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   24-JAN-2024, entry version 158.
DE   RecName: Full=Adenosine 3'-phospho 5'-phosphosulfate transporter 2 {ECO:0000305|PubMed:16492677};
DE   AltName: Full=3'-phosphoadenosine 5'-phosphosulfate transporter {ECO:0000303|PubMed:16492677};
DE   AltName: Full=PAPS transporter 2;
DE   AltName: Full=Solute carrier family 35 member B3 {ECO:0000312|HGNC:HGNC:21601};
GN   Name=SLC35B3 {ECO:0000312|HGNC:HGNC:21601};
GN   Synonyms=C6orf196 {ECO:0000312|HGNC:HGNC:21601}, PAPST2
GN   {ECO:0000303|PubMed:16492677}; 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, TRANSPORTER ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP   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: Probably functions as a 3'-phosphoadenylyl sulfate:adenosine
CC       3',5'-bisphosphate antiporter at the Golgi membranes. Mediates the
CC       transport from the cytosol into the lumen of the Golgi of 3'-
CC       phosphoadenylyl sulfate/adenosine 3'-phospho 5'-phosphosulfate (PAPS),
CC       a universal sulfuryl donor for sulfation events that take place in that
CC       compartment. {ECO:0000269|PubMed:16492677}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3'-phosphoadenylyl sulfate(in) + adenosine 3',5'-
CC         bisphosphate(out) = 3'-phosphoadenylyl sulfate(out) + adenosine
CC         3',5'-bisphosphate(in); Xref=Rhea:RHEA:76063, ChEBI:CHEBI:58339,
CC         ChEBI:CHEBI:58343; Evidence={ECO:0000305|PubMed:16492677};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.2 uM for 3'-phosphoadenylyl sulfate
CC         {ECO:0000269|PubMed:16492677};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:16492677}; Multi-pass membrane protein
CC       {ECO:0000255}.
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; 6.
DR   IntAct; Q9H1N7; 1.
DR   STRING; 9606.ENSP00000368981; -.
DR   TCDB; 2.A.7.11.5; the drug/metabolite transporter (dmt) superfamily.
DR   GlyCosmos; Q9H1N7; 3 sites, No reported glycans.
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; 9606-ENSP00000368981; -.
DR   PeptideAtlas; Q9H1N7; -.
DR   ProteomicsDB; 80431; -. [Q9H1N7-1]
DR   ProteomicsDB; 80432; -. [Q9H1N7-2]
DR   ProteomicsDB; 80433; -. [Q9H1N7-3]
DR   Antibodypedia; 24732; 10 antibodies from 6 providers.
DR   DNASU; 51000; -.
DR   Ensembl; ENST00000379660.4; ENSP00000368981.4; ENSG00000124786.13. [Q9H1N7-1]
DR   Ensembl; ENST00000644923.2; ENSP00000496368.1; ENSG00000124786.13. [Q9H1N7-1]
DR   Ensembl; ENST00000648867.1; ENSP00000497645.1; ENSG00000124786.13. [Q9H1N7-3]
DR   GeneID; 51000; -.
DR   KEGG; hsa:51000; -.
DR   UCSC; uc003myb.5; human. [Q9H1N7-1]
DR   AGR; HGNC:21601; -.
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   InParanoid; Q9H1N7; -.
DR   OMA; YNRTTQF; -.
DR   OrthoDB; 614761at2759; -.
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 1153 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 193 other cell types or tissues.
DR   ExpressionAtlas; Q9H1N7; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0046964; F:3'-phosphoadenosine 5'-phosphosulfate transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:1902558; P:5'-adenylyl sulfate transmembrane transport; TAS:Reactome.
DR   InterPro; IPR013657; SCL35B1-4/HUT1.
DR   PANTHER; PTHR10778:SF8; ADENOSINE 3'-PHOSPHO 5'-PHOSPHOSULFATE TRANSPORTER 2; 1.
DR   PANTHER; PTHR10778; SOLUTE CARRIER FAMILY 35 MEMBER B; 1.
DR   Pfam; PF08449; UAA; 1.
DR   Genevisible; Q9H1N7; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antiport; 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
//