ID   SO2B1_MOUSE             Reviewed;         683 AA.
AC   Q8BXB6; Q8BLV8;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 151.
DE   RecName: Full=Solute carrier organic anion transporter family member 2B1;
DE   AltName: Full=Organic anion transporting polypeptide 2B1 {ECO:0000303|PubMed:31123035};
DE            Short=OATP2B1 {ECO:0000303|PubMed:31123035};
DE   AltName: Full=Solute carrier family 21 member 9 {ECO:0000250|UniProtKB:O94956};
GN   Name=Slco2b1 {ECO:0000312|MGI:MGI:1351872};
GN   Synonyms=Oatp2b1 {ECO:0000303|PubMed:31123035}, Slc21a9
GN   {ECO:0000250|UniProtKB:O94956};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=31123035; DOI=10.1124/dmd.119.087619;
RA   Medwid S., Li M.M.J., Knauer M.J., Lin K., Mansell S.E., Schmerk C.L.,
RA   Zhu C., Griffin K.E., Yousif M.D., Dresser G.K., Schwarz U.I., Kim R.B.,
RA   Tirona R.G.;
RT   "Fexofenadine and Rosuvastatin Pharmacokinetics in Mice with Targeted
RT   Disruption of Organic Anion Transporting Polypeptide 2B1.";
RL   Drug Metab. Dispos. 47:832-842(2019).
RN   [5]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=32114507; DOI=10.1124/dmd.119.090316;
RA   Chen M., Hu S., Li Y., Gibson A.A., Fu Q., Baker S.D., Sparreboom A.;
RT   "Role of Oatp2b1 in Drug Absorption and Drug-Drug Interactions.";
RL   Drug Metab. Dispos. 48:419-425(2020).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=34205780; DOI=10.3390/pharmaceutics13060918;
RA   Marie S., Hernandez-Lozano I., Breuil L., Truillet C., Hu S.,
RA   Sparreboom A., Tournier N., Langer O.;
RT   "Imaging-Based Characterization of a Slco2b1(-/-) Mouse Model Using
RT   [11C]Erlotinib and [99mTc]Mebrofenin as Probe Substrates.";
RL   Pharmaceutics 13:0-0(2021).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Mediates the Na(+)-independent transport of steroid sulfate
CC       conjugates such as estrone 3-sulfate (E1S), dehydroepiandrosterone
CC       sulfate (DHEA-S) and pregnenolone sulfate (PregS) and other specific
CC       organic anions (PubMed:31123035). Responsible for the transport of E1S
CC       through the basal membrane of syncytiotrophoblast, highlighting a
CC       potential role in the placental absorption of fetal-derived sulfated
CC       steroids including DHEA-S (By similarity). Also facilitates the uptake
CC       of sulfated steroids at the basal/sinusoidal membrane of hepatocytes,
CC       therefore accounting for the major part of organic anions clearance of
CC       liver. Mediates the intestinal uptake of sulfated steroids. Mediates
CC       the uptake of the neurosteroids DHEA-S and PregS into the endothelial
CC       cells of the blood-brain barrier as the first step to enter the brain.
CC       Also plays a role in the reuptake of neuropeptides such as substance
CC       P/TAC1 and vasoactive intestinal peptide/VIP released from retinal
CC       neurons. May act as a heme transporter that promotes cellular iron
CC       availability. Also transports heme by-product coproporphyrin III
CC       (CPIII), and may be involved in their hepatic disposition (By
CC       similarity). Mediates the uptake of other substrates such as
CC       prostaglandins D2 (PGD2), E1 (PGE1) and E2 (PGE2), taurocholate, L-
CC       thyroxine, leukotriene C4 and thromboxane B2 (PubMed:31123035). May
CC       contribute to regulate the transport of organic compounds in testis
CC       across the blood-testis-barrier (By similarity). Shows a pH-sensitive
CC       substrate specificity which may be ascribed to the protonation state of
CC       the binding site and leads to a stimulation of substrate transport in
CC       an acidic microenvironment. The exact transport mechanism has not been
CC       yet deciphered but most likely involves an anion exchange, coupling the
CC       cellular uptake of organic substrate with the efflux of an anionic
CC       compound. Hydrogencarbonate/HCO3(-) acts as a probable counteranion
CC       that exchanges for organic anions. Cytoplasmic glutamate may also act
CC       as counteranion in the placenta. An inwardly directed proton gradient
CC       has also been proposed as the driving force of E1S uptake with a
CC       (H(+):E1S) stoichiometry of (1:1) (By similarity).
CC       {ECO:0000250|UniProtKB:O94956, ECO:0000269|PubMed:31123035}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dehydroepiandrosterone 3-sulfate(out) = dehydroepiandrosterone
CC         3-sulfate(in); Xref=Rhea:RHEA:71839, ChEBI:CHEBI:57905;
CC         Evidence={ECO:0000305|PubMed:31123035};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone 3-sulfate(out) = estrone 3-sulfate(in);
CC         Xref=Rhea:RHEA:71835, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000305|PubMed:31123035};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone 3-sulfate(out) + hydrogencarbonate(in) = estrone 3-
CC         sulfate(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:73055,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000250|UniProtKB:O94956};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=taurocholate(out) = taurocholate(in); Xref=Rhea:RHEA:71703,
CC         ChEBI:CHEBI:36257; Evidence={ECO:0000305|PubMed:31123035};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coproporphyrin III(out) = coproporphyrin III(in);
CC         Xref=Rhea:RHEA:74363, ChEBI:CHEBI:131725;
CC         Evidence={ECO:0000250|UniProtKB:O94956};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=substance P(out) = substance P(in); Xref=Rhea:RHEA:74367,
CC         ChEBI:CHEBI:190692; Evidence={ECO:0000250|UniProtKB:O94956};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pregnenolone sulfate(out) = pregnenolone sulfate(in);
CC         Xref=Rhea:RHEA:73023, ChEBI:CHEBI:133000;
CC         Evidence={ECO:0000250|UniProtKB:O94956};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin E2(out) = prostaglandin E2(in);
CC         Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000250|UniProtKB:O94956};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prostaglandin D2(out) = prostaglandin D2(in);
CC         Xref=Rhea:RHEA:50976, ChEBI:CHEBI:57406;
CC         Evidence={ECO:0000250|UniProtKB:Q9JHI3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-thyroxine(out) = L-thyroxine(in); Xref=Rhea:RHEA:71819,
CC         ChEBI:CHEBI:58448; Evidence={ECO:0000250|UniProtKB:O94956};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O94956};
CC       Multi-pass membrane protein {ECO:0000305}. Basal cell membrane
CC       {ECO:0000250|UniProtKB:O94956}; Multi-pass membrane protein
CC       {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:O94956};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver, kidney, small intestine mucosa,
CC       large intestine, brain, lung, spleen, stomach and heart.
CC       {ECO:0000269|PubMed:31123035, ECO:0000269|PubMed:32114507}.
CC   -!- DOMAIN: A conserved histidine residue in the third transmembrane domain
CC       (His-128) might play an essential role in the pH sensitivity of
CC       SLCO2B1/OATP2B1-mediated substrate transport. Transmembrane domain 1
CC       (TM1) may be localized within the substrate binding pocket.
CC       {ECO:0000250|UniProtKB:O94956}.
CC   -!- DISRUPTION PHENOTYPE: Knockout mice show no difference in growth rate,
CC       viability, fertility, progeny, life span, weight, organs, tissues and
CC       serum biochemistry (PubMed:31123035). Knockout females exhibit an
CC       increased in Cyp2c65 and Cyp2c66 gene expression, but not males
CC       (PubMed:32114507). Knockout mice exhibit a decreased plasma
CC       concentration of certain drugs administered orally such as fexofenadine
CC       and fluvastatin, whereas no difference were observed after intravenous
CC       administration (PubMed:31123035, PubMed:32114507). Also exhibit a
CC       decreased in the hepatic uptake of drugs erlotinib and mebrofenin after
CC       intravenous injection (PubMed:34205780). Don't show any difference in
CC       fluvastatin liver concentration after oral injection (PubMed:32114507).
CC       {ECO:0000269|PubMed:31123035, ECO:0000269|PubMed:32114507,
CC       ECO:0000269|PubMed:34205780}.
CC   -!- MISCELLANEOUS: Most likely contributes to the absorption and the
CC       disposition of a wide range of drugs in the intestine and the liver.
CC       {ECO:0000269|PubMed:31123035, ECO:0000269|PubMed:32114507,
CC       ECO:0000269|PubMed:34205780}.
CC   -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC       {ECO:0000305}.
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DR   EMBL; AK041144; BAC30838.1; -; mRNA.
DR   EMBL; AK048120; BAC33248.1; -; mRNA.
DR   CCDS; CCDS21485.1; -.
DR   RefSeq; NP_001239459.1; NM_001252530.1.
DR   RefSeq; NP_001239460.1; NM_001252531.1.
DR   RefSeq; NP_780525.1; NM_175316.3.
DR   RefSeq; XP_011239942.1; XM_011241640.2.
DR   RefSeq; XP_011239943.1; XM_011241641.2.
DR   AlphaFoldDB; Q8BXB6; -.
DR   SMR; Q8BXB6; -.
DR   STRING; 10090.ENSMUSP00000102703; -.
DR   GlyCosmos; Q8BXB6; 4 sites, No reported glycans.
DR   GlyGen; Q8BXB6; 4 sites.
DR   iPTMnet; Q8BXB6; -.
DR   PhosphoSitePlus; Q8BXB6; -.
DR   SwissPalm; Q8BXB6; -.
DR   jPOST; Q8BXB6; -.
DR   MaxQB; Q8BXB6; -.
DR   PaxDb; 10090-ENSMUSP00000032985; -.
DR   ProteomicsDB; 261105; -.
DR   Antibodypedia; 17309; 133 antibodies from 18 providers.
DR   DNASU; 101488; -.
DR   Ensembl; ENSMUST00000032985.11; ENSMUSP00000032985.5; ENSMUSG00000030737.18.
DR   Ensembl; ENSMUST00000107086.9; ENSMUSP00000102701.3; ENSMUSG00000030737.18.
DR   GeneID; 101488; -.
DR   KEGG; mmu:101488; -.
DR   UCSC; uc009ilw.2; mouse.
DR   AGR; MGI:1351872; -.
DR   CTD; 11309; -.
DR   MGI; MGI:1351872; Slco2b1.
DR   VEuPathDB; HostDB:ENSMUSG00000030737; -.
DR   eggNOG; KOG3626; Eukaryota.
DR   GeneTree; ENSGT01080000257336; -.
DR   HOGENOM; CLU_008954_4_1_1; -.
DR   InParanoid; Q8BXB6; -.
DR   OMA; FMLGSAM; -.
DR   OrthoDB; 2874223at2759; -.
DR   TreeFam; TF317540; -.
DR   Reactome; R-MMU-189483; Heme degradation.
DR   Reactome; R-MMU-879518; Transport of organic anions.
DR   Reactome; R-MMU-9749641; Aspirin ADME.
DR   Reactome; R-MMU-9754706; Atorvastatin ADME.
DR   BioGRID-ORCS; 101488; 5 hits in 77 CRISPR screens.
DR   ChiTaRS; Slco2b1; mouse.
DR   PRO; PR:Q8BXB6; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8BXB6; Protein.
DR   Bgee; ENSMUSG00000030737; Expressed in brain blood vessel and 189 other cell types or tissues.
DR   ExpressionAtlas; Q8BXB6; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0015125; F:bile acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; IMP:UniProtKB.
DR   GO; GO:0015132; F:prostaglandin transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0022857; F:transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015721; P:bile acid and bile salt transport; ISO:MGI.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0015711; P:organic anion transport; ISO:MGI.
DR   GO; GO:0071718; P:sodium-independent icosanoid transport; ISO:MGI.
DR   GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR002350; Kazal_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004156; OATP.
DR   NCBIfam; TIGR00805; oat; 1.
DR   PANTHER; PTHR11388; ORGANIC ANION TRANSPORTER; 1.
DR   PANTHER; PTHR11388:SF87; SOLUTE CARRIER ORGANIC ANION TRANSPORTER FAMILY MEMBER 2B1; 1.
DR   Pfam; PF03137; OATP; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   Genevisible; Q8BXB6; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..683
FT                   /note="Solute carrier organic anion transporter family
FT                   member 2B1"
FT                   /id="PRO_0000191062"
FT   TOPO_DOM        1..41
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..61
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..80
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        102..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..132
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        133..177
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..207
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        208..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        227..247
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        248..265
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..290
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        291..355
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..377
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        378..397
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        398..421
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        422..425
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..449
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        450..553
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        554..576
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        577..585
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        586..611
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        612..644
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        645..662
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        663..683
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          472..532
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17208939,
FT                   ECO:0007744|PubMed:18630941"
FT   MOD_RES         312
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94956"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JHI3"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        527
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        478..509
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        484..505
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        493..530
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ   SEQUENCE   683 AA;  74531 MW;  20D977BA1482688A CRC64;
     MPDRSTKTTM GTEDMHERKV SVEPQDSHQD AQPRGMFHNI KFFVLCHSLL QLTQLMISGY
     LKSSISTVEK RFGLSSQISG LLAAFNEVGN VSLILFVSYF GSRVHRPRMI GYGALLVATA
     GLLMALPHFI SEPYRYDHSS SDNRSLDFEA SLCLPTTMAP ASALSNGSCS SHTETKHLTM
     VGIMFAAQTL LGIGGVPIQP FGISYIDDFA HHSNSPLYIG ILFGITTMGP GLAYGLGSLM
     LRLYVDIDRM PEGGINLTPK DPRWVGAWWL GFLISSGLVV LASSPYFFFP REMPKEKHEF
     HFRRKVLASA ASTASKGEDL SSQHEPLKKQ AGLAQIAPDL TLVQFVKVFP RVLLRNLRHP
     IFLLVVLSQV CTSSMVAGMA TFLPKFLERQ FSITASFANM LLGCLTIPLV IVGIMMGGVL
     VKRLHLSPVQ CSALCLLGSL LCLLFSVPLF FIGCSTHQIA GITQDLGAQP GPSLFPGCSE
     PCSCQSDDFN PVCDTSAYVE YTTPCHAGCT GRVVQEALGK SQVFYTNCSC VAGNGTVPAG
     SCESACSRLV LPFIVLFSLG AGLASITHTP SFMLILRGVK KEDKTLAVGM QFMLLRVLAW
     MPSPVIHGSA IDTTCVHWAL TCGRRAVCRY YDHDLLRNRF IGLQFFFKSG SLVCFTLVLA
     ILRQQSREAS TRTTVKSSEL QQL
//