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 27-MAR-2024, entry version 186. 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"; 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; 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; 45. 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; 9606-ENSP00000290291; -. DR PeptideAtlas; Q9NZT2; -. DR ProteomicsDB; 83507; -. [Q9NZT2-1] DR ProteomicsDB; 83508; -. [Q9NZT2-2] DR Pumba; Q9NZT2; -. DR Antibodypedia; 14927; 201 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 AGR; HGNC:15768; -. 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; LHFAWEH; -. DR OrthoDB; 163180at2759; -. DR PhylomeDB; Q9NZT2; -. DR TreeFam; TF331377; -. DR PathwayCommons; Q9NZT2; -. DR SignaLink; Q9NZT2; -. DR BioGRID-ORCS; 11054; 109 hits in 1166 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 191 other cell types or tissues. DR ExpressionAtlas; Q9NZT2; baseline and differential. 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:SF1; OPIOID GROWTH FACTOR RECEPTOR; 1. DR PANTHER; PTHR14015; OPIOID GROWTH FACTOR RECEPTOR OGFR ZETA-TYPE OPIOID RECEPTOR; 1. DR Pfam; PF04680; OGFr_III; 7. DR Pfam; PF04664; OGFr_N; 1. DR Genevisible; Q9NZT2; HS. 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 //