ID   S35D2_HUMAN             Reviewed;         337 AA.
AC   Q76EJ3; O95454; Q498C1; Q75W21; Q7Z5X5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-JUN-2021, entry version 132.
DE   RecName: Full=UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose transporter;
DE   AltName: Full=Homolog of Fringe connection protein 1;
DE            Short=HFRC1;
DE   AltName: Full=SQV7-like protein;
DE            Short=SQV7L;
DE   AltName: Full=Solute carrier family 35 member D2;
DE   AltName: Full=UDP-galactose transporter-related protein 8;
DE            Short=UGTrel8;
GN   Name=SLC35D2; Synonyms=HFRC, UGTREL8;
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), BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RC   TISSUE=Colon;
RX   PubMed=15082721; DOI=10.1074/jbc.m311353200;
RA   Suda T., Kamiyama S., Suzuki M., Kikuchi N., Nakayama K., Narimatsu H.,
RA   Jigami Y., Aoki T., Nishihara S.;
RT   "Molecular cloning and characterization of a human multisubstrate specific
RT   nucleotide-sugar transporter homologous to Drosophila fringe connection.";
RL   J. Biol. Chem. 279:26469-26474(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, FUNCTION, AND VARIANT SER-184.
RX   PubMed=15607426; DOI=10.1016/j.ygeno.2004.09.010;
RA   Ishida N., Kuba T., Aoki K., Miyatake S., Kawakita M., Sanai Y.;
RT   "Identification and characterization of human Golgi nucleotide sugar
RT   transporter SLC35D2, a novel member of the SLC35 nucleotide sugar
RT   transporter family.";
RL   Genomics 85:106-116(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Lung, and 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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 77-337 (ISOFORM 1), AND VARIANT SER-184.
RC   TISSUE=Placenta;
RX   PubMed=9927678; DOI=10.1073/pnas.96.3.974;
RA   Herman T., Horvitz H.R.;
RT   "Three proteins involved in Caenorhabditis elegans vulval invagination are
RT   similar to components of a glycosylation pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:974-979(1999).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Antiporter transporting nucleotide sugars such as UDP-N-
CC       acetylglucosamine (UDP-GlcNAc), UDP-glucose (UDP-Glc) and GDP-mannose
CC       (GDP-Man) pooled in the cytosol into the lumen of the Golgi in exchange
CC       for the corresponding nucleosides monophosphates (UMP for UDP-sugars
CC       and GMP for GDP-sugars). May take part in heparan sulfate synthesis by
CC       supplying UDP-Glc-NAc, the donor substrate, and thus be involved in
CC       growth factor signaling. {ECO:0000269|PubMed:15082721,
CC       ECO:0000269|PubMed:15607426}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8 uM for UDP-N-acetylglucosamine {ECO:0000269|PubMed:15082721};
CC         KM=2.1 uM for UDP-glucose {ECO:0000269|PubMed:15082721};
CC         KM=0.14 uM for GDP-mannose {ECO:0000269|PubMed:15082721};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:15082721, ECO:0000269|PubMed:15607426}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:15082721,
CC       ECO:0000269|PubMed:15607426}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q76EJ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q76EJ3-2; Sequence=VSP_030006;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, kidney, small intestine,
CC       placenta, lung and peripheral blood leukocyte. Weakly expressed in
CC       skeletal muscle and spleen. Not expressed in brain, colon and thymus.
CC       {ECO:0000269|PubMed:15607426}.
CC   -!- SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB106537; BAD14396.1; -; mRNA.
DR   EMBL; AB122077; BAC99016.1; -; mRNA.
DR   EMBL; AL160269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471174; EAW92646.1; -; Genomic_DNA.
DR   EMBL; BC009413; AAH09413.1; -; mRNA.
DR   EMBL; BC100278; AAI00279.1; -; mRNA.
DR   EMBL; BC113579; AAI13580.1; -; mRNA.
DR   EMBL; AJ005866; CAA06743.1; -; mRNA.
DR   CCDS; CCDS6717.1; -. [Q76EJ3-1]
DR   CCDS; CCDS69625.1; -. [Q76EJ3-2]
DR   RefSeq; NP_001273919.1; NM_001286990.1. [Q76EJ3-2]
DR   RefSeq; NP_008932.2; NM_007001.2. [Q76EJ3-1]
DR   BioGRID; 116234; 1.
DR   IntAct; Q76EJ3; 1.
DR   STRING; 9606.ENSP00000253270; -.
DR   TCDB; 2.A.7.15.1; the drug/metabolite transporter (dmt) superfamily.
DR   BioMuta; SLC35D2; -.
DR   DMDM; 74749832; -.
DR   jPOST; Q76EJ3; -.
DR   MassIVE; Q76EJ3; -.
DR   MaxQB; Q76EJ3; -.
DR   PaxDb; Q76EJ3; -.
DR   PeptideAtlas; Q76EJ3; -.
DR   PRIDE; Q76EJ3; -.
DR   ProteomicsDB; 68663; -. [Q76EJ3-1]
DR   ProteomicsDB; 68664; -. [Q76EJ3-2]
DR   Antibodypedia; 28641; 89 antibodies.
DR   DNASU; 11046; -.
DR   Ensembl; ENST00000253270; ENSP00000253270; ENSG00000130958. [Q76EJ3-1]
DR   Ensembl; ENST00000375259; ENSP00000364408; ENSG00000130958. [Q76EJ3-2]
DR   GeneID; 11046; -.
DR   KEGG; hsa:11046; -.
DR   UCSC; uc004awc.4; human. [Q76EJ3-1]
DR   CTD; 11046; -.
DR   DisGeNET; 11046; -.
DR   GeneCards; SLC35D2; -.
DR   HGNC; HGNC:20799; SLC35D2.
DR   HPA; ENSG00000130958; Low tissue specificity.
DR   MIM; 609182; gene.
DR   neXtProt; NX_Q76EJ3; -.
DR   OpenTargets; ENSG00000130958; -.
DR   PharmGKB; PA134909604; -.
DR   VEuPathDB; HostDB:ENSG00000130958.11; -.
DR   eggNOG; KOG1444; Eukaryota.
DR   GeneTree; ENSGT00940000160237; -.
DR   HOGENOM; CLU_040726_1_0_1; -.
DR   InParanoid; Q76EJ3; -.
DR   OMA; LYVGNHL; -.
DR   PhylomeDB; Q76EJ3; -.
DR   TreeFam; TF313307; -.
DR   PathwayCommons; Q76EJ3; -.
DR   Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR   Reactome; R-HSA-2022928; HS-GAG biosynthesis.
DR   Reactome; R-HSA-727802; Transport of nucleotide sugars.
DR   BioGRID-ORCS; 11046; 9 hits in 993 CRISPR screens.
DR   ChiTaRS; SLC35D2; human.
DR   GenomeRNAi; 11046; -.
DR   Pharos; Q76EJ3; Tbio.
DR   PRO; PR:Q76EJ3; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q76EJ3; protein.
DR   Bgee; ENSG00000130958; Expressed in mucosa of transverse colon and 231 other tissues.
DR   ExpressionAtlas; Q76EJ3; baseline and differential.
DR   Genevisible; Q76EJ3; HS.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015297; F:antiporter activity; IBA:GO_Central.
DR   GO; GO:0005338; F:nucleotide-sugar transmembrane transporter activity; NAS:UniProtKB.
DR   GO; GO:0005461; F:UDP-glucuronic acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005463; F:UDP-N-acetylgalactosamine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005462; F:UDP-N-acetylglucosamine transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0006024; P:glycosaminoglycan biosynthetic process; TAS:Reactome.
DR   GO; GO:0018146; P:keratan sulfate biosynthetic process; TAS:Reactome.
DR   InterPro; IPR004853; Sugar_P_trans_dom.
DR   Pfam; PF03151; TPT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Golgi apparatus; Membrane; Reference proteome;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..337
FT                   /note="UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose
FT                   transporter"
FT                   /id="PRO_0000313080"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..53
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..201
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..237
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..292
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        316..337
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         164..251
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_030006"
FT   VARIANT         184
FT                   /note="A -> S (in dbSNP:rs1051763)"
FT                   /evidence="ECO:0000269|PubMed:15607426,
FT                   ECO:0000269|PubMed:9927678"
FT                   /id="VAR_037653"
SQ   SEQUENCE   337 AA;  36673 MW;  7895A9153A82BE5A CRC64;
     MTAGGQAEAE GAGGEPGAAR LPSRVARLLS ALFYGTCSFL IVLVNKALLT TYGFPSPIFL
     GIGQMAATIM ILYVSKLNKI IHFPDFDKKI PVKLFPLPLL YVGNHISGLS STSKLSLPMF
     TVLRKFTIPL TLLLETIILG KQYSLNIILS VFAIILGAFI AAGSDLAFNL EGYIFVFLND
     IFTAANGVYT KQKMDPKELG KYGVLFYNAC FMIIPTLIIS VSTGDLQQAT EFNQWKNVVF
     ILQFLLSCFL GFLLMYSTVL CSYYNSALTT AVVGAIKNVS VAYIGILIGG DYIFSLLNFV
     GLNICMAGGL RYSFLTLSSQ LKPKPVGEEN ICLDLKS
//