ID G3P3S2_GASAC Unreviewed; 428 AA.
AC G3P3S2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=UDP-sugar transporter protein SLC35A5 {ECO:0000256|ARBA:ARBA00040377};
DE AltName: Full=Solute carrier family 35 member A5 {ECO:0000256|ARBA:ARBA00041937};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000012245.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000012245.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000012245.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Probable UDP-sugar:UMP transmembrane antiporter involved in
CC UDP-alpha-D-glucuronate/UDP-GlcA, UDP-GlcNAc/UDP-N-acetyl-alpha-D-
CC glucosamine and UDP-N-acetyl-alpha-D-galactosamine/UDP-GalNAc transport
CC from the cytosol to the lumen of the Golgi.
CC {ECO:0000256|ARBA:ARBA00037779}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-galactosamine(in) + UMP(out) = UDP-N-
CC acetyl-alpha-D-galactosamine(out) + UMP(in); Xref=Rhea:RHEA:72735,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:67138;
CC Evidence={ECO:0000256|ARBA:ARBA00036186};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-N-acetyl-alpha-D-glucosamine(in) + UMP(out) = UDP-N-
CC acetyl-alpha-D-glucosamine(out) + UMP(in); Xref=Rhea:RHEA:72695,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:57865;
CC Evidence={ECO:0000256|ARBA:ARBA00036522};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucuronate(in) + UMP(out) = UDP-alpha-D-
CC glucuronate(out) + UMP(in); Xref=Rhea:RHEA:72727, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:58052; Evidence={ECO:0000256|ARBA:ARBA00036726};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004653}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35A
CC subfamily. {ECO:0000256|ARBA:ARBA00009976}.
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DR STRING; 69293.ENSGACP00000012239; -.
DR Ensembl; ENSGACT00000012263.1; ENSGACP00000012239.1; ENSGACG00000009271.1.
DR Ensembl; ENSGACT00000012269.1; ENSGACP00000012245.1; ENSGACG00000009271.1.
DR eggNOG; KOG2234; Eukaryota.
DR GeneTree; ENSGT00950000182827; -.
DR OMA; SCLKWAV; -.
DR TreeFam; TF354304; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000009271; Expressed in intestinal epithelial cell and 13 other cell types or tissues.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015165; F:pyrimidine nucleotide-sugar transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR007271; Nuc_sug_transpt.
DR PANTHER; PTHR10231; NUCLEOTIDE-SUGAR TRANSMEMBRANE TRANSPORTER; 1.
DR PANTHER; PTHR10231:SF90; UDP-SUGAR TRANSPORTER PROTEIN SLC35A5-RELATED; 1.
DR Pfam; PF04142; Nuc_sug_transp; 1.
DR PIRSF; PIRSF005799; UDP-gal_transpt; 1.
DR SUPFAM; SSF103481; Multidrug resistance efflux transporter EmrE; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 404..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 47421 MW; 706BE12B72F984C8 CRC64;
AMVTCRWCPG LRTRSSAYTL ALGLGFVTLG TGRILLLKFS ANAENKYDFL PASVNLLAEL
LKLLFCLAMS VRVIVKEGRS CKEPCFSSSA SFLNSLKWAV PAFLYFLDNL IIFYVMTYLQ
PAMAVLYSNF VILTTAVLFR VVLKRRLSWV QWAALFILFL SIVSLTTGSG VSQNSTALPG
LHSNPLSTPS NSCLLYTQLL EQMRNSSASE SWVSSLPAQA WRDTLVQKLR SLGVGHILLL
LQCFISAMAN IYNEKILKEG DQLTESIFIQ NSKLYLFGLV FNGLTLGLGT EARGLTAHCG
LLHGHNVYSL GLVLVTAALG LSVAFILKFR DNMFHVLTGQ ITTVLVTAFS LFLFDFRPSL
DFFLQAPTVL LAIFIYNASR LRDLDHSLQQ ERLRVINGEV LERSRGDGEE LQPLTKGNAD
SESEEESL
//