OSBP2_HUMAN
ID OSBP2_HUMAN Reviewed; 916 AA.
AC Q969R2; B0QYG1; B4DK24; B4DKE4; B4DTR3; F5H2A3; O60396; Q0VF99; Q8NA37;
AC Q9BY96; Q9BZF0;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Oxysterol-binding protein 2;
DE AltName: Full=Oxysterol-binding protein-related protein 4;
DE Short=ORP-4;
DE Short=OSBP-related protein 4;
GN Name=OSBP2; Synonyms=KIAA1664, ORP4, OSBPL4;
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 [GENOMIC DNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA]
RP OF 2-916 (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11278871; DOI=10.1074/jbc.m011259200;
RA Moreira E.F., Jaworski C., Li A., Rodriguez I.R.;
RT "Molecular and biochemical characterization of a novel oxysterol-binding
RT protein (OSBP2) highly expressed in retina.";
RL J. Biol. Chem. 276:18570-18578(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11483621;
RA Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C., Staels B.,
RA Ikonen E., Olkkonen V.M.;
RT "The OSBP-related protein family in humans.";
RL J. Lipid Res. 42:1203-1213(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22 by
RT expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
RN [4]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5 AND 6).
RC TISSUE=Placenta, Testis, 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Binds 7-ketocholesterol.
CC -!- INTERACTION:
CC Q969R2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-7405817, EBI-739832;
CC Q969R2-2; Q92796: DLG3; NbExp=3; IntAct=EBI-12211505, EBI-80440;
CC Q969R2-2; Q9HD26-2: GOPC; NbExp=3; IntAct=EBI-12211505, EBI-11102276;
CC Q969R2-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-12211505, EBI-739832;
CC Q969R2-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-12211505, EBI-79165;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q969R2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969R2-2; Sequence=VSP_054520;
CC Name=3;
CC IsoId=Q969R2-3; Sequence=VSP_054886, VSP_054887, VSP_054520;
CC Name=4;
CC IsoId=Q969R2-4; Sequence=VSP_055263, VSP_054520;
CC Name=5;
CC IsoId=Q969R2-5; Sequence=VSP_055262, VSP_054520;
CC Name=6;
CC IsoId=Q969R2-6; Sequence=VSP_055751, VSP_055752;
CC -!- TISSUE SPECIFICITY: Expressed mainly in retina, testis, and fetal
CC liver. {ECO:0000269|PubMed:11278871}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK56864.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK56865.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB33334.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF288741; AAK56864.1; ALT_INIT; mRNA.
DR EMBL; AF288742; AAK56865.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF323731; AAG53406.1; -; mRNA.
DR EMBL; AB051451; BAB33334.2; ALT_INIT; mRNA.
DR EMBL; AK093196; BAC04091.1; -; mRNA.
DR EMBL; AK296525; BAG59156.1; -; mRNA.
DR EMBL; AK300323; BAG62075.1; -; mRNA.
DR EMBL; AK296354; BAG59036.1; -; mRNA.
DR EMBL; AC004542; AAC12953.1; -; Genomic_DNA.
DR EMBL; AL022336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL079299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW59916.1; -; Genomic_DNA.
DR EMBL; BC118914; AAI18915.1; -; mRNA.
DR CCDS; CCDS43002.1; -. [Q969R2-1]
DR CCDS; CCDS63446.1; -. [Q969R2-3]
DR CCDS; CCDS63448.1; -. [Q969R2-2]
DR CCDS; CCDS63449.1; -. [Q969R2-6]
DR CCDS; CCDS63450.1; -. [Q969R2-4]
DR CCDS; CCDS63451.1; -. [Q969R2-5]
DR PIR; T02435; T02435.
DR RefSeq; NP_001269667.1; NM_001282738.1. [Q969R2-3]
DR RefSeq; NP_001269668.1; NM_001282739.1. [Q969R2-2]
DR RefSeq; NP_001269669.1; NM_001282740.1. [Q969R2-4]
DR RefSeq; NP_001269670.1; NM_001282741.1. [Q969R2-6]
DR RefSeq; NP_001269671.1; NM_001282742.1. [Q969R2-5]
DR RefSeq; NP_110385.1; NM_030758.3. [Q969R2-1]
DR RefSeq; XP_016884201.1; XM_017028712.1.
DR AlphaFoldDB; Q969R2; -.
DR SMR; Q969R2; -.
DR BioGRID; 117263; 17.
DR ELM; Q969R2; -.
DR IntAct; Q969R2; 10.
DR MINT; Q969R2; -.
DR STRING; 9606.ENSP00000332576; -.
DR BindingDB; Q969R2; -.
DR GlyGen; Q969R2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q969R2; -.
DR PhosphoSitePlus; Q969R2; -.
DR BioMuta; OSBP2; -.
DR DMDM; 88984633; -.
DR EPD; Q969R2; -.
DR jPOST; Q969R2; -.
DR MassIVE; Q969R2; -.
DR MaxQB; Q969R2; -.
DR PaxDb; Q969R2; -.
DR PeptideAtlas; Q969R2; -.
DR PRIDE; Q969R2; -.
DR ProteomicsDB; 25910; -.
DR ProteomicsDB; 4454; -.
DR ProteomicsDB; 5124; -.
DR ProteomicsDB; 58834; -.
DR ProteomicsDB; 72634; -.
DR ProteomicsDB; 75819; -. [Q969R2-1]
DR Antibodypedia; 5683; 113 antibodies from 22 providers.
DR DNASU; 23762; -.
DR Ensembl; ENST00000332585.11; ENSP00000332576.6; ENSG00000184792.16. [Q969R2-1]
DR Ensembl; ENST00000401475.5; ENSP00000385254.1; ENSG00000184792.16. [Q969R2-4]
DR Ensembl; ENST00000437268.6; ENSP00000389200.2; ENSG00000184792.16. [Q969R2-6]
DR Ensembl; ENST00000438716.3; ENSP00000411052.2; ENSG00000184792.16. [Q969R2-3]
DR Ensembl; ENST00000446658.6; ENSP00000392080.2; ENSG00000184792.16. [Q969R2-2]
DR Ensembl; ENST00000535268.5; ENSP00000438713.1; ENSG00000184792.16. [Q969R2-5]
DR GeneID; 23762; -.
DR KEGG; hsa:23762; -.
DR MANE-Select; ENST00000332585.11; ENSP00000332576.6; NM_030758.4; NP_110385.1.
DR UCSC; uc003aiy.1; human. [Q969R2-1]
DR CTD; 23762; -.
DR DisGeNET; 23762; -.
DR GeneCards; OSBP2; -.
DR HGNC; HGNC:8504; OSBP2.
DR HPA; ENSG00000184792; Tissue enhanced (bone marrow, retina).
DR MIM; 606729; gene.
DR neXtProt; NX_Q969R2; -.
DR OpenTargets; ENSG00000184792; -.
DR PharmGKB; PA32823; -.
DR VEuPathDB; HostDB:ENSG00000184792; -.
DR eggNOG; KOG1737; Eukaryota.
DR GeneTree; ENSGT00940000157987; -.
DR HOGENOM; CLU_007105_6_1_1; -.
DR InParanoid; Q969R2; -.
DR OMA; AQGHKWS; -.
DR OrthoDB; 542090at2759; -.
DR PhylomeDB; Q969R2; -.
DR TreeFam; TF320922; -.
DR PathwayCommons; Q969R2; -.
DR SignaLink; Q969R2; -.
DR SIGNOR; Q969R2; -.
DR BioGRID-ORCS; 23762; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; OSBP2; human.
DR GeneWiki; OSBP2; -.
DR GenomeRNAi; 23762; -.
DR Pharos; Q969R2; Tbio.
DR PRO; PR:Q969R2; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q969R2; protein.
DR Bgee; ENSG00000184792; Expressed in buccal mucosa cell and 139 other tissues.
DR ExpressionAtlas; Q969R2; baseline and differential.
DR Genevisible; Q969R2; HS.
DR GO; GO:0097440; C:apical dendrite; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
DR GO; GO:0032934; F:sterol binding; IBA:GO_Central.
DR GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
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 Alternative splicing; Lipid transport; Lipid-binding; Membrane;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..916
FT /note="Oxysterol-binding protein 2"
FT /id="PRO_0000100366"
FT DOMAIN 182..274
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..842
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QNQ6"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..455
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055262"
FT VAR_SEQ 1..366
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055263"
FT VAR_SEQ 1..284
FT /note="MGKAAAPSRGGGCGGRSRGLSSLFTVVPCLSCHTAAPGMSASTSGSGPEPKP
FT QPQPVPEPERGPLSEQVSEAVSEAVPRSEPVSETTSEPEPGAGQPSELLQGSRPGSESS
FT SGVGAGPFTKAASEPLSRAVGSATFLRPESGSLPALKPLPLLRPGQAKTPLGVPMSGTG
FT TTSSAPLALLPLDSFEGWLLKWTNYLKGYQRRWFVLGNGLLSYYRNQGEMAHTCRGTIN
FT LSTAHIDTEDSCGILLTSGARSYHLKASSEVDRQQWITALELAKAKAVRVMNTHS ->
FT MKGRGCWDTASVRSFCSSGCLNKFKK (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055751"
FT VAR_SEQ 1..49
FT /note="MGKAAAPSRGGGCGGRSRGLSSLFTVVPCLSCHTAAPGMSASTSGSGPE ->
FT MHRQRTRTMSSLAAKRLGMNRRPAGSGGGGGEAATWGHRFWRPQERPTD (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054886"
FT VAR_SEQ 50..214
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054887"
FT VAR_SEQ 473
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_054520"
FT VAR_SEQ 869
FT /note="E -> EA (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055752"
FT VARIANT 760
FT /note="M -> V (in dbSNP:rs34240867)"
FT /id="VAR_053546"
FT CONFLICT 34
FT /note="T -> A (in Ref. 3; BAB33334)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="Q -> H (in Ref. 5; BAG59036)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 916 AA; 101266 MW; 3EAC49EB56516F18 CRC64;
MGKAAAPSRG GGCGGRSRGL SSLFTVVPCL SCHTAAPGMS ASTSGSGPEP KPQPQPVPEP
ERGPLSEQVS EAVSEAVPRS EPVSETTSEP EPGAGQPSEL LQGSRPGSES SSGVGAGPFT
KAASEPLSRA VGSATFLRPE SGSLPALKPL PLLRPGQAKT PLGVPMSGTG TTSSAPLALL
PLDSFEGWLL KWTNYLKGYQ RRWFVLGNGL LSYYRNQGEM AHTCRGTINL STAHIDTEDS
CGILLTSGAR SYHLKASSEV DRQQWITALE LAKAKAVRVM NTHSDDSGDD DEATTPADKS
ELHHTLKNLS LKLDDLSTCN DLIAKHGAAL QRSLTELDGL KIPSESGEKL KVVNERATLF
RITSNAMINA CRDFLELAEI HSRKWQRALQ YEQEQRVHLE ETIEQLAKQH NSLERAFHSA
PGRPANPSKS FIEGSLLTPK GEDSEEDEDT EYFDAMEDST SFITVITEAK EDSRKAEGST
GTSSVDWSSA DNVLDGASLV PKGSSKVKRR VRIPNKPNYS LNLWSIMKNC IGRELSRIPM
PVNFNEPLSM LQRLTEDLEY HHLLDKAVHC TSSVEQMCLV AAFSVSSYST TVHRIAKPFN
PMLGETFELD RLDDMGLRSL CEQVSHHPPS AAHYVFSKHG WSLWQEITIS SKFRGKYISI
MPLGAIHLEF QASGNHYVWR KSTSTVHNII VGKLWIDQSG DIEIVNHKTN DRCQLKFLPY
SYFSKEAARK VTGVVSDSQG KAHYVLSGSW DEQMECSKVM HSSPSSPSSD GKQKTVYQTL
SAKLLWKKYP LPENAENMYY FSELALTLNE HEEGVAPTDS RLRPDQRLME KGRWDEANTE
KQRLEEKQRL SRRRRLEACG PGSSCSSEEE KEADAYTPLW FEKRLDPLTG EMACVYKGGY
WEAKEKQDWH MCPNIF
