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Database: UniProt
Entry: A0A3Q1B1X4_AMPOC
LinkDB: A0A3Q1B1X4_AMPOC
Original site: A0A3Q1B1X4_AMPOC 
ID   A0A3Q1B1X4_AMPOC        Unreviewed;       422 AA.
AC   A0A3Q1B1X4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000007850.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000007850.1}
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   AlphaFoldDB; A0A3Q1B1X4; -.
DR   STRING; 80972.ENSAOCP00000007850; -.
DR   Ensembl; ENSAOCT00000002119.1; ENSAOCP00000007850.1; ENSAOCG00000011739.1.
DR   GeneTree; ENSGT00950000182827; -.
DR   OMA; SCLKWAV; -.
DR   OrthoDB; 5388606at2759; -.
DR   Proteomes; UP000257160; Unplaced.
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:UP000257160};
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        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        55..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        272..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        352..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          398..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..415
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   422 AA;  46810 MW;  4BC65CD121C29D43 CRC64;
     MACCHSCPRL CSRSMAYTLA LGLGSVTLGT SRTLLLKFSE NAENKYDFLP ASVNLLAEAL
     KLLFCLVMSV RVIVREGRSC RELGFASSSP FLSSLKWAVP AFLYFLDNLI AFYVMAYLQP
     VMTVLSSNLV ILTTAVLFRI VLKRRLSWVQ WAALVILFLS IVSLTTGSAS SQNSNAVPGH
     HANLSAPSNS CLLYTQLLEQ SKNSSAGESW ASSLAGQAWR SRVMERLLCL GAGHILLLLQ
     CFIAAMANIY NEKILKDGDQ LTESIFIQNS KLYAFGVVFN GLTVWAQGLH HDLLHGHNVY
     SLGLVPVTAA LGLSVAFILK FRDNMFHVLT GQITTVLVTG LSFFLFDFHP TWHFFLQAPM
     VLLAIFIYNA SRLKDPEYSL QQEKLRVING EVFERSRGDG EELELLTKPN TDSESEEDSP
     QF
//
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