OSBP1_MOUSE
ID OSBP1_MOUSE Reviewed; 805 AA.
AC Q3B7Z2; E9QPD4; Q3V163; Q52KH7; Q570Y8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2013, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Oxysterol-binding protein 1;
GN Name=Osbp; Synonyms=Kiaa4220 {ECO:0000303|Ref.4};
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-805.
RC STRAIN=C57BL/6J;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 290-805.
RC TISSUE=Pancreatic islet;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191; SER-196;
RP SER-349 AND SER-380, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191 AND SER-349, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191; SER-238 AND
RP SER-349, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191; SER-196;
RP SER-343; SER-349; THR-375; SER-380 AND SER-383, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [10]
RP INTERACTION WITH RELCH, AND IDENTIFICATION IN A COMPLEX WITH RELCH AND
RP RAB11A.
RX PubMed=29514919; DOI=10.1083/jcb.201709123;
RA Sobajima T., Yoshimura S.I., Maeda T., Miyata H., Miyoshi E., Harada A.;
RT "The Rab11-binding protein RELCH/KIAA1468 controls intracellular
RT cholesterol distribution.";
RL J. Cell Biol. 217:1777-1796(2018).
CC -!- FUNCTION: Lipid transporter involved in lipid countertransport between
CC the Golgi complex and membranes of the endoplasmic reticulum:
CC specifically exchanges sterol with phosphatidylinositol 4-phosphate
CC (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is
CC degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum.
CC Binds cholesterol and a range of oxysterols including 25-
CC hydroxycholesterol. Cholesterol binding promotes the formation of a
CC complex with PP2A and a tyrosine phosphatase which dephosphorylates
CC ERK1/2, whereas 25-hydroxycholesterol causes its disassembly. Regulates
CC cholesterol efflux by decreasing ABCA1 stability.
CC {ECO:0000250|UniProtKB:P22059}.
CC -!- SUBUNIT: Homodimer or homotrimer. Interacts (via FFAT motif) with VAPA.
CC Interacts (via C-terminus) with RELCH (via the third HEAT repeat)
CC (PubMed:29514919). Found in a complex composed of RELCH, OSBP1 and
CC RAB11A (PubMed:29514919). {ECO:0000250|UniProtKB:P22059,
CC ECO:0000269|PubMed:29514919}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P22059}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P22059}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P22059}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P22059}. Note=Predominantly cytosolic.
CC {ECO:0000250|UniProtKB:P22059}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3B7Z2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3B7Z2-2; Sequence=VSP_035281, VSP_035282;
CC -!- DOMAIN: The FFAT motif is required for interaction with VATA and proper
CC localization of the protein. {ECO:0000250|UniProtKB:P22059}.
CC -!- DOMAIN: The PH and the Ala/Gly-rich domains control cholesterol binding
CC without affecting 25-hydroxycholesterol binding.
CC {ECO:0000250|UniProtKB:P16258}.
CC -!- DOMAIN: The second coiled-coil domain is required for interaction with
CC the tyrosine phosphatase. {ECO:0000250|UniProtKB:P16258}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI07328.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAI07329.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; 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; AK132663; BAE21289.1; -; mRNA.
DR EMBL; AC124464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094342; AAH94342.1; -; mRNA.
DR EMBL; BC107327; AAI07328.1; ALT_SEQ; mRNA.
DR EMBL; BC107328; AAI07329.1; ALT_SEQ; mRNA.
DR EMBL; AK220301; BAD90226.1; -; mRNA.
DR CCDS; CCDS37925.1; -. [Q3B7Z2-1]
DR RefSeq; NP_001028346.1; NM_001033174.1. [Q3B7Z2-1]
DR RefSeq; XP_006527502.1; XM_006527439.3. [Q3B7Z2-2]
DR AlphaFoldDB; Q3B7Z2; -.
DR BMRB; Q3B7Z2; -.
DR SMR; Q3B7Z2; -.
DR BioGRID; 218069; 19.
DR ComplexPortal; CPX-507; Vapa-Osbp complex.
DR IntAct; Q3B7Z2; 1.
DR MINT; Q3B7Z2; -.
DR STRING; 10090.ENSMUSP00000025590; -.
DR iPTMnet; Q3B7Z2; -.
DR PhosphoSitePlus; Q3B7Z2; -.
DR SwissPalm; Q3B7Z2; -.
DR EPD; Q3B7Z2; -.
DR jPOST; Q3B7Z2; -.
DR MaxQB; Q3B7Z2; -.
DR PaxDb; Q3B7Z2; -.
DR PeptideAtlas; Q3B7Z2; -.
DR PRIDE; Q3B7Z2; -.
DR ProteomicsDB; 294118; -. [Q3B7Z2-1]
DR ProteomicsDB; 294119; -. [Q3B7Z2-2]
DR Antibodypedia; 27760; 278 antibodies from 32 providers.
DR Ensembl; ENSMUST00000025590; ENSMUSP00000025590; ENSMUSG00000024687. [Q3B7Z2-1]
DR GeneID; 76303; -.
DR KEGG; mmu:76303; -.
DR UCSC; uc008gtj.1; mouse. [Q3B7Z2-1]
DR UCSC; uc008gtk.1; mouse. [Q3B7Z2-2]
DR CTD; 5007; -.
DR MGI; MGI:97447; Osbp.
DR VEuPathDB; HostDB:ENSMUSG00000024687; -.
DR eggNOG; KOG1737; Eukaryota.
DR GeneTree; ENSGT00940000156164; -.
DR HOGENOM; CLU_007105_5_1_1; -.
DR InParanoid; Q3B7Z2; -.
DR OMA; EFEMANS; -.
DR OrthoDB; 542090at2759; -.
DR PhylomeDB; Q3B7Z2; -.
DR TreeFam; TF320922; -.
DR Reactome; R-MMU-1660661; Sphingolipid de novo biosynthesis.
DR Reactome; R-MMU-192105; Synthesis of bile acids and bile salts.
DR BioGRID-ORCS; 76303; 20 hits in 75 CRISPR screens.
DR ChiTaRS; Osbp; mouse.
DR PRO; PR:Q3B7Z2; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3B7Z2; protein.
DR Bgee; ENSMUSG00000024687; Expressed in submandibular gland and 260 other tissues.
DR Genevisible; Q3B7Z2; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0120015; F:sterol transfer activity; ISS:UniProtKB.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0035627; P:ceramide transport; ISO:MGI.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISS:UniProtKB.
DR GO; GO:0015914; P:phospholipid transport; ISO:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:1904411; P:positive regulation of secretory granule organization; ISO:MGI.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; ISO:MGI.
DR GO; GO:0015918; P:sterol transport; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR037239; OSBP_sf.
DR InterPro; IPR000648; Oxysterol-bd.
DR InterPro; IPR018494; Oxysterol-bd_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF144000; SSF144000; 1.
DR PROSITE; PS01013; OSBP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Endoplasmic reticulum; Golgi apparatus; Lipid transport; Lipid-binding;
KW Membrane; Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P22059"
FT CHAIN 2..805
FT /note="Oxysterol-binding protein 1"
FT /id="PRO_0000349262"
FT DOMAIN 86..179
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 18..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..324
FT /evidence="ECO:0000255"
FT COILED 728..759
FT /evidence="ECO:0000255"
FT MOTIF 356..362
FT /note="FFAT"
FT /evidence="ECO:0000250|UniProtKB:P22059"
FT COMPBIAS 371..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 115..120
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 312
FT /ligand="20-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:1296"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 312
FT /ligand="25-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:42977"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 312
FT /ligand="7beta-hydroxycholesterol"
FT /ligand_id="ChEBI:CHEBI:42989"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 312
FT /ligand="cholesterol"
FT /ligand_id="ChEBI:CHEBI:16113"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 312
FT /ligand="ergosterol"
FT /ligand_id="ChEBI:CHEBI:16933"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 491..494
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT BINDING 520..521
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol
FT 4-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58178"
FT /evidence="ECO:0000250|UniProtKB:P35844"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P22059"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22059"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22059"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 375
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22059"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22059"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22059"
FT VAR_SEQ 1..268
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035281"
FT VAR_SEQ 269..272
FT /note="AMIN -> MLQL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035282"
SQ SEQUENCE 805 AA; 88797 MW; 0922E5C6D660B425 CRC64;
MAATELRGVV GPGPAAIAAP GGGGAGPPAV GGGGGRGDAG PGPGVAAATA ATAGGPGPGA
GGVAAGGPGS APPAAGSGGS GAGGSGSARE GWLFKWTNYI KGYQRRWFVL SNGLLSYYRS
KAEMRHTCRG TINLATANIT VEDSCNFIIS NGGAQTYHLK ASSEVERQRW VTALELAKAK
AVKMLAESDD SGDEESVSQT DKTELQSTLR TLSSKVEDLS TCNDLIAKHG TALQRSLSEL
ESLKLPAESN EKIKQVNERA TLFRITSNAM INACRDFLML AQTHSKKWQK SLQYERDQRI
RLEETLEQLA KQHNHLERAF RGATVLPANP PGSAGSGKDQ CCSGKGDMSD EDDENEFFDA
PEIITMPENL GHKRTGSNIS GASSDVSLDE QYKHQLEETK KEKRTRIPYK PNYSLNLWSI
MKNCIGKELS KIPMPVNFNE PLSMLQRLTE DLEYHELLDR AAKCENSLEQ LCYVAAFTVS
SYSTTVFRTS KPFNPLLGET FELDRLEENG YRSICEQVSH HPPAAAHHAE SKNGWTLRQE
IKITSKFRGK YLSIMPLGTI HCIFHSTGHH YTWKKVTTTV HNIIVGKLWI DQSGEIDIVN
HKTGDKCNLK FVPYSYFSRD VARKVTGEVT DPSGKVHFAL LGTWDEKMDC FKVQAASGEN
GGDARQRGHE AEDSRVMLWK RNPLPKNAEN MYYFSELALT LNAWEGGTAP TDSRLRPDQR
LMENGRWDEA NAEKQRLEEK QRLSRKKREA EAAKATEDGT PHDPYKALWF ERKKDPVTRE
LTHIYSGEYW ECKEKQDWGS CPDIF
