S35D2_HUMAN
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 03-AUG-2022, entry version 136.
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 AlphaFoldDB; Q76EJ3; -.
DR SMR; Q76EJ3; -.
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 EPD; Q76EJ3; -.
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; 93 antibodies from 24 providers.
DR DNASU; 11046; -.
DR Ensembl; ENST00000253270.13; ENSP00000253270.7; ENSG00000130958.13. [Q76EJ3-1]
DR Ensembl; ENST00000375259.9; ENSP00000364408.4; ENSG00000130958.13. [Q76EJ3-2]
DR GeneID; 11046; -.
DR KEGG; hsa:11046; -.
DR MANE-Select; ENST00000253270.13; ENSP00000253270.7; NM_007001.3; NP_008932.2.
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; -.
DR eggNOG; KOG1444; Eukaryota.
DR GeneTree; ENSGT00940000160237; -.
DR HOGENOM; CLU_040726_1_0_1; -.
DR InParanoid; Q76EJ3; -.
DR OMA; ERTINFP; -.
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 SignaLink; Q76EJ3; -.
DR BioGRID-ORCS; 11046; 12 hits in 1075 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 jejunal mucosa and 190 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; TAS:Reactome.
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
