SO1C1_HUMAN
ID SO1C1_HUMAN Reviewed; 712 AA.
AC Q9NYB5; B7Z251; B7Z3Q3; B7Z8P1; F5GZD6; Q5JPA4;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Solute carrier organic anion transporter family member 1C1;
DE AltName: Full=Organic anion transporter F;
DE Short=OATP-F;
DE AltName: Full=Organic anion transporter polypeptide-related protein 5;
DE Short=OAT-RP-5;
DE Short=OATPRP5;
DE AltName: Full=Organic anion-transporting polypeptide 14;
DE Short=OATP-14;
DE AltName: Full=Solute carrier family 21 member 14;
DE AltName: Full=Thyroxine transporter;
GN Name=SLCO1C1; Synonyms=OATP14, OATP1C1, OATPF, SLC21A14;
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).
RC TISSUE=Brain;
RX PubMed=12351693; DOI=10.1210/me.2001-0309;
RA Pizzagalli F., Hagenbuch B., Stieger B., Klenk U., Folkers G., Meier P.J.;
RT "Identification of a novel human organic anion transporting polypeptide as
RT a high affinity thyroxine transporter.";
RL Mol. Endocrinol. 16:2283-2296(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wu Y., Hsiang B.H., Zhu Y., Yang W.-P., Kirchgessner T.G.;
RT "Identification and characterization of novel human OATP family members.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Amygdala, Kidney, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18687783; DOI=10.1210/en.2008-0378;
RA Roberts L.M., Woodford K., Zhou M., Black D.S., Haggerty J.E., Tate E.H.,
RA Grindstaff K.K., Mengesha W., Raman C., Zerangue N.;
RT "Expression of the thyroid hormone transporters monocarboxylate
RT transporter-8 (SLC16A2) and organic ion transporter-14 (SLCO1C1) at the
RT blood-brain barrier.";
RL Endocrinology 149:6251-6261(2008).
CC -!- FUNCTION: Mediates the Na(+)-independent high affinity transport of
CC organic anions such as the thyroid hormones thyroxine (T4) and rT3.
CC Other potential substrates, such as triiodothyronine (T3), 17-beta-
CC glucuronosyl estradiol, estrone-3-sulfate and sulfobromophthalein (BSP)
CC are transported with much lower efficiency. May play a significant role
CC in regulating T4 flux into and out of the brain (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18687783};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18687783}.
CC Note=Expressed in both luminal and abluminal membranes of brain
CC capillary endothelial cells. Localized to the apical membrane and basal
CC surfaces of choroid plexus (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NYB5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYB5-2; Sequence=VSP_042882;
CC Name=3;
CC IsoId=Q9NYB5-3; Sequence=VSP_045279;
CC Name=4;
CC IsoId=Q9NYB5-4; Sequence=VSP_045278, VSP_045279;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and in Leydig cells in
CC testis. Detected in many brain regions with the exception of pons and
CC cerebellum. Not strongly enriched in cerebral microvessels.
CC {ECO:0000269|PubMed:18687783}.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000305}.
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DR EMBL; AF260704; AAF70338.1; -; mRNA.
DR EMBL; AF205076; AAG42208.1; -; mRNA.
DR EMBL; AK294333; BAH11737.1; -; mRNA.
DR EMBL; AK296236; BAH12289.1; -; mRNA.
DR EMBL; AK303713; BAH14027.1; -; mRNA.
DR EMBL; AL834209; CAI46209.1; -; mRNA.
DR EMBL; AC092491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022461; AAH22461.1; -; mRNA.
DR CCDS; CCDS53757.1; -. [Q9NYB5-3]
DR CCDS; CCDS53758.1; -. [Q9NYB5-2]
DR CCDS; CCDS53759.1; -. [Q9NYB5-4]
DR CCDS; CCDS8683.1; -. [Q9NYB5-1]
DR RefSeq; NP_001139416.1; NM_001145944.1. [Q9NYB5-4]
DR RefSeq; NP_001139417.1; NM_001145945.1. [Q9NYB5-2]
DR RefSeq; NP_001139418.1; NM_001145946.1. [Q9NYB5-3]
DR RefSeq; NP_059131.1; NM_017435.4. [Q9NYB5-1]
DR RefSeq; XP_005253451.1; XM_005253394.2. [Q9NYB5-1]
DR RefSeq; XP_005253453.1; XM_005253396.2. [Q9NYB5-4]
DR RefSeq; XP_011519011.1; XM_011520709.2.
DR RefSeq; XP_016874973.1; XM_017019484.1.
DR RefSeq; XP_016874974.1; XM_017019485.1.
DR AlphaFoldDB; Q9NYB5; -.
DR SMR; Q9NYB5; -.
DR BioGRID; 119819; 1.
DR IntAct; Q9NYB5; 2.
DR MINT; Q9NYB5; -.
DR STRING; 9606.ENSP00000444149; -.
DR ChEMBL; CHEMBL2073697; -.
DR DrugBank; DB00286; Conjugated estrogens.
DR DrugBank; DB00509; Dextrothyroxine.
DR DrugBank; DB00586; Diclofenac.
DR DrugBank; DB00917; Dinoprostone.
DR DrugBank; DB00783; Estradiol.
DR DrugBank; DB13952; Estradiol acetate.
DR DrugBank; DB13953; Estradiol benzoate.
DR DrugBank; DB13954; Estradiol cypionate.
DR DrugBank; DB13955; Estradiol dienanthate.
DR DrugBank; DB13956; Estradiol valerate.
DR DrugBank; DB00451; Levothyroxine.
DR DrugBank; DB00279; Liothyronine.
DR DrugBank; DB01583; Liotrix.
DR DrugBank; DB00939; Meclofenamic acid.
DR DrugBank; DB00563; Methotrexate.
DR DrugBank; DB01092; Ouabain.
DR DrugBank; DB00252; Phenytoin.
DR DrugBank; DB01032; Probenecid.
DR DrugBank; DB04348; Taurocholic acid.
DR DrugBank; DB09100; Thyroid, porcine.
DR TCDB; 2.A.60.1.15; the organo anion transporter (oat) family.
DR GlyGen; Q9NYB5; 4 sites.
DR iPTMnet; Q9NYB5; -.
DR PhosphoSitePlus; Q9NYB5; -.
DR BioMuta; SLCO1C1; -.
DR DMDM; 27734564; -.
DR jPOST; Q9NYB5; -.
DR MassIVE; Q9NYB5; -.
DR PaxDb; Q9NYB5; -.
DR PeptideAtlas; Q9NYB5; -.
DR PRIDE; Q9NYB5; -.
DR Antibodypedia; 23947; 115 antibodies from 21 providers.
DR DNASU; 53919; -.
DR Ensembl; ENST00000266509.7; ENSP00000266509.2; ENSG00000139155.9. [Q9NYB5-1]
DR Ensembl; ENST00000540354.5; ENSP00000438665.1; ENSG00000139155.9. [Q9NYB5-2]
DR Ensembl; ENST00000545102.1; ENSP00000444527.1; ENSG00000139155.9. [Q9NYB5-4]
DR Ensembl; ENST00000545604.5; ENSP00000444149.1; ENSG00000139155.9. [Q9NYB5-3]
DR GeneID; 53919; -.
DR KEGG; hsa:53919; -.
DR MANE-Select; ENST00000266509.7; ENSP00000266509.2; NM_017435.5; NP_059131.1.
DR UCSC; uc001rei.3; human. [Q9NYB5-1]
DR CTD; 53919; -.
DR DisGeNET; 53919; -.
DR GeneCards; SLCO1C1; -.
DR HGNC; HGNC:13819; SLCO1C1.
DR HPA; ENSG00000139155; Group enriched (brain, choroid plexus).
DR MIM; 613389; gene.
DR neXtProt; NX_Q9NYB5; -.
DR OpenTargets; ENSG00000139155; -.
DR PharmGKB; PA37815; -.
DR VEuPathDB; HostDB:ENSG00000139155; -.
DR eggNOG; KOG3626; Eukaryota.
DR GeneTree; ENSGT01050000244856; -.
DR HOGENOM; CLU_008954_4_0_1; -.
DR InParanoid; Q9NYB5; -.
DR OMA; NAGCEKE; -.
DR OrthoDB; 1029129at2759; -.
DR PhylomeDB; Q9NYB5; -.
DR PathwayCommons; Q9NYB5; -.
DR Reactome; R-HSA-879518; Transport of organic anions.
DR SignaLink; Q9NYB5; -.
DR BioGRID-ORCS; 53919; 8 hits in 1057 CRISPR screens.
DR ChiTaRS; SLCO1C1; human.
DR GenomeRNAi; 53919; -.
DR Pharos; Q9NYB5; Tbio.
DR PRO; PR:Q9NYB5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NYB5; protein.
DR Bgee; ENSG00000139155; Expressed in choroid plexus epithelium and 123 other tissues.
DR ExpressionAtlas; Q9NYB5; baseline and differential.
DR Genevisible; Q9NYB5; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015721; P:bile acid and bile salt transport; IBA:GO_Central.
DR GO; GO:2000611; P:positive regulation of thyroid hormone generation; IMP:ARUK-UCL.
DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR GO; GO:0070327; P:thyroid hormone transport; IDA:ARUK-UCL.
DR GO; GO:0055085; P:transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004156; OATP.
DR InterPro; IPR030764; OATP1C1.
DR PANTHER; PTHR11388; PTHR11388; 1.
DR PANTHER; PTHR11388:SF99; PTHR11388:SF99; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF03137; OATP; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00805; oat; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..712
FT /note="Solute carrier organic anion transporter family
FT member 1C1"
FT /id="PRO_0000191054"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..134
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..213
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..271
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..296
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..370
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..390
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..414
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..418
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..442
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..554
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..577
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..612
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 613..646
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..664
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..712
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 470..525
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 533
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 476..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 482..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 491..523
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045278"
FT VAR_SEQ 177..225
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042882"
FT VAR_SEQ 640..712
FT /note="HIYLGLTVILGTVSILLSIAVLFILKKNYVSKHRSFITKRERTMVSTRFQKE
FT NYTTSDHLLQPNYWPGKETQL -> YQIKSIPASHCYSIPDLHNATDTNKFSCHFTACK
FT TYISGTNCDTGHSVNSPKHCSTFHFKEKLCFKTQKFYNQERKNNGVYKIPKGKLHYK
FT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_045279"
FT CONFLICT 444
FT /note="A -> T (in Ref. 3; BAH14027)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9NYB5-3:660
FT /note="T -> S (in Ref. 3; BAH14027)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9NYB5-4:559
FT /note="S -> F (in Ref. 3; BAH11737)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 712 AA; 78696 MW; CB6D37AAAA8FA7CD CRC64;
MDTSSKENIQ LFCKTSVQPV GRPSFKTEYP SSEEKQPCCG ELKVFLCALS FVYFAKALAE
GYLKSTITQI ERRFDIPSSL VGVIDGSFEI GNLLVITFVS YFGAKLHRPK IIGAGCVIMG
VGTLLIAMPQ FFMEQYKYER YSPSSNSTLS ISPCLLESSS QLPVSVMEKS KSKISNECEV
DTSSSMWIYV FLGNLLRGIG ETPIQPLGIA YLDDFASEDN AAFYIGCVQT VAIIGPIFGF
LLGSLCAKLY VDIGFVNLDH ITITPKDPQW VGAWWLGYLI AGIISLLAAV PFWYLPKSLP
RSQSREDSNS SSEKSKFIID DHTDYQTPQG ENAKIMEMAR DFLPSLKNLF GNPVYFLYLC
TSTVQFNSLF GMVTYKPKYI EQQYGQSSSR ANFVIGLINI PAVALGIFSG GIVMKKFRIS
VCGAAKLYLG SSVFGYLLFL SLFALGCENS DVAGLTVSYQ GTKPVSYHER ALFSDCNSRC
KCSETKWEPM CGENGITYVS ACLAGCQTSN RSGKNIIFYN CTCVGIAASK SGNSSGIVGR
CQKDNGCPQM FLYFLVISVI TSYTLSLGGI PGYILLLRCI KPQLKSFALG IYTLAIRVLA
GIPAPVYFGV LIDTSCLKWG FKRCGSRGSC RLYDSNVFRH IYLGLTVILG TVSILLSIAV
LFILKKNYVS KHRSFITKRE RTMVSTRFQK ENYTTSDHLL QPNYWPGKET QL
