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OGFR_HUMAN
ID   OGFR_HUMAN              Reviewed;         677 AA.
AC   Q9NZT2; O96029; Q4VXW5; Q96CM2; Q9BQW1; Q9H4H0; Q9H7J5; Q9NZT3; Q9NZT4;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 3.
DT   03-AUG-2022, entry version 177.
DE   RecName: Full=Opioid growth factor receptor;
DE            Short=OGFr;
DE   AltName: Full=Protein 7-60;
DE   AltName: Full=Zeta-type opioid receptor;
GN   Name=OGFR;
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] (ISOFORMS 1 AND 2), AND VARIANT THR-577.
RC   TISSUE=Placenta;
RX   PubMed=10677613; DOI=10.1016/s0006-8993(99)02330-6;
RA   Zagon I.S., Verderame M.F., Allen S.S., McLaughlin P.J.;
RT   "Cloning, sequencing, chromosomal location, and function of cDNAs encoding
RT   an opioid growth factor receptor (OGFr) in humans.";
RL   Brain Res. 856:75-83(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT THR-577.
RA   Takanosu M., Liu J., Mayne R., Wood B.M., Brewton R.G.;
RT   "Genomic structure of human gene 7-60.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Skin;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-677 (ISOFORM 1), AND VARIANT
RP   THR-577.
RC   TISSUE=Spleen;
RX   PubMed=11214971; DOI=10.1093/dnares/7.6.357;
RA   Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
RT   "Characterization of long cDNA clones from human adult spleen.";
RL   DNA Res. 7:357-366(2000).
RN   [6]
RP   REVIEW.
RX   PubMed=11890982; DOI=10.1016/s0165-0173(01)00160-6;
RA   Zagon I.S., Verderame M.F., McLaughlin P.J.;
RT   "The biology of the opioid growth factor receptor (OGFr).";
RL   Brain Res. Brain Res. Rev. 38:351-376(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE 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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT   and fractionation of phosphopeptides with strong anion exchange
RT   chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND IDENTIFICATION BY
RP   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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-361; SER-378;
RP   SER-484; SER-537; SER-557 AND SER-617, AND IDENTIFICATION BY MASS
RP   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   [16]
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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-378, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-315; SER-349;
RP   SER-361; SER-378; SER-382; SER-403 AND SER-484, AND IDENTIFICATION BY MASS
RP   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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-378, AND
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).
CC   -!- FUNCTION: Receptor for opioid growth factor (OGF), also known as Met-
CC       enkephalin. Seems to be involved in growth regulation.
CC   -!- INTERACTION:
CC       Q9NZT2; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-1044212, EBI-750109;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Note=The OGF/OGFR complex is probably translocated to the nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NZT2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NZT2-2; Sequence=VSP_004060;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the heart and liver, moderately
CC       in skeletal muscle and kidney and to a lesser extent in brain and
CC       pancreas. Expressed in fetal tissues including liver and kidney.
CC   -!- SIMILARITY: Belongs to the opioid growth factor receptor family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD03737.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAD03745.1; Type=Frameshift; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=OGFr entry;
CC       URL="https://en.wikipedia.org/wiki/OGFr";
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DR   EMBL; AF172451; AAF64404.1; -; mRNA.
DR   EMBL; AF172452; AAF64405.1; -; mRNA.
DR   EMBL; AF172453; AAF64406.1; -; mRNA.
DR   EMBL; AF112980; AAD03745.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AF109134; AAD03737.1; ALT_FRAME; mRNA.
DR   EMBL; AL035669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014137; AAH14137.1; -; mRNA.
DR   EMBL; AK024485; BAB15775.1; -; mRNA.
DR   CCDS; CCDS13504.1; -. [Q9NZT2-1]
DR   RefSeq; NP_031372.2; NM_007346.3. [Q9NZT2-1]
DR   AlphaFoldDB; Q9NZT2; -.
DR   BioGRID; 116239; 35.
DR   IntAct; Q9NZT2; 7.
DR   MINT; Q9NZT2; -.
DR   STRING; 9606.ENSP00000290291; -.
DR   ChEMBL; CHEMBL4105797; -.
DR   GlyGen; Q9NZT2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9NZT2; -.
DR   PhosphoSitePlus; Q9NZT2; -.
DR   SwissPalm; Q9NZT2; -.
DR   BioMuta; OGFR; -.
DR   DMDM; 146331047; -.
DR   EPD; Q9NZT2; -.
DR   jPOST; Q9NZT2; -.
DR   MassIVE; Q9NZT2; -.
DR   MaxQB; Q9NZT2; -.
DR   PaxDb; Q9NZT2; -.
DR   PeptideAtlas; Q9NZT2; -.
DR   PRIDE; Q9NZT2; -.
DR   ProteomicsDB; 83507; -. [Q9NZT2-1]
DR   ProteomicsDB; 83508; -. [Q9NZT2-2]
DR   Antibodypedia; 14927; 176 antibodies from 28 providers.
DR   DNASU; 11054; -.
DR   Ensembl; ENST00000290291.10; ENSP00000290291.6; ENSG00000060491.17. [Q9NZT2-1]
DR   GeneID; 11054; -.
DR   KEGG; hsa:11054; -.
DR   MANE-Select; ENST00000290291.10; ENSP00000290291.6; NM_007346.4; NP_031372.2.
DR   UCSC; uc002ydj.4; human. [Q9NZT2-1]
DR   CTD; 11054; -.
DR   DisGeNET; 11054; -.
DR   GeneCards; OGFR; -.
DR   HGNC; HGNC:15768; OGFR.
DR   HPA; ENSG00000060491; Low tissue specificity.
DR   MIM; 606459; gene.
DR   neXtProt; NX_Q9NZT2; -.
DR   OpenTargets; ENSG00000060491; -.
DR   PharmGKB; PA31911; -.
DR   VEuPathDB; HostDB:ENSG00000060491; -.
DR   eggNOG; ENOG502QVIF; Eukaryota.
DR   GeneTree; ENSGT00390000018730; -.
DR   HOGENOM; CLU_025735_1_0_1; -.
DR   InParanoid; Q9NZT2; -.
DR   OMA; TRNWRAM; -.
DR   OrthoDB; 1450738at2759; -.
DR   PhylomeDB; Q9NZT2; -.
DR   TreeFam; TF331377; -.
DR   PathwayCommons; Q9NZT2; -.
DR   SignaLink; Q9NZT2; -.
DR   BioGRID-ORCS; 11054; 105 hits in 1088 CRISPR screens.
DR   ChiTaRS; OGFR; human.
DR   GeneWiki; OGFr; -.
DR   GenomeRNAi; 11054; -.
DR   Pharos; Q9NZT2; Tbio.
DR   PRO; PR:Q9NZT2; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9NZT2; protein.
DR   Bgee; ENSG00000060491; Expressed in granulocyte and 189 other tissues.
DR   ExpressionAtlas; Q9NZT2; baseline and differential.
DR   Genevisible; Q9NZT2; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140625; F:opioid growth factor receptor activity; IEA:InterPro.
DR   GO; GO:0001558; P:regulation of cell growth; NAS:UniProtKB.
DR   InterPro; IPR006757; OGF_rcpt.
DR   InterPro; IPR006770; OGF_rcpt_rpt.
DR   InterPro; IPR039574; OGFr.
DR   PANTHER; PTHR14015; PTHR14015; 1.
DR   Pfam; PF04680; OGFr_III; 7.
DR   Pfam; PF04664; OGFr_N; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Growth regulation; Nucleus;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat.
FT   CHAIN           1..677
FT                   /note="Opioid growth factor receptor"
FT                   /id="PRO_0000058030"
FT   REPEAT          517..536
FT                   /note="1"
FT   REPEAT          537..556
FT                   /note="2"
FT   REPEAT          557..576
FT                   /note="3"
FT   REPEAT          577..596
FT                   /note="4"
FT   REPEAT          597..616
FT                   /note="5"
FT   REPEAT          617..636
FT                   /note="6"
FT   REPEAT          637..656
FT                   /note="7"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..656
FT                   /note="7 X 20 AA approximate tandem repeats of [ST]-P-S-E-
FT                   T-P-G-P-[SR]-P-A-G-P-[AT]-[GR]-D-E-P-A-[EK]"
FT   MOTIF           267..283
FT                   /note="Bipartite nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..44
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..531
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         299
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         361
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         378
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18318008,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         403
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         420
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   MOD_RES         484
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         557
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         617
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         637
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99PG2"
FT   VAR_SEQ         558..577
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10677613,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_004060"
FT   VARIANT         545
FT                   /note="R -> S (in dbSNP:rs6122313)"
FT                   /id="VAR_059706"
FT   VARIANT         577
FT                   /note="S -> T (in dbSNP:rs6122315)"
FT                   /evidence="ECO:0000269|PubMed:10677613,
FT                   ECO:0000269|PubMed:11214971, ECO:0000269|Ref.2"
FT                   /id="VAR_030011"
FT   CONFLICT        27..28
FT                   /note="DG -> EA (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        37..80
FT                   /note="DAGDEDEESEEPRAARPSSFQSRMTGSRNWRATRDMCRYRHNYP -> GARR
FT                   ALGVLGQPGGLQMRLPERHGGPQGSLCLMDPCCPLSLALQ (in Ref. 5)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50..52
FT                   /note="AAR -> GPE (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172
FT                   /note="E -> A (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        220..221
FT                   /note="LG -> PC (in Ref. 1; AAF64404/AAF64405)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        224
FT                   /note="G -> S (in Ref. 1; AAF64404/AAF64405/AAF64406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="T -> S (in Ref. 2; AAD03745/AAD03737)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="R -> G (in Ref. 2; AAD03745/AAD03737)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        331
FT                   /note="G -> E (in Ref. 1; AAF64406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="E -> G (in Ref. 1; AAF64406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        465
FT                   /note="A -> T (in Ref. 1; AAF64406)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        535
FT                   /note="A -> AKTPSETPGPSPAGPTRDEPA (in Ref. 1; AAF64405)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        564
FT                   /note="P -> L (in Ref. 1; AAF64404)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        576
FT                   /note="E -> K (in Ref. 1; AAF64406, 2 and 5; BAB15775)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        577
FT                   /note="S -> I (in Ref. 1; AAF64406)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   677 AA;  73325 MW;  D4DD6AF86291B663 CRC64;
     MDDPDCDSTW EEDEEDAEDA EDEDCEDGEA AGARDADAGD EDEESEEPRA ARPSSFQSRM
     TGSRNWRATR DMCRYRHNYP DLVERDCNGD TPNLSFYRNE IRFLPNGCFI EDILQNWTDN
     YDLLEDNHSY IQWLFPLREP GVNWHAKPLT LREVEVFKSS QEIQERLVRA YELMLGFYGI
     RLEDRGTGTV GRAQNYQKRF QNLNWRSHNN LRITRILKSL GELGLEHFQA PLVRFFLEET
     LVRRELPGVR QSALDYFMFA VRCRHQRRQL VHFAWEHFRP RCKFVWGPQD KLRRFKPSSL
     PHPLEGSRKV EEEGSPGDPD HEASTQGRTC GPEHSKGGGR VDEGPQPRSV EPQDAGPLER
     SQGDEAGGHG EDRPEPLSPK ESKKRKLELS RREQPPTEPG PQSASEVEKI ALNLEGCALS
     QGSLRTGTQE VGGQDPGEAV QPCRQPLGAR VADKVRKRRK VDEGAGDSAA VASGGAQTLA
     LAGSPAPSGH PKAGHSENGV EEDTEGRTGP KEGTPGSPSE TPGPSPAGPA GDEPAESPSE
     TPGPRPAGPA GDEPAESPSE TPGPRPAGPA GDEPAESPSE TPGPSPAGPT RDEPAESPSE
     TPGPRPAGPA GDEPAESPSE TPGPRPAGPA GDEPAESPSE TPGPSPAGPT RDEPAKAGEA
     AELQDAEVES SAKSGKP
 
 
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