S35A4_MOUSE
ID S35A4_MOUSE Reviewed; 324 AA.
AC Q9D321; Q8BMH3; Q99JK8; Q9D0A7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable UDP-sugar transporter protein SLC35A4 {ECO:0000305};
DE AltName: Full=Solute carrier family 35 member A4 {ECO:0000312|MGI:MGI:1915093};
GN Name=Slc35a4 {ECO:0000312|MGI:MGI:1915093};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Colon, Embryo, Forelimb, and Mammary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: Mediates the transport of CDP-ribitol (By similarity). Does
CC not exhibit CMP-sialic acid, UDP-galactose and UDP-N-acetylglucosamine
CC transport activity (By similarity). {ECO:0000250|UniProtKB:Q96G79}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CDP(out) + CDP-L-ribitol(in) = CDP(in) + CDP-L-ribitol(out);
CC Xref=Rhea:RHEA:71579, ChEBI:CHEBI:57608, ChEBI:CHEBI:58069;
CC Evidence={ECO:0000250|UniProtKB:Q96G79};
CC -!- SUBUNIT: Found in a complex with SLC35A2 and SLC35A3.
CC {ECO:0000250|UniProtKB:Q96G79}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q91ZR7}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35A
CC subfamily. {ECO:0000305}.
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DR EMBL; AK011633; BAB27747.1; -; mRNA.
DR EMBL; AK018546; BAB31267.1; -; mRNA.
DR EMBL; AK031132; BAC27268.1; -; mRNA.
DR EMBL; AK145812; BAE26666.1; -; mRNA.
DR EMBL; AK164797; BAE37923.1; -; mRNA.
DR EMBL; AK170045; BAE41529.1; -; mRNA.
DR EMBL; BC006050; AAH06050.1; -; mRNA.
DR EMBL; BC117795; AAI17796.1; -; mRNA.
DR EMBL; BC117796; AAI17797.1; -; mRNA.
DR CCDS; CCDS29158.1; -.
DR RefSeq; NP_001076786.1; NM_001083317.1.
DR RefSeq; NP_080680.2; NM_026404.2.
DR RefSeq; XP_011245288.1; XM_011246986.1.
DR AlphaFoldDB; Q9D321; -.
DR SMR; Q9D321; -.
DR STRING; 10090.ENSMUSP00000036081; -.
DR PhosphoSitePlus; Q9D321; -.
DR PaxDb; Q9D321; -.
DR PRIDE; Q9D321; -.
DR Antibodypedia; 45451; 24 antibodies from 12 providers.
DR DNASU; 67843; -.
DR Ensembl; ENSMUST00000036158; ENSMUSP00000036081; ENSMUSG00000033272.
DR Ensembl; ENSMUST00000050476; ENSMUSP00000129718; ENSMUSG00000033272.
DR Ensembl; ENSMUST00000186538; ENSMUSP00000140615; ENSMUSG00000033272.
DR GeneID; 67843; -.
DR KEGG; mmu:67843; -.
DR UCSC; uc008eob.1; mouse.
DR CTD; 113829; -.
DR MGI; MGI:1915093; Slc35a4.
DR VEuPathDB; HostDB:ENSMUSG00000033272; -.
DR eggNOG; KOG2234; Eukaryota.
DR GeneTree; ENSGT00950000182827; -.
DR HOGENOM; CLU_024645_5_1_1; -.
DR InParanoid; Q9D321; -.
DR OMA; SSCVVMI; -.
DR OrthoDB; 754910at2759; -.
DR PhylomeDB; Q9D321; -.
DR TreeFam; TF315345; -.
DR BioGRID-ORCS; 67843; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Slc35a4; mouse.
DR PRO; PR:Q9D321; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D321; protein.
DR Bgee; ENSMUSG00000033272; Expressed in embryonic post-anal tail and 247 other tissues.
DR ExpressionAtlas; Q9D321; baseline and differential.
DR Genevisible; Q9D321; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0015165; F:pyrimidine nucleotide-sugar transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0032056; P:positive regulation of translation in response to stress; ISO:MGI.
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 2: Evidence at transcript level;
KW Golgi apparatus; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..324
FT /note="Probable UDP-sugar transporter protein SLC35A4"
FT /id="PRO_0000337749"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96G79"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..52
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96G79"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96G79"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..142
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96G79"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96G79"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..214
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96G79"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96G79"
FT TRANSMEM 249..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..279
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96G79"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96G79"
FT CONFLICT 157
FT /note="A -> V (in Ref. 1; BAC27268)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="L -> F (in Ref. 1; BAB27747)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="G -> GP (in Ref. 2; AAH06050)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="F -> L (in Ref. 2; AAH06050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 34695 MW; FE0209EDAE839961 CRC64;
MSVEDGGVPG LARPRQARWT LLLFLSTAMY GAHAPFLALC HVDGRVPFRP SSAVLLTELT
KLLLCAFSLL VGWQTWPQGT PPWRQAVPFA LSALLYGANN NLVIYLQRYM DPSTYQVLSN
LKIGSTALLY CLCLGHRLSA RQGLALLLLM AAGACYASGG FQEPVNTLPG PASAAGAHPM
PLHITPLGLL LLILYCLISG LSSVYTELIM KRQRLPLALQ NLFLYTFGVI LNFGLYAGSG
PGPGFLEGFS GWAVLVVLNQ AVNGLLMSAV MKHGSSITRL FIVSCSLVVN AVLSAVLLQL
QLTAIFFLAA LLIGLAVCLY YGSP
