsDB; 3913; -.
DR ProteomicsDB; 57603; -. [P78381-1]
DR ProteomicsDB; 57604; -. [P78381-2]
DR ProteomicsDB; 57605; -. [P78381-3]
DR Antibodypedia; 25927; 65 antibodies from 16 providers.
DR DNASU; 7355; -.
DR Ensembl; ENST00000247138.11; ENSP00000247138.5; ENSG00000102100.16. [P78381-1]
DR Ensembl; ENST00000376521.6; ENSP00000365704.1; ENSG00000102100.16. [P78381-2]
DR Ensembl; ENST00000445167.7; ENSP00000402726.2; ENSG00000102100.16. [P78381-3]
DR Ensembl; ENST00000452555.7; ENSP00000416002.2; ENSG00000102100.16. [P78381-4]
DR Ensembl; ENST00000635285.1; ENSP00000489484.1; ENSG00000102100.16. [P78381-2]
DR Ensembl; ENST00000635589.1; ENSP00000489197.1; ENSG00000102100.16. [P78381-5]
DR GeneID; 7355; -.
DR KEGG; hsa:7355; -.
DR MANE-Select; ENST00000247138.11; ENSP00000247138.5; NM_005660.3; NP_005651.1.
DR UCSC; uc004dlo.3; human. [P78381-1]
DR CTD; 7355; -.
DR DisGeNET; 7355; -.
DR GeneCards; SLC35A2; -.
DR HGNC; HGNC:11022; SLC35A2.
DR HPA; ENSG00000102100; Low tissue specificity.
DR MalaCards; SLC35A2; -.
DR MIM; 300896; phenotype.
DR MIM; 314375; gene.
DR neXtProt; NX_P78381; -.
DR OpenTargets; ENSG00000102100; -.
DR Orphanet; 268973; Isolated focal cortical dysplasia type Ia.
DR Orphanet; 356961; SLC35A2-CDG.
DR PharmGKB; PA35890; -.
DR VEuPathDB; HostDB:ENSG00000102100; -.
DR eggNOG; KOG2234; Eukaryota.
DR GeneTree; ENSGT00950000182827; -.
DR HOGENOM; CLU_024645_1_1_1; -.
DR InParanoid; P78381; -.
DR OMA; YSRIMPP; -.
DR OrthoDB; 703674at2759; -.
DR PhylomeDB; P78381; -.
DR TreeFam; TF315345; -.
DR PathwayCommons; P78381; -.
DR Reactome; R-HSA-5619072; Defective SLC35A2 causes congenital disorder of glycosylation 2M (CDG2M).
DR Reactome; R-HSA-727802; Transport of nucleotide sugars.
DR SignaLink; P78381; -.
DR SIGNOR; P78381; -.
DR BioGRID-ORCS; 7355; 65 hits in 718 CRISPR screens.
DR ChiTaRS; SLC35A2; human.
DR GeneWiki; SLC35A2; -.
DR GenomeRNAi; 7355; -.
DR Pharos; P78381; Tbio.
DR PRO; PR:P78381; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P78381; protein.
DR Bgee; ENSG00000102100; Expressed in secondary oocyte and 188 other tissues.
DR ExpressionAtlas; P78381; baseline and differential.
DR Genevisible; P78381; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005459; F:UDP-galactose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0006012; P:galactose metabolic process; TAS:ProtInc.
DR GO; GO:0072334; P:UDP-galactose transmembrane transport; TAS:ProtInc.
DR InterPro; IPR007271; Nuc_sug_transpt.
DR PANTHER; PTHR10231; PTHR10231; 1.
DR Pfam; PF04142; Nuc_sug_transp; 1.
DR PIRSF; PIRSF005799; UDP-gal_transpt; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Congenital disorder of glycosylation;
KW Disease variant; Epilepsy; Golgi apparatus; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..396
FT /note="UDP-galactose translocator"
FT /id="PRO_0000213353"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 358..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 30
FT /note="A -> AELLLTWEEAEARGQGLPQPLPDTSVRIP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054335"
FT VAR_SEQ 31..91
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055197"
FT VAR_SEQ 143..396
FT /note="VTYQLKILTTALFSVLMLNRSLSRLQWASLLLLFTGVAIVQAQQAGGGGPRP
FT LDQNPGAGLAAVVASCLSSGFAGVYFEKILKGSSGSVWLRNLQLGLFGTALGLVGLWWA
FT EGTAVATRGFFFGYTPAVWGVVLNQAFGGLLVAVVVKYADNILKGFATSLSIVLSTVAS
FT IRLFGFHVDPLFALGAGLVIGAVYLYSLPRGAAKAIASASASASGPCVHQQPPGQPPPP
FT QLSSHRGDLITEPFLPKLLTKVKGS -> PSPRCSQSHSLCLCLRLRALRSPAASRAAT
FT TTAAVFPPWRPHHGALSAKVSAGEVRAGSNGGTQGRGTGVEGVGHLQDPSRHPPGPGSS
FT GFGRWSFLPGH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_042029"
FT VAR_SEQ 389..396
FT /note="LLTKVKGS -> SVLVK (in isoform 2, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:9010752"
FT /id="VSP_003728"
FT VARIANT 213
FT /note="S -> F (in CDG2M; dbSNP:rs587777436)"
FT /evidence="ECO:0000269|PubMed:24115232"
FT /id="VAR_071699"
FT VARIANT 252
FT /note="W -> C (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036579"
FT VARIANT 258
FT /note="V -> M (found in a patient with Rett syndrome-like
FT phenotype; unknown pathological significance;
FT dbSNP:rs1557042828)"
FT /evidence="ECO:0000269|PubMed:26740508"
FT /id="VAR_079035"
FT VARIANT 331
FT /note="V -> I (in CDG2M; dbSNP:rs587776961)"
FT /evidence="ECO:0000269|PubMed:23561849"
FT /id="VAR_069773"
FT CONFLICT 85
FT /note="L -> P (in Ref. 5; BAF82973)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="V -> A (in Ref. 5; BAG60694)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 41307 MW; 6EC1DC9532FE9221 CRC64;
MAAVGAGGST AAPGPGAVSA GALEPGTASA AHRRLKYISL AVLVVQNASL ILSIRYARTL
PGDRFFATTA VVMAEVLKGL TCLLLLFAQK RGNVKHLVLF LHEAVLVQYV DTLKLAVPSL
IYTLQNNLQY VAISNLPAAT FQVTYQLKIL TTALFSVLML NRSLSRLQWA SLLLLFTGVA
IVQAQQAGGG GPRPLDQNPG AGLAAVVASC LSSGFAGVYF EKILKGSSGS VWLRNLQLGL
FGTALGLVGL WWAEGTAVAT RGFFFGYTPA VWGVVLNQAF GGLLVAVVVK YADNILKGFA
TSLSIVLSTV ASIRLFGFHV DPLFALGAGL VIGAVYLYSL PRGAAKAIAS ASASASGPCV
HQQPPGQPPP PQLSSHRGDL ITEPFLPKLL TKVKGS
