OSBL3_HUMAN
ID OSBL3_HUMAN Reviewed; 887 AA.
AC Q9H4L5; A4D167; A4D168; A4D169; A4D170; A4D171; A4D172; B8ZZ79; B8ZZP0;
AC O14591; O43357; O43358; Q8N702; Q8N703; Q8N704; Q8NFH0; Q8NFH1; Q8NI12;
AC Q8NI13; Q9BZF4; Q9UED6;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Oxysterol-binding protein-related protein 3;
DE Short=ORP-3;
DE Short=OSBP-related protein 3;
GN Name=OSBPL3; Synonyms=KIAA0704, ORP3, OSBP3;
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 1A).
RX PubMed=11568019; DOI=10.1182/blood.v98.7.2279;
RA Gregorio-King C.C., Collier G.R., McMillan J.S., Waugh C.M., McLeod J.L.,
RA Collier F.M., Kirkland M.A.;
RT "ORP-3, a human oxysterol-binding protein gene differentially expressed in
RT hematopoietic cells.";
RL Blood 98:2279-2281(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
RX PubMed=11735225; DOI=10.1006/geno.2001.6663;
RA Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R.;
RT "A family of 12 human genes containing oxysterol-binding domains.";
RL Genomics 78:185-196(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 1C; 1D; 2A; 2B; 2C AND 2D),
RP AND TISSUE SPECIFICITY.
RX PubMed=12590732; DOI=10.1089/104454903321112442;
RA Collier F.M., Gregorio-King C.C., Apostolopoulos J., Walder K.,
RA Kirkland M.A.;
RT "ORP3 splice variants and their expression in human tissues and
RT hematopoietic cells.";
RL DNA Cell Biol. 22:1-9(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [5]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
RC TISSUE=Uterus;
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 [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-245 (ISOFORM 1A).
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 [11]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14593528; DOI=10.1007/s00441-003-0817-y;
RA Lehto M., Tienari J., Lehtonen S., Lehtonen E., Olkkonen V.M.;
RT "Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues:
RT the expression and intracellular localization of ORP3, ORP6, and ORP7.";
RL Cell Tissue Res. 315:39-57(2004).
RN [12]
RP FUNCTION, SUBUNIT, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, PH DOMAIN,
RP FFAT MOTIF, AND MUTAGENESIS OF LYS-60; LYS-61; LYS-71; ARG-72; GLY-97 AND
RP 451-PHE--ASP-453.
RX PubMed=16143324; DOI=10.1016/j.yexcr.2005.08.003;
RA Lehto M., Hynynen R., Karjalainen K., Kuismanen E., Hyvaerinen K.,
RA Olkkonen V.M.;
RT "Targeting of OSBP-related protein 3 (ORP3) to endoplasmic reticulum and
RT plasma membrane is controlled by multiple determinants.";
RL Exp. Cell Res. 310:445-462(2005).
RN [13]
RP FUNCTION.
RX PubMed=17428193; DOI=10.1042/bj20070176;
RA Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M., Saarinen H.,
RA Radzikowska A., Thiele C., Olkkonen V.M.;
RT "The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-
RT hydroxycholesterol in an evolutionarily conserved pocket.";
RL Biochem. J. 405:473-480(2007).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RRAS, DOMAIN PH, AND
RP PHOSPHORYLATION.
RX PubMed=18270267; DOI=10.1242/jcs.016964;
RA Lehto M., Maeyraenpaeae M.I., Pellinen T., Ihalmo P., Lehtonen S.,
RA Kovanen P.T., Groop P.H., Ivaska J., Olkkonen V.M.;
RT "The R-Ras interaction partner ORP3 regulates cell adhesion.";
RL J. Cell Sci. 121:695-705(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND SER-437, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-251; SER-304; SER-372
RP AND SER-410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-410 AND SER-437, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-372 AND SER-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-200; SER-251;
RP SER-265; SER-304; SER-309; SER-320; SER-372; SER-410; SER-425; SER-437 AND
RP SER-440, AND IDENTIFICATION BY 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).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [25]
RP FUNCTION, INTERACTION WITH VAPA, SUBCELLULAR LOCATION, DOMAIN FFAT MOTIF,
RP PHOSPHORYLATION AT SER-251; SER-265; SER-304; SER-320; SER-323; SER-371;
RP SER-372; SER-410 AND SER-437, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP MUTAGENESIS OF 162-PHE--THR-167 AND 451-PHE--ASP-453.
RX PubMed=25447204; DOI=10.1016/j.yexcr.2014.10.019;
RA Weber-Boyvat M., Kentala H., Lilja J., Vihervaara T., Hanninen R., Zhou Y.,
RA Peranen J., Nyman T.A., Ivaska J., Olkkonen V.M.;
RT "OSBP-related protein 3 (ORP3) coupling with VAMP-associated protein A
RT regulates R-Ras activity.";
RL Exp. Cell Res. 331:278-291(2015).
CC -!- FUNCTION: Phosphoinositide-binding protein which associates with both
CC cell and endoplasmic reticulum (ER) membranes (PubMed:16143324). Can
CC bind to the ER membrane protein VAPA and recruit VAPA to plasma
CC membrane sites, thus linking these intracellular compartments
CC (PubMed:25447204). The ORP3-VAPA complex stimulates RRAS signaling
CC which in turn attenuates integrin beta-1 (ITGB1) activation at the cell
CC surface (PubMed:18270267, PubMed:25447204). With VAPA, may regulate ER
CC morphology (PubMed:16143324). Has a role in regulation of the actin
CC cytoskeleton, cell polarity and cell adhesion (PubMed:18270267). Binds
CC to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3
CC (PubMed:16143324). Also binds 25-hydroxycholesterol and cholesterol
CC (PubMed:17428193). {ECO:0000269|PubMed:16143324,
CC ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:18270267,
CC ECO:0000269|PubMed:25447204}.
CC -!- SUBUNIT: Homodimer (PubMed:16143324). Interacts with RRAS
CC (PubMed:18270267). Interacts (phosphorylated form) with VAPA
CC (PubMed:16143324, PubMed:25447204). Interacts with OSBPL6 (By
CC similarity). {ECO:0000250|UniProtKB:Q9DBS9,
CC ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:18270267,
CC ECO:0000269|PubMed:25447204}.
CC -!- INTERACTION:
CC Q9H4L5; Q08AH1: ACSM1; NbExp=3; IntAct=EBI-1051317, EBI-2818055;
CC Q9H4L5; Q13895: BYSL; NbExp=3; IntAct=EBI-1051317, EBI-358049;
CC Q9H4L5; Q3B820: FAM161A; NbExp=3; IntAct=EBI-1051317, EBI-719941;
CC Q9H4L5; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-1051317, EBI-746969;
CC Q9H4L5; P60520: GABARAPL2; NbExp=3; IntAct=EBI-1051317, EBI-720116;
CC Q9H4L5; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-1051317, EBI-739832;
CC Q9H4L5; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-1051317, EBI-348259;
CC Q9H4L5; O00444: PLK4; NbExp=3; IntAct=EBI-1051317, EBI-746202;
CC Q9H4L5; Q99633: PRPF18; NbExp=3; IntAct=EBI-1051317, EBI-2798416;
CC Q9H4L5; O43395: PRPF3; NbExp=3; IntAct=EBI-1051317, EBI-744322;
CC Q9H4L5; Q86X27: RALGPS2; NbExp=3; IntAct=EBI-1051317, EBI-1050841;
CC Q9H4L5; P62913-2: RPL11; NbExp=3; IntAct=EBI-1051317, EBI-11027771;
CC Q9H4L5; Q8TDR2: STK35; NbExp=3; IntAct=EBI-1051317, EBI-18986091;
CC Q9H4L5; Q96C24: SYTL4; NbExp=3; IntAct=EBI-1051317, EBI-747142;
CC Q9H4L5; Q15560: TCEA2; NbExp=3; IntAct=EBI-1051317, EBI-710310;
CC Q9H4L5; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-1051317, EBI-11955057;
CC Q9H4L5; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-1051317, EBI-765817;
CC Q9H4L5; P19544-6: WT1; NbExp=3; IntAct=EBI-1051317, EBI-11745701;
CC Q9H4L5; Q05516: ZBTB16; NbExp=3; IntAct=EBI-1051317, EBI-711925;
CC Q9H4L5; Q96MX3: ZNF48; NbExp=3; IntAct=EBI-1051317, EBI-12006434;
CC Q9H4L5; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-1051317, EBI-10486136;
CC Q9H4L5; Q5T619: ZNF648; NbExp=3; IntAct=EBI-1051317, EBI-11985915;
CC Q9H4L5; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-1051317, EBI-5667516;
CC Q9H4L5; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-1051317, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16143324}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16143324}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:16143324}. Cell membrane
CC {ECO:0000269|PubMed:14593528, ECO:0000269|PubMed:16143324,
CC ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:25447204}; Peripheral
CC membrane protein {ECO:0000269|PubMed:14593528,
CC ECO:0000269|PubMed:16143324, ECO:0000269|PubMed:18270267,
CC ECO:0000269|PubMed:25447204}. Cell projection, filopodium tip
CC {ECO:0000269|PubMed:18270267}. Nucleus membrane
CC {ECO:0000269|PubMed:16143324}; Peripheral membrane protein
CC {ECO:0000305}. Note=Co-localizes with OSBPL6 at contact sites between
CC the plasma membrane and the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:Q9DBS9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1a;
CC IsoId=Q9H4L5-1; Sequence=Displayed;
CC Name=1b;
CC IsoId=Q9H4L5-2; Sequence=VSP_008219;
CC Name=1c;
CC IsoId=Q9H4L5-3; Sequence=VSP_008220;
CC Name=1d;
CC IsoId=Q9H4L5-4; Sequence=VSP_008219, VSP_008220;
CC Name=2a;
CC IsoId=Q9H4L5-5; Sequence=VSP_008221, VSP_008222;
CC Name=2b;
CC IsoId=Q9H4L5-6; Sequence=VSP_008219, VSP_008221, VSP_008222;
CC Name=2c;
CC IsoId=Q9H4L5-7; Sequence=VSP_008220, VSP_008221, VSP_008222;
CC Name=2d;
CC IsoId=Q9H4L5-8; Sequence=VSP_008219, VSP_008220, VSP_008221,
CC VSP_008222;
CC -!- TISSUE SPECIFICITY: Expressed in a subset of small lymphocytes (at
CC protein level). Expressed at high concentration in kidney, lymph node
CC and thymus. Expressed at moderate concentration in stomach, jejunum,
CC ileum, appendix, spleen, leukocytes, trachea, lung and thyroid gland.
CC Expressed at low concentration in whole brain, esophagus, duodenum,
CC ileocecum, colon, skeletal muscle, bone marrow, placenta and mammary
CC gland (PubMed:14593528). Isoform 1a, isoform 1b, isoform 1c and isoform
CC 1d are highly expressed in brain, bone marrow, colon, kidney, lung,
CC skeletal muscle, spleen, thymus and thyroid. Not expressed in heart and
CC liver. Isoform 2a, isoform 2b, isoform 2c and isoform 2d are expressed
CC in brain, bone marrow, kidney, skeletal muscle, spleen, thymus and
CC thyroid. Not expressed in heart, liver and lung (PubMed:12590732).
CC {ECO:0000269|PubMed:12590732, ECO:0000269|PubMed:14593528}.
CC -!- DEVELOPMENTAL STAGE: Expressed in several fetal tissues including
CC kidney, thymus, spleen and lung. {ECO:0000269|PubMed:14593528}.
CC -!- DOMAIN: The FFAT 2 motif is required for interaction with VAPA and
CC regulation of the endoplasmic reticulum targeting of ORP3. The FFAT 1
CC motif may contribute to VAPA binding. {ECO:0000269|PubMed:16143324,
CC ECO:0000269|PubMed:25447204}.
CC -!- DOMAIN: The PH domain binds phosphoinositides, with a preference for
CC PI(3,4)P2 and PI(3,4,5)P3. The PH domain mediates targeting to the
CC plasma membrane (PubMed:18270267). {ECO:0000269|PubMed:16143324,
CC ECO:0000269|PubMed:18270267}.
CC -!- PTM: Phosphorylation is enhanced in vitro by phorbol-12-myristate-13-
CC acetate (PMA), forskolin and calcium ionophore A23187
CC (PubMed:25447204). Phosphorylation seems to be stimulated in conditions
CC of low cell-cell (or cell-matrix) adhesion (PubMed:18270267).
CC {ECO:0000269|PubMed:18270267, ECO:0000269|PubMed:25447204}.
CC -!- MISCELLANEOUS: [Isoform 2a]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2b]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2c]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2d]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31679.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY008372; AAG23400.1; -; mRNA.
DR EMBL; AF392444; AAL40657.1; -; mRNA.
DR EMBL; AF491781; AAM27386.1; -; mRNA.
DR EMBL; AF491782; AAM27387.1; -; mRNA.
DR EMBL; AF491783; AAM27388.1; -; mRNA.
DR EMBL; AF491784; AAM27389.1; -; mRNA.
DR EMBL; AF491785; AAM27390.1; -; mRNA.
DR EMBL; AF491786; AAM27391.1; -; mRNA.
DR EMBL; AF515639; AAM74165.1; -; mRNA.
DR EMBL; AF515640; AAM74166.1; -; mRNA.
DR EMBL; AB014604; BAA31679.2; ALT_INIT; mRNA.
DR EMBL; AC003093; AAB83939.1; -; Genomic_DNA.
DR EMBL; AC004008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004016; AAC26986.2; -; Genomic_DNA.
DR EMBL; AC004239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236948; EAL24240.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24241.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24242.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24243.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24244.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24245.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93816.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93817.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93818.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93819.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93820.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93821.1; -; Genomic_DNA.
DR EMBL; BC017731; AAH17731.1; -; mRNA.
DR EMBL; AF323727; AAG53408.1; -; mRNA.
DR CCDS; CCDS47564.1; -. [Q9H4L5-4]
DR CCDS; CCDS5390.1; -. [Q9H4L5-1]
DR CCDS; CCDS5391.1; -. [Q9H4L5-2]
DR CCDS; CCDS5392.1; -. [Q9H4L5-3]
DR RefSeq; NP_056365.1; NM_015550.3. [Q9H4L5-1]
DR RefSeq; NP_663160.1; NM_145320.2. [Q9H4L5-2]
DR RefSeq; NP_663161.1; NM_145321.2. [Q9H4L5-3]
DR RefSeq; NP_663162.1; NM_145322.2. [Q9H4L5-4]
DR RefSeq; XP_005249755.1; XM_005249698.3. [Q9H4L5-1]
DR RefSeq; XP_006715744.1; XM_006715681.3. [Q9H4L5-2]
DR RefSeq; XP_006715745.1; XM_006715682.3. [Q9H4L5-3]
DR RefSeq; XP_006715746.1; XM_006715683.3. [Q9H4L5-4]
DR RefSeq; XP_011513560.1; XM_011515258.2. [Q9H4L5-1]
DR PDB; 7CYZ; X-ray; 2.10 A; A/B=511-887.
DR PDB; 7DEI; X-ray; 2.60 A; A/B=504-887.
DR PDB; 7DEJ; X-ray; 2.70 A; A/B=504-887.
DR PDBsum; 7CYZ; -.
DR PDBsum; 7DEI; -.
DR PDBsum; 7DEJ; -.
DR AlphaFoldDB; Q9H4L5; -.
DR SMR; Q9H4L5; -.
DR BioGRID; 117497; 113.
DR ELM; Q9H4L5; -.
DR IntAct; Q9H4L5; 57.
DR MINT; Q9H4L5; -.
DR STRING; 9606.ENSP00000315410; -.
DR iPTMnet; Q9H4L5; -.
DR PhosphoSitePlus; Q9H4L5; -.
DR BioMuta; OSBPL3; -.
DR DMDM; 20139176; -.
DR EPD; Q9H4L5; -.
DR jPOST; Q9H4L5; -.
DR MassIVE; Q9H4L5; -.
DR MaxQB; Q9H4L5; -.
DR PaxDb; Q9H4L5; -.
DR PeptideAtlas; Q9H4L5; -.
DR PRIDE; Q9H4L5; -.
DR ProteomicsDB; 80852; -. [Q9H4L5-1]
DR ProteomicsDB; 80853; -. [Q9H4L5-2]
DR ProteomicsDB; 80854; -. [Q9H4L5-3]
DR ProteomicsDB; 80855; -. [Q9H4L5-4]
DR ProteomicsDB; 80856; -. [Q9H4L5-5]
DR ProteomicsDB; 80857; -. [Q9H4L5-6]
DR ProteomicsDB; 80858; -. [Q9H4L5-7]
DR ProteomicsDB; 80859; -. [Q9H4L5-8]
DR Antibodypedia; 12224; 118 antibodies from 26 providers.
DR DNASU; 26031; -.
DR Ensembl; ENST00000313367.7; ENSP00000315410.2; ENSG00000070882.13. [Q9H4L5-1]
DR Ensembl; ENST00000396429.5; ENSP00000379706.1; ENSG00000070882.13. [Q9H4L5-3]
DR Ensembl; ENST00000396431.5; ENSP00000379708.1; ENSG00000070882.13. [Q9H4L5-2]
DR Ensembl; ENST00000409069.5; ENSP00000386953.1; ENSG00000070882.13. [Q9H4L5-4]
DR Ensembl; ENST00000409452.5; ENSP00000386801.1; ENSG00000070882.13. [Q9H4L5-5]
DR Ensembl; ENST00000409555.5; ENSP00000386990.1; ENSG00000070882.13. [Q9H4L5-8]
DR Ensembl; ENST00000409759.5; ENSP00000386325.1; ENSG00000070882.13. [Q9H4L5-7]
DR Ensembl; ENST00000409863.5; ENSP00000386429.1; ENSG00000070882.13. [Q9H4L5-6]
DR GeneID; 26031; -.
DR KEGG; hsa:26031; -.
DR MANE-Select; ENST00000313367.7; ENSP00000315410.2; NM_015550.4; NP_056365.1.
DR UCSC; uc003sxf.5; human. [Q9H4L5-1]
DR CTD; 26031; -.
DR DisGeNET; 26031; -.
DR GeneCards; OSBPL3; -.
DR HGNC; HGNC:16370; OSBPL3.
DR HPA; ENSG00000070882; Low tissue specificity.
DR MIM; 606732; gene.
DR neXtProt; NX_Q9H4L5; -.
DR OpenTargets; ENSG00000070882; -.
DR PharmGKB; PA32828; -.
DR VEuPathDB; HostDB:ENSG00000070882; -.
DR eggNOG; KOG1737; Eukaryota.
DR GeneTree; ENSGT00940000155957; -.
DR HOGENOM; CLU_007105_4_1_1; -.
DR InParanoid; Q9H4L5; -.
DR OMA; LPAXAKY; -.
DR OrthoDB; 542090at2759; -.
DR PhylomeDB; Q9H4L5; -.
DR TreeFam; TF320922; -.
DR PathwayCommons; Q9H4L5; -.
DR Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
DR SignaLink; Q9H4L5; -.
DR BioGRID-ORCS; 26031; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; OSBPL3; human.
DR GeneWiki; OSBPL3; -.
DR GenomeRNAi; 26031; -.
DR Pharos; Q9H4L5; Tbio.
DR PRO; PR:Q9H4L5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9H4L5; protein.
DR Bgee; ENSG00000070882; Expressed in bronchial epithelial cell and 159 other tissues.
DR ExpressionAtlas; Q9H4L5; baseline and differential.
DR Genevisible; Q9H4L5; HS.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032433; C:filopodium tip; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:BHF-UCL.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
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:0006699; P:bile acid biosynthetic process; TAS:Reactome.
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; IPR041680; PH_8.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10972; PTHR10972; 1.
DR Pfam; PF01237; Oxysterol_BP; 1.
DR Pfam; PF15409; PH_8; 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 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Endoplasmic reticulum; Lipid transport; Lipid-binding; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..887
FT /note="Oxysterol-binding protein-related protein 3"
FT /id="PRO_0000100371"
FT DOMAIN 51..146
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 161..167
FT /note="FFAT 1"
FT /evidence="ECO:0000269|PubMed:25447204"
FT MOTIF 450..454
FT /note="FFAT 2"
FT /evidence="ECO:0000269|PubMed:25447204"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25447204,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25447204,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25447204,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25447204"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25447204"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25447204,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25447204,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:25447204,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 259..289
FT /note="Missing (in isoform 1b, isoform 1d, isoform 2b and
FT isoform 2d)"
FT /evidence="ECO:0000303|PubMed:12590732"
FT /id="VSP_008219"
FT VAR_SEQ 387..422
FT /note="Missing (in isoform 1c, isoform 1d, isoform 2c and
FT isoform 2d)"
FT /evidence="ECO:0000303|PubMed:12590732"
FT /id="VSP_008220"
FT VAR_SEQ 584..631
FT /note="YVAAFAISAYASSYYRAGSKPFNPVLGETYECIREDKGFQFFSEQVSH ->
FT RSQPSLATVQPRSPSHEAIHGAHQRDSPCSLRFHFDCSVNRFITQSCLASSAWLFPVTL
FT (in isoform 2a, isoform 2b, isoform 2c and isoform 2d)"
FT /evidence="ECO:0000303|PubMed:12590732"
FT /id="VSP_008221"
FT VAR_SEQ 632..887
FT /note="Missing (in isoform 2a, isoform 2b, isoform 2c and
FT isoform 2d)"
FT /evidence="ECO:0000303|PubMed:12590732"
FT /id="VSP_008222"
FT VARIANT 354
FT /note="M -> V (in dbSNP:rs11768296)"
FT /id="VAR_053548"
FT MUTAGEN 60
FT /note="K->I: Abolishes plasma membrane targeting and
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:16143324"
FT MUTAGEN 61
FT /note="K->A: Abolishes plasma membrane targeting and
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:16143324"
FT MUTAGEN 71
FT /note="K->A: Abolishes plasma membrane targeting and
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:16143324"
FT MUTAGEN 72
FT /note="R->I: Abolishes plasma membrane targeting and
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:16143324"
FT MUTAGEN 97
FT /note="G->E: Decreases plasma membrane targeting and
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:16143324"
FT MUTAGEN 162..167
FT /note="FFSGST->AAAAAA: No effect on interaction with VAPA."
FT /evidence="ECO:0000269|PubMed:25447204"
FT MUTAGEN 451..453
FT /note="FFD->VVV: Reduces VAPA binding. Abolishes
FT association with endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:16143324,
FT ECO:0000269|PubMed:25447204"
FT HELIX 525..533
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 540..542
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 550..554
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 555..561
FT /evidence="ECO:0007829|PDB:7CYZ"
FT TURN 562..566
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 567..572
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 578..591
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 592..598
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 612..617
FT /evidence="ECO:0007829|PDB:7CYZ"
FT TURN 618..621
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 622..630
FT /evidence="ECO:0007829|PDB:7CYZ"
FT TURN 631..634
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 635..644
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 646..658
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 661..667
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 669..674
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 679..684
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 687..691
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 693..697
FT /evidence="ECO:0007829|PDB:7DEJ"
FT STRAND 699..710
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 716..722
FT /evidence="ECO:0007829|PDB:7CYZ"
FT TURN 730..733
FT /evidence="ECO:0007829|PDB:7DEI"
FT STRAND 734..741
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 746..753
FT /evidence="ECO:0007829|PDB:7CYZ"
FT TURN 754..756
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 757..761
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:7DEJ"
FT STRAND 766..771
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 779..782
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 787..792
FT /evidence="ECO:0007829|PDB:7CYZ"
FT TURN 797..799
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 800..802
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 808..810
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 812..818
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 822..845
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 853..857
FT /evidence="ECO:0007829|PDB:7CYZ"
FT STRAND 863..865
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 869..874
FT /evidence="ECO:0007829|PDB:7CYZ"
FT HELIX 878..880
FT /evidence="ECO:0007829|PDB:7CYZ"
SQ SEQUENCE 887 AA; 101224 MW; 12E16912BD3F2E99 CRC64;
MMSDEKNLGV SQKLVSPSRS TSSCSSKQGS RQDSWEVVEG LRGEMNYTQE PPVQKGFLLK
KRKWPLKGWH KRFFYLDKGI LKYAKSQTDI EREKLHGCID VGLSVMSVKK SSKCIDLDTE
EHIYHLKVKS EEVFDEWVSK LRHHRMYRQN EIAMFPHEVN HFFSGSTITD SSSGVFDSIS
SRKRSSISKQ NLFQTGSNVS FSCGGETRVP LWLQSSEDME KCSKDLAHCH AYLVEMSQLL
QSMDVLHRTY SAPAINAIQG GSFESPKKEK RSHRRWRSRA IGKDAKGTLQ VPKPFSGPVR
LHSSNPNLST LDFGEEKNYS DGSETSSEFS KMQEDLCHIA HKVYFTLRSA FNIMSAEREK
LKQLMEQDAS SSPSAQVIGL KNALSSALAQ NTDLKERLRR IHAESLLLDS PAVAKSGDNL
AEENSRDENR ALVHQLSNES RLSITDSLSE FFDAQEVLLS PSSSENEISD DDSYVSDISD
NLSLDNLSND LDNERQTLGP VLDSGREAKS RRRTCLPAPC PSSSNISLWN ILRNNIGKDL
SKVAMPVELN EPLNTLQRLC EELEYSELLD KAAQIPSPLE RMVYVAAFAI SAYASSYYRA
GSKPFNPVLG ETYECIREDK GFQFFSEQVS HHPPISACHA ESRNFVFWQD VRWKNKFWGK
SMEIVPIGTT HVTLPVFGDH FEWNKVTSCI HNILSGQRWI EHYGEIVIKN LHDDSCYCKV
NFIKAKYWST NAHEIEGTVF DRSGKAVHRL FGKWHESIYC GGGSSSACVW RANPMPKGYE
QYYSFTQFAL ELNEMDPSSK SLLPPTDTRF RPDQRFLEEG NLEEAEIQKQ RIEQLQRERR
RVLEENHVEH QPRFFRKSDD DSWVSNGTYL ELRKDLGFSK LDHPVLW
