S22AF_HUMAN
ID S22AF_HUMAN Reviewed; 547 AA.
AC Q8IZD6; A8MUR3; Q6UXP5; Q8TAL9; Q9NSH5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Solute carrier family 22 member 15;
DE AltName: Full=Fly-like putative transporter 1;
DE Short=Flipt 1;
GN Name=SLC22A15; Synonyms=FLIPT1; ORFNames=UNQ9429/PRO34686;
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), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Kidney;
RX PubMed=12372408; DOI=10.1016/s0006-291x(02)02343-4;
RA Eraly S.A., Nigam S.K.;
RT "Novel human cDNAs homologous to Drosophila Orct and mammalian carnitine
RT transporters.";
RL Biochem. Biophys. Res. Commun. 297:1159-1166(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-349.
RC TISSUE=Brain;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 391-547 (ISOFORM 1).
RC TISSUE=Amygdala;
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 [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15028572; DOI=10.1196/annals.1304.008;
RA Molderings G.J., Bruss M., Bonisch H., Gothert M.;
RT "Identification and pharmacological characterization of a specific agmatine
RT transport system in human tumor cell lines.";
RL Ann. N. Y. Acad. Sci. 1009:75-81(2003).
CC -!- FUNCTION: Probably transports organic cations (By similarity). Appears
CC not to be the agmatine transporter. {ECO:0000250,
CC ECO:0000269|PubMed:15028572}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IZD6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZD6-2; Sequence=VSP_034059, VSP_034060;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in kidney and brain.
CC Expressed at high levels in skeletal muscle, heart, liver, placenta and
CC white blood cells. Expressed at moderate levels in lung and spleen.
CC Expressed at low levels in thymus, small intestine and colon. Expressed
CC in several intestinal tumor cell lines. {ECO:0000269|PubMed:12372408,
CC ECO:0000269|PubMed:15028572}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels at 20-25 weeks of
CC gestation in fetal brain, lung, liver and kidney.
CC {ECO:0000269|PubMed:12372408}.
CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26358.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH26358.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY145501; AAN52927.1; -; mRNA.
DR EMBL; AY358258; AAQ88625.1; -; mRNA.
DR EMBL; AL357137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56640.1; -; Genomic_DNA.
DR EMBL; BC026358; AAH26358.1; ALT_SEQ; mRNA.
DR EMBL; AL353933; CAB89246.1; -; mRNA.
DR CCDS; CCDS44198.1; -. [Q8IZD6-1]
DR PIR; T48683; T48683.
DR RefSeq; NP_060890.2; NM_018420.2. [Q8IZD6-1]
DR AlphaFoldDB; Q8IZD6; -.
DR SMR; Q8IZD6; -.
DR BioGRID; 120636; 22.
DR STRING; 9606.ENSP00000358515; -.
DR TCDB; 2.A.1.19.32; the major facilitator superfamily (mfs).
DR GlyGen; Q8IZD6; 4 sites.
DR iPTMnet; Q8IZD6; -.
DR PhosphoSitePlus; Q8IZD6; -.
DR BioMuta; SLC22A15; -.
DR DMDM; 74750790; -.
DR EPD; Q8IZD6; -.
DR MassIVE; Q8IZD6; -.
DR PaxDb; Q8IZD6; -.
DR PeptideAtlas; Q8IZD6; -.
DR PRIDE; Q8IZD6; -.
DR Antibodypedia; 9786; 73 antibodies from 19 providers.
DR DNASU; 55356; -.
DR Ensembl; ENST00000369502.1; ENSP00000358514.1; ENSG00000163393.13. [Q8IZD6-2]
DR Ensembl; ENST00000369503.9; ENSP00000358515.4; ENSG00000163393.13. [Q8IZD6-1]
DR GeneID; 55356; -.
DR KEGG; hsa:55356; -.
DR MANE-Select; ENST00000369503.9; ENSP00000358515.4; NM_018420.3; NP_060890.2.
DR UCSC; uc001ega.3; human. [Q8IZD6-1]
DR CTD; 55356; -.
DR DisGeNET; 55356; -.
DR GeneCards; SLC22A15; -.
DR HGNC; HGNC:20301; SLC22A15.
DR HPA; ENSG00000163393; Tissue enhanced (bone marrow, brain).
DR MIM; 608275; gene.
DR neXtProt; NX_Q8IZD6; -.
DR OpenTargets; ENSG00000163393; -.
DR PharmGKB; PA134870374; -.
DR VEuPathDB; HostDB:ENSG00000163393; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000160364; -.
DR HOGENOM; CLU_001265_33_7_1; -.
DR InParanoid; Q8IZD6; -.
DR OMA; AGQFYPM; -.
DR OrthoDB; 464838at2759; -.
DR PhylomeDB; Q8IZD6; -.
DR TreeFam; TF315847; -.
DR PathwayCommons; Q8IZD6; -.
DR Reactome; R-HSA-549127; Organic cation transport.
DR BioGRID-ORCS; 55356; 8 hits in 1068 CRISPR screens.
DR ChiTaRS; SLC22A15; human.
DR GenomeRNAi; 55356; -.
DR Pharos; Q8IZD6; Tdark.
DR PRO; PR:Q8IZD6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8IZD6; protein.
DR Bgee; ENSG00000163393; Expressed in corpus callosum and 145 other tissues.
DR Genevisible; Q8IZD6; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..547
FT /note="Solute carrier family 22 member 15"
FT /id="PRO_0000338619"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 522..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 244..245
FT /note="FI -> VD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_034059"
FT VAR_SEQ 246..547
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_034060"
FT VARIANT 349
FT /note="P -> Q (in dbSNP:rs17852419)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_043813"
SQ SEQUENCE 547 AA; 60540 MW; AFE2EEA64B7FFDBC CRC64;
MEVEEAFQAV GEMGIYQMYL CFLLAVLLQL YVATEAILIA LVGATPSYHW DLAELLPNQS
HGNQSAGEDQ AFGDWLLTAN GSEIHKHVHF SSSFTSIASE WFLIANRSYK VSAASSFFFS
GVFVGVISFG QLSDRFGRKK VYLTGFALDI LFAIANGFSP SYEFFAVTRF LVGMMNGGMS
LVAFVLLNEC VGTAYWALAG SIGGLFFAVG IAQYALLGYF IRSWRTLAIL VNLQGTVVFL
LSLFIPESPR WLYSQGRLSE AEEALYLIAK RNRKLKCTFS LTHPANRSCR ETGSFLDLFR
YRVLLGHTLI LMFIWFVCSL VYYGLTLSAG DLGGSIYANL ALSGLIEIPS YPLCIYLINQ
KWFGRKRTLS AFLCLGGLAC LIVMFLPEKK DTGVFAVVNS HSLSLLGKLT ISAAFNIVYI
YTSELYPTVI RNVGLGTCSM FSRVGGIIAP FIPSLKYVQW SLPFIVFGAT GLTSGLLSLL
LPETLNSPLL ETFSDLQVYS YRRLGEEALS LQALDPQQCV DKESSLGSES EEEEEFYDAD
EETQMIK
