JMY_HUMAN
ID JMY_HUMAN Reviewed; 988 AA.
AC Q8N9B5; A1L4P5; B5MDS2; B5MDT0;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Junction-mediating and -regulatory protein;
GN Name=JMY;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-364.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-988 (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 351-988 (ISOFORM 1), AND VARIANT
RP LEU-364.
RC TISSUE=Substantia nigra;
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 [5]
RP INDUCTION.
RX PubMed=15706352; DOI=10.1038/sj.cdd.4401575;
RA Hershko T., Chaussepied M., Oren M., Ginsberg D.;
RT "Novel link between E2F and p53: proapoptotic cofactors of p53 are
RT transcriptionally upregulated by E2F.";
RL Cell Death Differ. 12:377-383(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974, 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 [7]
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=19287377; DOI=10.1038/ncb1852;
RA Zuchero J.B., Coutts A.S., Quinlan M.E., Thangue N.B., Mullins R.D.;
RT "p53-cofactor JMY is a multifunctional actin nucleation factor.";
RL Nat. Cell Biol. 11:451-459(2009).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-121 AND SER-713, AND
RP 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 [11]
RP FUNCTION, INTERACTION WITH TTC5 AND MAP1LC3B, SUBCELLULAR LOCATION, AND
RP DOMAIN.
RX PubMed=30420355; DOI=10.1083/jcb.201802157;
RA Hu X., Mullins R.D.;
RT "LC3 and STRAP regulate actin filament assembly by JMY during autophagosome
RT formation.";
RL J. Cell Biol. 218:251-266(2019).
CC -!- FUNCTION: Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic
CC regulator of actin dynamics depending on conditions (PubMed:30420355).
CC In nucleus, acts as a cofactor that increases p53/TP53 response via its
CC interaction with p300/EP300. Increases p53/TP53-dependent transcription
CC and apoptosis, suggesting an important role in p53/TP53 stress response
CC such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor
CC for both branched and unbranched actin filaments (PubMed:30420355).
CC Activates the Arp2/3 complex to induce branched actin filament
CC networks. Also catalyzes actin polymerization in the absence of Arp2/3,
CC creating unbranched filaments (PubMed:30420355). Contributes to cell
CC motility by controlling actin dynamics. May promote the rapid formation
CC of a branched actin network by first nucleating new mother filaments
CC and then activating Arp2/3 to branch off these filaments. Upon nutrient
CC stress, directly recruited by MAP1LC3B to the phagophore membrane
CC surfaces to promote actin assembly during autophagy (PubMed:30420355).
CC The p53/TP53-cofactor and actin activator activities are regulated via
CC its subcellular location (By similarity).
CC {ECO:0000250|UniProtKB:Q9QXM1, ECO:0000269|PubMed:30420355}.
CC -!- SUBUNIT: Interacts with p300/EP300, the complex activates p53/TP53
CC transcriptional activity. Interacts with TTC5; the interaction
CC facilitates the association between JMY and p300/EP300 (By similarity).
CC Interacts with MAP1LC3B; the interaction results in the activation of
CC JYM's nucleation activity in the cytoplasm (PubMed:30420355). Interacts
CC with TTC5/STRAP; the interaction results in the inhibition of JYM's
CC nucleation activity in the cytoplasm due to competition with MAP1LC3B
CC binding (PubMed:30420355). {ECO:0000250|UniProtKB:Q9QXM1,
CC ECO:0000269|PubMed:30420355}.
CC -!- INTERACTION:
CC Q8N9B5; Q00987: MDM2; NbExp=2; IntAct=EBI-866435, EBI-389668;
CC Q8N9B5-2; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-10268138, EBI-10171416;
CC Q8N9B5-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-10268138, EBI-5916454;
CC Q8N9B5-2; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-10268138, EBI-11522433;
CC Q8N9B5-2; Q5RL73: RBM48; NbExp=3; IntAct=EBI-10268138, EBI-473821;
CC Q8N9B5-2; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-10268138, EBI-726876;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QXM1}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:30420355}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:19287377,
CC ECO:0000269|PubMed:30420355}. Endomembrane system; Lipid-anchor.
CC Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:30420355}. Note=Localizes to the nucleus in most
CC cell types. Accumulates in nucleus under DNA damage conditions,
CC increasing p53/TP53 transcription response and reducing its influence
CC on cell motility (By similarity). In primary neutrophils, it
CC colocalizes with actin filaments at the leading edge and is excluded
CC from the nucleus. Localization correlates with motility, because it
CC moves from the nucleus to the cytoplasmic compartment when cells are
CC differentiated from nonmotile cells into highly motile neutrophil-like
CC cells. Localizes to cytoplasmic vesicles which associate with actin
CC filament and autophagosomal membranes upon starvation-induced autophagy
CC (PubMed:30420355). {ECO:0000250, ECO:0000269|PubMed:30420355}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N9B5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N9B5-2; Sequence=VSP_032310;
CC -!- INDUCTION: By E2F. {ECO:0000269|PubMed:15706352}.
CC -!- DOMAIN: The N-terminal region is involved in actin binding and actin
CC nucleation activity. {ECO:0000269|PubMed:30420355}.
CC -!- PTM: Ubiquitinated by MDM2, leading to its subsequent degradation by
CC the proteasome. In case of DNA damage, the interaction with MDM2 is
CC altered, preventing degradation and allowing interaction with
CC p300/EP300 and its function in p53/TP53 stress response (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the JMY family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI30625.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC04495.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAW95834.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC016559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471084; EAW95834.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC130624; AAI30625.1; ALT_INIT; mRNA.
DR EMBL; AK095189; BAC04495.1; ALT_INIT; mRNA.
DR CCDS; CCDS4047.3; -. [Q8N9B5-1]
DR RefSeq; NP_689618.4; NM_152405.4. [Q8N9B5-1]
DR AlphaFoldDB; Q8N9B5; -.
DR BioGRID; 126372; 41.
DR IntAct; Q8N9B5; 19.
DR MINT; Q8N9B5; -.
DR STRING; 9606.ENSP00000379441; -.
DR GlyGen; Q8N9B5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N9B5; -.
DR PhosphoSitePlus; Q8N9B5; -.
DR BioMuta; JMY; -.
DR DMDM; 172045777; -.
DR EPD; Q8N9B5; -.
DR jPOST; Q8N9B5; -.
DR MassIVE; Q8N9B5; -.
DR MaxQB; Q8N9B5; -.
DR PaxDb; Q8N9B5; -.
DR PeptideAtlas; Q8N9B5; -.
DR PRIDE; Q8N9B5; -.
DR ProteomicsDB; 72518; -. [Q8N9B5-1]
DR ProteomicsDB; 72519; -. [Q8N9B5-2]
DR Antibodypedia; 24555; 265 antibodies from 30 providers.
DR DNASU; 133746; -.
DR Ensembl; ENST00000396137.5; ENSP00000379441.4; ENSG00000152409.9. [Q8N9B5-1]
DR GeneID; 133746; -.
DR KEGG; hsa:133746; -.
DR MANE-Select; ENST00000396137.5; ENSP00000379441.4; NM_152405.5; NP_689618.4.
DR UCSC; uc003kfx.5; human. [Q8N9B5-1]
DR CTD; 133746; -.
DR DisGeNET; 133746; -.
DR GeneCards; JMY; -.
DR HGNC; HGNC:28916; JMY.
DR HPA; ENSG00000152409; Low tissue specificity.
DR MIM; 604279; gene.
DR neXtProt; NX_Q8N9B5; -.
DR OpenTargets; ENSG00000152409; -.
DR PharmGKB; PA164721124; -.
DR VEuPathDB; HostDB:ENSG00000152409; -.
DR eggNOG; ENOG502QRHU; Eukaryota.
DR GeneTree; ENSGT00510000046704; -.
DR HOGENOM; CLU_012316_0_0_1; -.
DR InParanoid; Q8N9B5; -.
DR OMA; PREDQCD; -.
DR OrthoDB; 183925at2759; -.
DR PhylomeDB; Q8N9B5; -.
DR TreeFam; TF331023; -.
DR PathwayCommons; Q8N9B5; -.
DR Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
DR SignaLink; Q8N9B5; -.
DR SIGNOR; Q8N9B5; -.
DR BioGRID-ORCS; 133746; 10 hits in 1080 CRISPR screens.
DR ChiTaRS; JMY; human.
DR GenomeRNAi; 133746; -.
DR Pharos; Q8N9B5; Tbio.
DR PRO; PR:Q8N9B5; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8N9B5; protein.
DR Bgee; ENSG00000152409; Expressed in endothelial cell and 191 other tissues.
DR Genevisible; Q8N9B5; HS.
DR GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:HGNC-UCL.
DR GO; GO:0070060; P:'de novo' actin filament nucleation; ISS:UniProtKB.
DR GO; GO:0070358; P:actin polymerization-dependent cell motility; ISS:UniProtKB.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:HGNC-UCL.
DR InterPro; IPR033324; Jmy.
DR InterPro; IPR031738; JMY/WHAMM.
DR InterPro; IPR031808; JMY/WHAMM_N.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR23330:SF8; PTHR23330:SF8; 1.
DR Pfam; PF15871; JMY; 1.
DR Pfam; PF15920; WHAMM-JMY_N; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; DNA damage; DNA repair; Lipoprotein;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..988
FT /note="Junction-mediating and -regulatory protein"
FT /id="PRO_0000324611"
FT DOMAIN 921..938
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..126
FT /note="Interaction with p300/EP300"
FT /evidence="ECO:0000250"
FT REGION 51..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..567
FT /note="Interaction with p300/EP300"
FT /evidence="ECO:0000250"
FT REGION 731..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 324..360
FT /evidence="ECO:0000255"
FT COILED 489..541
FT /evidence="ECO:0000255"
FT COILED 590..621
FT /evidence="ECO:0000255"
FT COMPBIAS 801..830
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..988
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXM1"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 814..825
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032310"
FT VARIANT 364
FT /note="M -> L (in dbSNP:rs13182512)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT /id="VAR_039846"
FT VARIANT 592
FT /note="A -> V (in dbSNP:rs12109475)"
FT /id="VAR_039847"
FT VARIANT 720
FT /note="H -> R (in dbSNP:rs16876657)"
FT /id="VAR_039848"
SQ SEQUENCE 988 AA; 111445 MW; 7166FF8AE325F37A CRC64;
MSFALEETLE SDWVAVRPHV FDEREKHKFV FIVAWNEIEG KFAITCHNRT AQRQRSGSRE
QAGARGGAEA GGAASDGSRG PGSPAGRGRP EATASATLVR SPGPRRSSAW AEGGSPRSTR
SLLGDPRLRS PGSKGAESRL RSPVRAKPIP GQKTSEADDA AGAAAAAARP APREAQVSSV
RIVSASGTVS EEIEVLEMVK EDEAPLALSD AEQPPPATEL ESPAEECSWA GLFSFQDLRA
VHQQLCSVNS QLEPCLPVFP EEPSGMWTVL FGGAPEMTEQ EIDTLCYQLQ VYLGHGLDTC
GWKILSQVLF TETDDPEEYY ESLSELRQKG YEEVLQRARK RIQELLDKHK NTESMVELLD
LYQMEDEAYS SLAEATTELY QYLLQPFRDM RELAMLRRQQ IKISMENDYL GPRRIESLQK
EDADWQRKAH MAVLSIQDLT VKYFEITAKA QKAVYDRMRA DQKKFGKASW AAAAERMEKL
QYAVSKETLQ MMRAKEICLE QRKHALKEEM QSLRGGTEAI ARLDQLEADY YDLQLQLYEV
QFEILKCEEL LLTAQLESIK RLISEKRDEV VYYDTYESME AMLEKEEMAA SAYLQREELQ
KLQQKARQLE ARRGRVSAKK SYLRNKKEIC IAKHNEKIQQ RTRIEDEYRT HHTVQLKREK
LHDEEERKSA WVSQERQRTL DRLRTFKQRY PGQVILKSTR LRLAHARRKG AASPVLQEDH
CDSLPSVLQV EEKTEEVGEG RVKRGPSQTT EPQSLVQLED TSLTQLEATS LPLSGVTSEL
PPTISLPLLN NNLEPCSVTI NPLPSPLPPT PPPPPPPPPP PPPPPLPVAK DSGPETLEKD
LPRKEGNEKR IPKSASAPSA HLFDSSQLVS ARKKLRKTAE GLQRRRVSSP MDEVLASLKR
GSFHLKKVEQ RTLPPFPDED DSNNILAQIR KGVKLKKVQK DVLRESFTLL PDTDPLTRSI
HEALRRIKEA SPESEDEEEA LPCTDWEN
