S35A1_CRIGR
ID S35A1_CRIGR Reviewed; 336 AA.
AC O08520;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=CMP-sialic acid transporter;
DE Short=CMP-SA-Tr;
DE Short=CMP-Sia-Tr {ECO:0000303|PubMed:9310377};
DE AltName: Full=Solute carrier family 35 member A1;
GN Name=SLC35A1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TRANSPORTER
RP ACTIVITY.
RX PubMed=9310377; DOI=10.1111/j.1432-1033.1997.00187.x;
RA Eckhardt M., Gerardy-Schahn R.;
RT "Molecular cloning of the hamster CMP-sialic acid transporter.";
RL Eur. J. Biochem. 248:187-192(1997).
CC -!- FUNCTION: Transports CMP-sialic acid from the cytosol into Golgi
CC vesicles where glycosyltransferases function (PubMed:9310377).
CC Efficient CMP-sialic acid uptake depends on the presence of free CMP
CC inside the vesicles, suggesting the proteins functions as an
CC antiporter. Binds both CMP-sialic acid and free CMP, but has higher
CC affinity for free CMP (By similarity). Also mediates the transport of
CC CDP-ribitol (By similarity). {ECO:0000250|UniProtKB:Q61420,
CC ECO:0000269|PubMed:9310377}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP(out) + CMP-N-acetyl-beta-neuraminate(in) = CMP(in) + CMP-
CC N-acetyl-beta-neuraminate(out); Xref=Rhea:RHEA:67724,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377;
CC Evidence={ECO:0000269|PubMed:9310377};
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:Q61420};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P78382}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:9310377}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35A
CC subfamily. {ECO:0000305}.
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DR EMBL; Y12074; CAA72794.1; -; mRNA.
DR RefSeq; NP_001233684.1; NM_001246755.1.
DR AlphaFoldDB; O08520; -.
DR SMR; O08520; -.
DR STRING; 10029.NP_001233684.1; -.
DR Ensembl; ENSCGRT00001025160; ENSCGRP00001020916; ENSCGRG00001019920.
DR GeneID; 100689322; -.
DR KEGG; cge:100689322; -.
DR CTD; 10559; -.
DR eggNOG; KOG2234; Eukaryota.
DR GeneTree; ENSGT00950000182827; -.
DR OrthoDB; 703674at2759; -.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0015297; F:antiporter activity; ISS:UniProtKB.
DR GO; GO:0005456; F:CMP-N-acetylneuraminate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0015782; P:CMP-N-acetylneuraminate transmembrane transport; ISS:UniProtKB.
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; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..336
FT /note="CMP-sialic acid transporter"
FT /id="PRO_0000213350"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT TOPO_DOM 31..45
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT TOPO_DOM 65..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT TOPO_DOM 109..114
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT TOPO_DOM 136..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT TOPO_DOM 161..175
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT TOPO_DOM 197..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 210..228
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT TOPO_DOM 229..243
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 244..262
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT TOPO_DOM 263..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..288
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT TOPO_DOM 289..296
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 297..315
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT TOPO_DOM 316..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 316..336
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT BINDING 55
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT BINDING 101..102
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT BINDING 117..124
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT BINDING 188
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT BINDING 210..214
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
FT BINDING 272
FT /ligand="CMP-N-acetyl-beta-neuraminate"
FT /ligand_id="ChEBI:CHEBI:57812"
FT /evidence="ECO:0000250|UniProtKB:Q61420"
SQ SEQUENCE 336 AA; 36608 MW; 209D8C524A67D8F9 CRC64;
MAQARENVSL FFKLYCLAVM TLVAAAYTVA LRYTRTTAKE LYFSTTAVCV TEVIKLLISV
GLLAKETGSL GRFKASLSEN VLGSPKELMK LSVPSLVYAV QNNMAFLALS NLDAAVYQVT
YQLKIPCTAL CTVLMLNRTL SKLQWVSVFM LCGGVILVQW KPAQATKVVV EQSPLLGFGA
IAIAVLCSGF AGVYFEKVLK SSDTSLWVRN IQMYLSGIVV TLVGTYLSDG AEIKEKGFFY
GYTYYVWFVI FLASVGGLYT SVVVKYTDNI MKGFSAAAAI VLSTIASVML FGLQITLSFA
MGALLVCISI YLYGLPRQDT TCIQQEATSK ERVIGV
