S35B3_HUMAN
ID S35B3_HUMAN Reviewed; 401 AA.
AC Q9H1N7; A6NKX9; Q1XH11; Q6MZJ0; Q7Z662; Q9Y308;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Adenosine 3'-phospho 5'-phosphosulfate transporter 2;
DE AltName: Full=3'-phosphoadenosine 5'-phosphosulfate transporter;
DE AltName: Full=PAPS transporter 2;
DE AltName: Full=Solute carrier family 35 member B3;
GN Name=SLC35B3; Synonyms=C6orf196, PAPST2; ORFNames=CGI-19;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Colon;
RX PubMed=16492677; DOI=10.1074/jbc.m508991200;
RA Kamiyama S., Sasaki N., Goda E., Ui-Tei K., Saigo K., Narimatsu H.,
RA Jigami Y., Kannagi R., Irimura T., Nishihara S.;
RT "Molecular cloning and characterization of a novel 3'-phosphoadenosine 5'-
RT phosphosulfate transporter, PAPST2.";
RL J. Biol. Chem. 281:10945-10953(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2-401 (ISOFORM 2).
RC TISSUE=Endometrial tumor, and Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 adenosine 3'-phospho 5'-
CC phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal
CC sulfuryl donor for sulfation events that take place in the Golgi.
CC Compensates for the insufficient expression of SLC35B2/PAPST1 during
CC the synthesis of sulfated glycoconjugates in the colon.
CC {ECO:0000269|PubMed:16492677}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.2 uM for PAPS {ECO:0000269|PubMed:16492677};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:16492677}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16492677}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H1N7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H1N7-2; Sequence=VSP_016193, VSP_016194;
CC Name=3;
CC IsoId=Q9H1N7-3; Sequence=VSP_016195, VSP_016196;
CC -!- TISSUE SPECIFICITY: Preferentially and highly expressed in colon.
CC {ECO:0000269|PubMed:16492677}.
CC -!- SIMILARITY: Belongs to the nucleotide-sugar transporter family. SLC35B
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27728.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAE46041.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB231931; BAE93015.1; -; mRNA.
DR EMBL; AF132953; AAD27728.1; ALT_FRAME; mRNA.
DR EMBL; BX538271; CAD98078.1; -; mRNA.
DR EMBL; BX641086; CAE46041.1; ALT_INIT; mRNA.
DR EMBL; AL355815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006973; AAH06973.1; -; mRNA.
DR CCDS; CCDS4508.1; -. [Q9H1N7-1]
DR RefSeq; NP_001136013.1; NM_001142541.2. [Q9H1N7-1]
DR RefSeq; NP_057032.2; NM_015948.4. [Q9H1N7-1]
DR RefSeq; XP_005249214.1; XM_005249157.2.
DR RefSeq; XP_006715165.1; XM_006715102.3.
DR RefSeq; XP_016866399.1; XM_017010910.1. [Q9H1N7-1]
DR RefSeq; XP_016866400.1; XM_017010911.1. [Q9H1N7-1]
DR AlphaFoldDB; Q9H1N7; -.
DR SMR; Q9H1N7; -.
DR BioGRID; 119208; 5.
DR IntAct; Q9H1N7; 1.
DR STRING; 9606.ENSP00000368981; -.
DR TCDB; 2.A.7.11.5; the drug/metabolite transporter (dmt) superfamily.
DR GlyGen; Q9H1N7; 3 sites.
DR iPTMnet; Q9H1N7; -.
DR PhosphoSitePlus; Q9H1N7; -.
DR BioMuta; SLC35B3; -.
DR DMDM; 74752580; -.
DR EPD; Q9H1N7; -.
DR jPOST; Q9H1N7; -.
DR MassIVE; Q9H1N7; -.
DR MaxQB; Q9H1N7; -.
DR PaxDb; Q9H1N7; -.
DR PeptideAtlas; Q9H1N7; -.
DR PRIDE; Q9H1N7; -.
DR ProteomicsDB; 80431; -. [Q9H1N7-1]
DR ProteomicsDB; 80432; -. [Q9H1N7-2]
DR ProteomicsDB; 80433; -. [Q9H1N7-3]
DR Antibodypedia; 24732; 9 antibodies from 5 providers.
DR DNASU; 51000; -.
DR Ensembl; ENST00000379660.4; ENSP00000368981.4; ENSG00000124786.12. [Q9H1N7-1]
DR Ensembl; ENST00000644923.2; ENSP00000496368.1; ENSG00000124786.12. [Q9H1N7-1]
DR Ensembl; ENST00000648867.1; ENSP00000497645.1; ENSG00000124786.12. [Q9H1N7-3]
DR GeneID; 51000; -.
DR KEGG; hsa:51000; -.
DR MANE-Select; ENST00000644923.2; ENSP00000496368.1; NM_001370476.2; NP_001357405.1.
DR UCSC; uc003myb.5; human. [Q9H1N7-1]
DR CTD; 51000; -.
DR DisGeNET; 51000; -.
DR GeneCards; SLC35B3; -.
DR HGNC; HGNC:21601; SLC35B3.
DR HPA; ENSG00000124786; Low tissue specificity.
DR MIM; 610845; gene.
DR neXtProt; NX_Q9H1N7; -.
DR OpenTargets; ENSG00000124786; -.
DR PharmGKB; PA134889889; -.
DR VEuPathDB; HostDB:ENSG00000124786; -.
DR eggNOG; KOG1582; Eukaryota.
DR GeneTree; ENSGT00940000157040; -.
DR HOGENOM; CLU_036019_2_0_1; -.
DR OMA; QFGYYIG; -.
DR OrthoDB; 1116466at2759; -.
DR PhylomeDB; Q9H1N7; -.
DR TreeFam; TF314523; -.
DR PathwayCommons; Q9H1N7; -.
DR Reactome; R-HSA-174362; Transport and synthesis of PAPS.
DR Reactome; R-HSA-727802; Transport of nucleotide sugars.
DR SABIO-RK; Q9H1N7; -.
DR SignaLink; Q9H1N7; -.
DR BioGRID-ORCS; 51000; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; SLC35B3; human.
DR GenomeRNAi; 51000; -.
DR Pharos; Q9H1N7; Tdark.
DR PRO; PR:Q9H1N7; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9H1N7; protein.
DR Bgee; ENSG00000124786; Expressed in pancreatic ductal cell and 191 other tissues.
DR ExpressionAtlas; Q9H1N7; baseline and differential.
DR Genevisible; Q9H1N7; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0046964; F:3'-phosphoadenosine 5'-phosphosulfate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0050428; P:3'-phosphoadenosine 5'-phosphosulfate biosynthetic process; TAS:Reactome.
DR InterPro; IPR013657; UAA.
DR PANTHER; PTHR10778; PTHR10778; 1.
DR Pfam; PF08449; UAA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Golgi apparatus; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..401
FT /note="Adenosine 3'-phospho 5'-phosphosulfate transporter
FT 2"
FT /id="PRO_0000213379"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 141..153
FT /note="IPGKTYMIIAFLT -> YVVCFYFLIFHLY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016193"
FT VAR_SEQ 154..401
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016194"
FT VAR_SEQ 261..283
FT /note="VLYSYSIGFVYILLGLTCTSGLG -> NITTSSYSGVFIFPNKLKIPLVL
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016195"
FT VAR_SEQ 284..401
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016196"
SQ SEQUENCE 401 AA; 44593 MW; 2582EFD45ECA842C CRC64;
MDLTQQAKDI QNITVQETNK NNSESIECSK ITMDLKFNNS RKYISITVPS KTQTMSPHIK
SVDDVVVLGM NLSKFNKLTQ FFICVAGVFV FYLIYGYLQE LIFSVEGFKS CGWYLTLVQF
AFYSIFGLIE LQLIQDKRRR IPGKTYMIIA FLTVGTMGLS NTSLGYLNYP TQVIFKCCKL
IPVMLGGVFI QGKRYNVADV SAAICMSLGL IWFTLADSTT APNFNLTGVV LISLALCADA
VIGNVQEKAM KLHNASNSEM VLYSYSIGFV YILLGLTCTS GLGPAVTFCA KNPVRTYGYA
FLFSLTGYFG ISFVLALIKI FGALIAVTVT TGRKAMTIVL SFIFFAKPFT FQYVWSGLLV
VLGIFLNVYS KNMDKIRLPS LYDLINKSVE ARKSRTLAQT V
