S35D1_MOUSE
ID S35D1_MOUSE Reviewed; 355 AA.
AC A2AKQ0; Q3TE90; Q5DU40; Q8BKX2; Q8BX24;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=UDP-glucuronic acid/UDP-N-acetylgalactosamine transporter {ECO:0000312|MGI:MGI:2140361};
DE Short=UDP-GlcA/UDP-GalNAc transporter {ECO:0000305};
DE AltName: Full=Solute carrier family 35 member D1 {ECO:0000303|PubMed:17952091};
GN Name=Slc35d1 {ECO:0000303|PubMed:17952091, ECO:0000312|MGI:MGI:2140361};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000312|EMBL:BAC33591.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 22-355 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33591.1}, and
RC NOD {ECO:0000312|EMBL:BAE41358.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAC33758.1},
RC Embryonic stem cell {ECO:0000312|EMBL:BAC33591.1}, and
RC Thymus {ECO:0000312|EMBL:BAE41358.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|EMBL:BAD90239.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-355.
RC TISSUE=Fetal brain {ECO:0000312|EMBL:BAD90239.1};
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17952091; DOI=10.1038/nm1655;
RA Hiraoka S., Furuichi T., Nishimura G., Shibata S., Yanagishita M.,
RA Rimoin D.L., Superti-Furga A., Nikkels P.G., Ogawa M., Katsuyama K.,
RA Toyoda H., Kinoshita-Toyoda A., Ishida N., Isono K., Sanai Y., Cohn D.H.,
RA Koseki H., Ikegawa S.;
RT "Nucleotide-sugar transporter SLC35D1 is critical to chondroitin sulfate
RT synthesis in cartilage and skeletal development in mouse and human.";
RL Nat. Med. 13:1363-1367(2007).
CC -!- FUNCTION: Transports both UDP-glucuronic acid (UDP-GlcA) and UDP-N-
CC acetylgalactosamine (UDP-GalNAc) from the cytoplasm into the
CC endoplasmic reticulum lumen. Plays a role in chondroitin sulfate
CC biosynthesis, which is important for formation of cartilage
CC extracellular matrix and normal skeletal development.
CC {ECO:0000269|PubMed:17952091}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17952091}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AKQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AKQ0-2; Sequence=VSP_059020;
CC -!- DISRUPTION PHENOTYPE: Neonatal lethality. Skeletal development is
CC severely impaired leading to reduced snout and body length, and
CC extremely short limbs. The proliferating zone of epiphyseal cartilage
CC is disorganized with densely packed round chondrocytes and little
CC extracellular matrix, in contrast to the regular columnar organization
CC of chondrocytes in wild type cartilage. Chondroitin sulfate content of
CC cartilage is significantly reduced, associated with reduced
CC proteoglycan aggregates in the extracellular matrix.
CC {ECO:0000269|PubMed:17952091}.
CC -!- SIMILARITY: Belongs to the TPT transporter family. SLC35D subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-31 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AL772338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK049180; BAC33591.1; -; mRNA.
DR EMBL; AK049462; BAC33758.1; -; mRNA.
DR EMBL; AK169775; BAE41358.1; -; mRNA.
DR EMBL; AK220330; BAD90239.1; -; mRNA.
DR CCDS; CCDS18409.1; -. [A2AKQ0-2]
DR RefSeq; NP_808400.1; NM_177732.4. [A2AKQ0-2]
DR RefSeq; XP_006503143.1; XM_006503080.3.
DR AlphaFoldDB; A2AKQ0; -.
DR SMR; A2AKQ0; -.
DR iPTMnet; A2AKQ0; -.
DR PhosphoSitePlus; A2AKQ0; -.
DR jPOST; A2AKQ0; -.
DR PeptideAtlas; A2AKQ0; -.
DR PRIDE; A2AKQ0; -.
DR ProteomicsDB; 256886; -. [A2AKQ0-1]
DR ProteomicsDB; 256887; -. [A2AKQ0-2]
DR Antibodypedia; 33400; 117 antibodies from 19 providers.
DR DNASU; 242585; -.
DR Ensembl; ENSMUST00000150285; ENSMUSP00000122124; ENSMUSG00000028521. [A2AKQ0-2]
DR GeneID; 242585; -.
DR KEGG; mmu:242585; -.
DR UCSC; uc008txk.1; mouse.
DR UCSC; uc008txl.1; mouse. [A2AKQ0-1]
DR CTD; 23169; -.
DR MGI; MGI:2140361; Slc35d1.
DR VEuPathDB; HostDB:ENSMUSG00000028521; -.
DR GeneTree; ENSGT00940000155665; -.
DR HOGENOM; CLU_040726_1_0_1; -.
DR InParanoid; A2AKQ0; -.
DR OMA; IRVWIPV; -.
DR OrthoDB; 1093260at2759; -.
DR PhylomeDB; A2AKQ0; -.
DR TreeFam; TF313307; -.
DR Reactome; R-MMU-173599; Formation of the active cofactor, UDP-glucuronate.
DR Reactome; R-MMU-727802; Transport of nucleotide sugars.
DR BioGRID-ORCS; 242585; 4 hits in 41 CRISPR screens.
DR ChiTaRS; Slc35d1; mouse.
DR PRO; PR:A2AKQ0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2AKQ0; protein.
DR Bgee; ENSMUSG00000028521; Expressed in left lobe of liver and 212 other tissues.
DR ExpressionAtlas; A2AKQ0; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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:0015165; F:pyrimidine nucleotide-sugar transmembrane transporter activity; IDA:MGI.
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:0030206; P:chondroitin sulfate biosynthetic process; IMP:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; IMP:MGI.
DR GO; GO:0090481; P:pyrimidine nucleotide-sugar transmembrane transport; IDA:MGI.
DR InterPro; IPR004853; Sugar_P_trans_dom.
DR Pfam; PF03151; TPT; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Membrane; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..355
FT /note="UDP-glucuronic acid/UDP-N-acetylgalactosamine
FT transporter"
FT /id="PRO_0000440990"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 244..292
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059020"
FT CONFLICT 116
FT /note="Y -> N (in Ref. 2; BAC33758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 39272 MW; 917C3E01F9F7BDBD CRC64;
MAEVHRRQHA PVKGEAPAKS STHRDEEELG MAPAETLTVF LKLLAAGFYG VSSFLIVVVN
KSVLTNYRFP SSLCVGLGQM VATVAVLWVG KTLRVVKFPD FDRNVPRKTF PLPLLYFGNQ
ITGLFSTKKL NLPMFTVLRR FSILFTMFAE GALLKKTFSW GIKMTVFAMI IGAFVAASSD
LAFDLEGYVF ILINDVLTAA NGAYVKQKLD SKELGKYGLL YYNALFMILP TLAIAYFTGD
AQKAMEFEGW ADTLFLLQFT LSCVMGFILM YATVLCTQYN SALTTTIVGC IKNILITYIG
MVFGGDYIFT WTNFIGLNIS IAGSLVYSYI TFTEEQLSKQ SEASNKLDTK GKGAV
