ID   MGP_HUMAN               Reviewed;         103 AA.
AC   P08493; A0M8W5; B2R519; J3KMX7; Q2TU41; Q567P9; Q6ICN5;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   27-MAR-2024, entry version 210.
DE   RecName: Full=Matrix Gla protein;
DE            Short=MGP;
DE   AltName: Full=Cell growth-inhibiting gene 36 protein;
DE   Flags: Precursor;
GN   Name=MGP; Synonyms=MGLAP; ORFNames=GIG36;
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 / MRNA] (ISOFORM 1).
RX   PubMed=2394711; DOI=10.1016/s0021-9258(18)77221-9;
RA   Cancela M.L., Hsieh C.-L., Francke U., Price P.A.;
RT   "Molecular structure, chromosome assignment, and promoter organization of
RT   the human matrix Gla protein gene.";
RL   J. Biol. Chem. 265:15040-15048(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-102.
RX   PubMed=3387234; DOI=10.1093/nar/16.11.5213;
RA   Kiefer M.C., Bauer D.M., Young D., Hermsen K.M., Masiarz F.K., Barr P.J.;
RT   "The cDNA and derived amino acid sequences for human and bovine matrix Gla
RT   protein.";
RL   Nucleic Acids Res. 16:5213-5213(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-102.
RX   PubMed=2216462;
RA   Chen L., O'Bryan J.P., Smith H.S., Liu E.;
RT   "Overexpression of matrix Gla protein mRNA in malignant human breast cells:
RT   isolation by differential cDNA hybridization.";
RL   Oncogene 5:1391-1395(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kim J.W.;
RT   "Identification of a human cell growth inhibition gene.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-102.
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-102.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-102.
RC   TISSUE=Cervix;
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   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-102.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [10]
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   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-102.
RC   TISSUE=Brain;
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   [12]
RP   PHOSPHORYLATION AT SER-22; SER-25 AND SER-28.
RX   PubMed=8061611; DOI=10.1002/pro.5560030511;
RA   Price P.A., Rice J.S., Williamson M.K.;
RT   "Conserved phosphorylation of serines in the Ser-X-Glu/Ser(P) sequences of
RT   the vitamin K-dependent matrix Gla protein from shark, lamb, rat, cow, and
RT   human.";
RL   Protein Sci. 3:822-830(1994).
RN   [13]
RP   PARTIAL PROTEIN SEQUENCE, AND PROTEOLYTIC PROCESSING OF C-TERMINAL.
RX   PubMed=1939157; DOI=10.1016/s0021-9258(18)54832-8;
RA   Hale J.E., Williamson M.K., Price P.A.;
RT   "Carboxyl-terminal proteolytic processing of matrix Gla protein.";
RL   J. Biol. Chem. 266:21145-21149(1991).
RN   [14]
RP   INVOLVEMENT IN KTLS.
RX   PubMed=9916809; DOI=10.1038/5102;
RA   Munroe P.B., Olgunturk R.O., Fryns J.-P., Van Maldergem L., Ziereisen F.,
RA   Yuksel B., Gardiner R.M., Chung E.;
RT   "Mutations in the gene encoding the human matrix Gla protein cause Keutel
RT   syndrome.";
RL   Nat. Genet. 21:142-144(1999).
CC   -!- FUNCTION: Associates with the organic matrix of bone and cartilage.
CC       Thought to act as an inhibitor of bone formation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P08493-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P08493-2; Sequence=VSP_046999;
CC   -!- PTM: Requires vitamin K-dependent gamma-carboxylation for its function.
CC   -!- DISEASE: Keutel syndrome (KTLS) [MIM:245150]: An autosomal recessive
CC       disorder characterized by abnormal cartilage calcification, peripheral
CC       pulmonary stenosis neural hearing loss and midfacial hypoplasia.
CC       {ECO:0000269|PubMed:9916809}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/mgp/";
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DR   EMBL; M58549; AAB53766.1; -; mRNA.
DR   EMBL; M55270; AAB53765.1; -; Genomic_DNA.
DR   EMBL; X07362; CAA30287.1; -; mRNA.
DR   EMBL; X53331; CAA37418.1; -; mRNA.
DR   EMBL; AY542304; AAT08173.1; -; mRNA.
DR   EMBL; BT006733; AAP35379.1; -; mRNA.
DR   EMBL; CR450358; CAG29354.1; -; mRNA.
DR   EMBL; AK312029; BAG34966.1; -; mRNA.
DR   EMBL; DQ004248; AAY16978.1; -; Genomic_DNA.
DR   EMBL; AC007655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471094; EAW96333.1; -; Genomic_DNA.
DR   EMBL; BC005272; AAH05272.1; -; mRNA.
DR   EMBL; BC070314; AAH70314.1; -; mRNA.
DR   EMBL; BC093078; AAH93078.1; -; mRNA.
DR   CCDS; CCDS53752.1; -. [P08493-2]
DR   CCDS; CCDS8669.1; -. [P08493-1]
DR   PIR; A35811; GEHUM.
DR   RefSeq; NP_000891.2; NM_000900.4. [P08493-1]
DR   RefSeq; NP_001177768.1; NM_001190839.2. [P08493-2]
DR   AlphaFoldDB; P08493; -.
DR   SMR; P08493; -.
DR   BioGRID; 110412; 6.
DR   IntAct; P08493; 2.
DR   MINT; P08493; -.
DR   STRING; 9606.ENSP00000228938; -.
DR   DrugBank; DB01373; Calcium.
DR   iPTMnet; P08493; -.
DR   PhosphoSitePlus; P08493; -.
DR   BioMuta; MGP; -.
DR   DMDM; 118572668; -.
DR   CPTAC; non-CPTAC-1141; -.
DR   jPOST; P08493; -.
DR   MassIVE; P08493; -.
DR   MaxQB; P08493; -.
DR   PeptideAtlas; P08493; -.
DR   ProteomicsDB; 52112; -. [P08493-1]
DR   Antibodypedia; 2842; 349 antibodies from 30 providers.
DR   DNASU; 4256; -.
DR   Ensembl; ENST00000228938.5; ENSP00000228938.5; ENSG00000111341.10. [P08493-2]
DR   Ensembl; ENST00000539261.6; ENSP00000445907.1; ENSG00000111341.10. [P08493-1]
DR   GeneID; 4256; -.
DR   KEGG; hsa:4256; -.
DR   MANE-Select; ENST00000539261.6; ENSP00000445907.1; NM_000900.5; NP_000891.2.
DR   UCSC; uc001rcn.3; human. [P08493-1]
DR   AGR; HGNC:7060; -.
DR   CTD; 4256; -.
DR   DisGeNET; 4256; -.
DR   GeneCards; MGP; -.
DR   HGNC; HGNC:7060; MGP.
DR   HPA; ENSG00000111341; Low tissue specificity.
DR   MalaCards; MGP; -.
DR   MIM; 154870; gene.
DR   MIM; 245150; phenotype.
DR   neXtProt; NX_P08493; -.
DR   OpenTargets; ENSG00000111341; -.
DR   Orphanet; 85202; Keutel syndrome.
DR   PharmGKB; PA30790; -.
DR   VEuPathDB; HostDB:ENSG00000111341; -.
DR   GeneTree; ENSGT00390000003753; -.
DR   HOGENOM; CLU_177119_1_0_1; -.
DR   InParanoid; P08493; -.
DR   OMA; NANTFMS; -.
DR   OrthoDB; 3885479at2759; -.
DR   PhylomeDB; P08493; -.
DR   TreeFam; TF330920; -.
DR   PathwayCommons; P08493; -.
DR   SignaLink; P08493; -.
DR   BioGRID-ORCS; 4256; 13 hits in 1151 CRISPR screens.
DR   ChiTaRS; MGP; human.
DR   GeneWiki; Matrix_gla_protein; -.
DR   GenomeRNAi; 4256; -.
DR   Pharos; P08493; Tbio.
DR   PRO; PR:P08493; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P08493; Protein.
DR   Bgee; ENSG00000111341; Expressed in descending thoracic aorta and 189 other cell types or tissues.
DR   ExpressionAtlas; P08493; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
DR   GO; GO:0008147; F:structural constituent of bone; TAS:ProtInc.
DR   GO; GO:0001502; P:cartilage condensation; TAS:ProtInc.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0001503; P:ossification; TAS:ProtInc.
DR   GO; GO:0030500; P:regulation of bone mineralization; IEA:InterPro.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR027118; MGP.
DR   InterPro; IPR002384; Osteocalcin/MGP.
DR   PANTHER; PTHR10109; MATRIX GLA PROTEIN; 1.
DR   PANTHER; PTHR10109:SF0; MATRIX GLA PROTEIN; 1.
DR   PRINTS; PR00002; GLABONE.
DR   SMART; SM00069; GLA; 1.
DR   SUPFAM; SSF57630; GLA-domain; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   Genevisible; P08493; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chondrogenesis; Deafness; Developmental protein;
KW   Differentiation; Direct protein sequencing; Disulfide bond;
KW   Gamma-carboxyglutamic acid; Osteogenesis; Phosphoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT   CHAIN           20..96
FT                   /note="Matrix Gla protein"
FT                   /id="PRO_0000011109"
FT   PROPEP          97..103
FT                   /note="Removed in mature form; probably by carboxypeptidase
FT                   N"
FT                   /id="PRO_0000011110"
FT   DOMAIN          51..97
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         21
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07507,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8061611"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8061611"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:8061611"
FT   MOD_RES         56
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07507,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         60
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07507,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         67
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07507,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         71
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P07507,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   DISULFID        73..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   VAR_SEQ         20
FT                   /note="Y -> YGEWQKEENFGFDIVSVLSLNWHRAQ (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046999"
FT   VARIANT         53
FT                   /note="K -> E (in dbSNP:rs1801716)"
FT                   /id="VAR_016177"
FT   VARIANT         102
FT                   /note="T -> A (in dbSNP:rs4236)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2216462,
FT                   ECO:0000269|PubMed:3387234, ECO:0000269|Ref.5,
FT                   ECO:0000269|Ref.6, ECO:0000269|Ref.8"
FT                   /id="VAR_016178"
FT   CONFLICT        20
FT                   /note="Y -> C (in Ref. 11; AAH93078)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="R -> G (in Ref. 6; CAG29354)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   103 AA;  12353 MW;  243968D715D54549 CRC64;
     MKSLILLAIL AALAVVTLCY ESHESMESYE LNPFINRRNA NTFISPQQRW RAKVQERIRE
     RSKPVHELNR EACDDYRLCE RYAMVYGYNA AYNRYFRKRR GTK
//