MYOM1_HUMAN
ID MYOM1_HUMAN Reviewed; 1685 AA.
AC P52179; Q14BD6; Q6H969; Q6ZUU0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Myomesin-1;
DE AltName: Full=190 kDa connectin-associated protein;
DE AltName: Full=190 kDa titin-associated protein;
DE AltName: Full=Myomesin family member 1;
GN Name=MYOM1;
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 1), AND VARIANTS ALA-341 AND THR-960.
RC TISSUE=Skeletal muscle;
RA Hayess K., Matschke K., Fuerst D.O.;
RT "SUMO modification of the M-band protein myomesin.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-181;
RP ALA-341 AND THR-960.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS PRO-181
RP AND ALA-341.
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 [MRNA] OF 99-1685 (ISOFORM 2), AND VARIANTS PRO-181;
RP ALA-341 AND THR-960.
RC TISSUE=Skeletal muscle;
RX PubMed=7505783; DOI=10.1242/jcs.106.1.319;
RA Vinkemeier U., Obermann W., Weber K., Fuerst D.O.;
RT "The globular head domain of titin extends into the center of the
RT sarcomeric M band. cDNA cloning, epitope mapping and immunoelectron
RT microscopy of two titin-associated proteins.";
RL J. Cell Sci. 106:319-330(1993).
RN [6]
RP INTERACTION WITH PNKD.
RX PubMed=15188056; DOI=10.1093/abbs/36.6.412;
RA Li T.-B., Liu X.-H., Feng S., Hu Y., Yang W.-X., Han Y., Wang Y.-G.,
RA Gong L.-M.;
RT "Characterization of MR-1, a novel myofibrillogenesis regulator in human
RT muscle.";
RL Acta Biochim. Biophys. Sin. 36:412-418(2004).
CC -!- FUNCTION: Major component of the vertebrate myofibrillar M band. Binds
CC myosin, titin, and light meromyosin. This binding is dose dependent.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with TTN/titin (By
CC similarity). Interacts with PNKD. {ECO:0000250,
CC ECO:0000269|PubMed:15188056}.
CC -!- INTERACTION:
CC P52179; O75923: DYSF; NbExp=3; IntAct=EBI-5353249, EBI-2799016;
CC P52179; P52179: MYOM1; NbExp=4; IntAct=EBI-5353249, EBI-5353249;
CC P52179-1; P52179-1: MYOM1; NbExp=7; IntAct=EBI-15971501, EBI-15971501;
CC P52179-2; Q15323: KRT31; NbExp=3; IntAct=EBI-12010196, EBI-948001;
CC P52179-2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-12010196, EBI-11959885;
CC P52179-2; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-12010196, EBI-11987425;
CC P52179-2; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-12010196, EBI-11522433;
CC P52179-2; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-12010196, EBI-9640281;
CC P52179-2; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-12010196, EBI-710402;
CC P52179-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-12010196, EBI-1105213;
CC P52179-2; P36406: TRIM23; NbExp=3; IntAct=EBI-12010196, EBI-740098;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P52179-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P52179-2; Sequence=VSP_035663;
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA48833.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ621424; CAF18565.1; -; mRNA.
DR EMBL; AK125322; BAC86128.1; -; mRNA.
DR EMBL; AP005329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116183; AAI16184.1; -; mRNA.
DR EMBL; X69090; CAA48833.1; ALT_INIT; mRNA.
DR CCDS; CCDS45823.1; -. [P52179-2]
DR CCDS; CCDS45824.1; -. [P52179-1]
DR PIR; S42167; S42167.
DR RefSeq; NP_003794.3; NM_003803.3. [P52179-1]
DR RefSeq; NP_062830.1; NM_019856.1. [P52179-2]
DR PDB; 2R15; X-ray; 2.24 A; A/B=1459-1667.
DR PDB; 2Y23; X-ray; 2.50 A; A=1141-1447.
DR PDB; 2Y25; X-ray; 3.50 A; A/B/C/D=1357-1667.
DR PDB; 3RBS; X-ray; 1.85 A; A=1247-1447.
DR PDB; 5FM4; X-ray; 2.80 A; A/B/C/D/E/F=510-618.
DR PDB; 5FM5; X-ray; 3.10 A; M/N=510-739.
DR PDB; 5FM8; X-ray; 2.05 A; A/B/C/D=510-618.
DR PDB; 6T3O; X-ray; 1.80 A; A=1247-1357.
DR PDB; 6ZVA; X-ray; 2.68 A; A/B=632-735.
DR PDBsum; 2R15; -.
DR PDBsum; 2Y23; -.
DR PDBsum; 2Y25; -.
DR PDBsum; 3RBS; -.
DR PDBsum; 5FM4; -.
DR PDBsum; 5FM5; -.
DR PDBsum; 5FM8; -.
DR PDBsum; 6T3O; -.
DR PDBsum; 6ZVA; -.
DR AlphaFoldDB; P52179; -.
DR SASBDB; P52179; -.
DR SMR; P52179; -.
DR BioGRID; 114273; 20.
DR CORUM; P52179; -.
DR DIP; DIP-59649N; -.
DR IntAct; P52179; 17.
DR MINT; P52179; -.
DR STRING; 9606.ENSP00000348821; -.
DR CarbonylDB; P52179; -.
DR iPTMnet; P52179; -.
DR PhosphoSitePlus; P52179; -.
DR BioMuta; MYOM1; -.
DR DMDM; 212276443; -.
DR EPD; P52179; -.
DR jPOST; P52179; -.
DR MassIVE; P52179; -.
DR MaxQB; P52179; -.
DR PaxDb; P52179; -.
DR PeptideAtlas; P52179; -.
DR PRIDE; P52179; -.
DR ProteomicsDB; 56469; -. [P52179-1]
DR ProteomicsDB; 56470; -. [P52179-2]
DR Antibodypedia; 2827; 171 antibodies from 28 providers.
DR DNASU; 8736; -.
DR Ensembl; ENST00000261606.11; ENSP00000261606.7; ENSG00000101605.14. [P52179-2]
DR Ensembl; ENST00000356443.9; ENSP00000348821.4; ENSG00000101605.14. [P52179-1]
DR GeneID; 8736; -.
DR KEGG; hsa:8736; -.
DR MANE-Select; ENST00000356443.9; ENSP00000348821.4; NM_003803.4; NP_003794.3.
DR UCSC; uc002klp.3; human. [P52179-1]
DR CTD; 8736; -.
DR DisGeNET; 8736; -.
DR GeneCards; MYOM1; -.
DR HGNC; HGNC:7613; MYOM1.
DR HPA; ENSG00000101605; Group enriched (heart muscle, skeletal muscle, tongue).
DR MIM; 603508; gene.
DR neXtProt; NX_P52179; -.
DR OpenTargets; ENSG00000101605; -.
DR PharmGKB; PA31418; -.
DR VEuPathDB; HostDB:ENSG00000101605; -.
DR eggNOG; KOG0613; Eukaryota.
DR GeneTree; ENSGT00940000154982; -.
DR InParanoid; P52179; -.
DR OMA; GYPECVL; -.
DR OrthoDB; 57219at2759; -.
DR PhylomeDB; P52179; -.
DR TreeFam; TF331825; -.
DR PathwayCommons; P52179; -.
DR SignaLink; P52179; -.
DR SIGNOR; P52179; -.
DR BioGRID-ORCS; 8736; 7 hits in 1067 CRISPR screens.
DR ChiTaRS; MYOM1; human.
DR EvolutionaryTrace; P52179; -.
DR GeneWiki; MYOM1; -.
DR GenomeRNAi; 8736; -.
DR Pharos; P52179; Tbio.
DR PRO; PR:P52179; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P52179; protein.
DR Bgee; ENSG00000101605; Expressed in hindlimb stylopod muscle and 132 other tissues.
DR ExpressionAtlas; P52179; baseline and differential.
DR Genevisible; P52179; HS.
DR GO; GO:0031430; C:M band; ISS:UniProtKB.
DR GO; GO:0005863; C:striated muscle myosin thick filament; TAS:ProtInc.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IPI:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008307; F:structural constituent of muscle; TAS:ProtInc.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:CAFA.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:CAFA.
DR GO; GO:0010737; P:protein kinase A signaling; IMP:CAFA.
DR CDD; cd00063; FN3; 5.
DR DisProt; DP00517; -.
DR Gene3D; 2.60.40.10; -; 12.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 5.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 7.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disulfide bond;
KW Immunoglobulin domain; Muscle protein; Phosphoprotein; Reference proteome;
KW Repeat; Thick filament.
FT CHAIN 1..1685
FT /note="Myomesin-1"
FT /id="PRO_0000072684"
FT REPEAT 182..187
FT /note="1"
FT REPEAT 188..193
FT /note="2"
FT REPEAT 194..199
FT /note="3"
FT REPEAT 200..205
FT /note="4"
FT REPEAT 206..211
FT /note="5"
FT REPEAT 212..217
FT /note="6"
FT DOMAIN 277..368
FT /note="Ig-like C2-type 1"
FT DOMAIN 396..498
FT /note="Ig-like C2-type 2"
FT DOMAIN 512..607
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 640..734
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 741..834
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 933..1034
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1041..1140
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1132..1230
FT /note="Ig-like C2-type 3"
FT DOMAIN 1358..1444
FT /note="Ig-like C2-type 4"
FT DOMAIN 1573..1662
FT /note="Ig-like C2-type 5"
FT REGION 33..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..217
FT /note="6 X 6 AA tandem repeats"
FT REGION 840..938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62234"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62234"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62234"
FT MOD_RES 1054
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62234"
FT DISULFID 1160..1210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 836..931
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7505783"
FT /id="VSP_035663"
FT VARIANT 22
FT /note="V -> L (in dbSNP:rs1791085)"
FT /id="VAR_047221"
FT VARIANT 181
FT /note="S -> P (in dbSNP:rs1962519)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7505783"
FT /id="VAR_047222"
FT VARIANT 215
FT /note="T -> M (in dbSNP:rs2230165)"
FT /id="VAR_047223"
FT VARIANT 341
FT /note="G -> A (in dbSNP:rs8099021)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:7505783,
FT ECO:0000269|Ref.1"
FT /id="VAR_047224"
FT VARIANT 600
FT /note="E -> V (in dbSNP:rs9807556)"
FT /id="VAR_047225"
FT VARIANT 960
FT /note="I -> T (in dbSNP:rs1071600)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:7505783, ECO:0000269|Ref.1"
FT /id="VAR_047226"
FT VARIANT 1408
FT /note="D -> N (in dbSNP:rs3765623)"
FT /id="VAR_047227"
FT VARIANT 1453
FT /note="M -> T (in dbSNP:rs16944397)"
FT /id="VAR_047228"
FT CONFLICT 247
FT /note="E -> G (in Ref. 5; CAA48833)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="Q -> R (in Ref. 5; CAA48833)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="S -> F (in Ref. 4; AAI16184)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="P -> A (in Ref. 5; CAA48833)"
FT /evidence="ECO:0000305"
FT CONFLICT 615
FT /note="S -> G (in Ref. 4; AAI16184)"
FT /evidence="ECO:0000305"
FT CONFLICT 616..625
FT /note="RPSAPWTGQI -> PLSTLDWTV (in Ref. 5; CAA48833)"
FT /evidence="ECO:0000305"
FT CONFLICT 776
FT /note="S -> N (in Ref. 5; CAA48833)"
FT /evidence="ECO:0000305"
FT CONFLICT 793..794
FT /note="GS -> TH (in Ref. 5; CAA48833)"
FT /evidence="ECO:0000305"
FT CONFLICT 992
FT /note="S -> R (in Ref. 5; CAA48833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1001
FT /note="L -> S (in Ref. 2; BAC86128)"
FT /evidence="ECO:0000305"
FT CONFLICT 1080
FT /note="Missing (in Ref. 5; CAA48833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1141
FT /note="T -> R (in Ref. 5; CAA48833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1615..1616
FT /note="SD -> QT (in Ref. 5; CAA48833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1617
FT /note="D -> G (in Ref. 2; BAC86128)"
FT /evidence="ECO:0000305"
FT STRAND 514..521
FT /evidence="ECO:0007829|PDB:5FM8"
FT STRAND 526..531
FT /evidence="ECO:0007829|PDB:5FM8"
FT STRAND 543..550
FT /evidence="ECO:0007829|PDB:5FM8"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:5FM8"
FT STRAND 564..571
FT /evidence="ECO:0007829|PDB:5FM8"
FT STRAND 579..588
FT /evidence="ECO:0007829|PDB:5FM8"
FT STRAND 591..595
FT /evidence="ECO:0007829|PDB:5FM5"
FT HELIX 609..612
FT /evidence="ECO:0007829|PDB:5FM4"
FT STRAND 626..630
FT /evidence="ECO:0007829|PDB:5FM5"
FT STRAND 642..659
FT /evidence="ECO:0007829|PDB:6ZVA"
FT STRAND 670..679
FT /evidence="ECO:0007829|PDB:6ZVA"
FT STRAND 694..700
FT /evidence="ECO:0007829|PDB:6ZVA"
FT STRAND 707..715
FT /evidence="ECO:0007829|PDB:6ZVA"
FT STRAND 727..730
FT /evidence="ECO:0007829|PDB:6ZVA"
FT STRAND 1145..1148
FT /evidence="ECO:0007829|PDB:2Y23"
FT STRAND 1154..1159
FT /evidence="ECO:0007829|PDB:2Y23"
FT STRAND 1169..1173
FT /evidence="ECO:0007829|PDB:2Y23"
FT STRAND 1184..1189
FT /evidence="ECO:0007829|PDB:2Y23"
FT STRAND 1192..1199
FT /evidence="ECO:0007829|PDB:2Y23"
FT HELIX 1202..1204
FT /evidence="ECO:0007829|PDB:2Y23"
FT STRAND 1206..1215
FT /evidence="ECO:0007829|PDB:2Y23"
FT STRAND 1220..1224
FT /evidence="ECO:0007829|PDB:2Y23"
FT HELIX 1226..1240
FT /evidence="ECO:0007829|PDB:2Y23"
FT STRAND 1248..1254
FT /evidence="ECO:0007829|PDB:6T3O"
FT HELIX 1256..1258
FT /evidence="ECO:0007829|PDB:3RBS"
FT STRAND 1260..1265
FT /evidence="ECO:0007829|PDB:6T3O"
FT STRAND 1274..1279
FT /evidence="ECO:0007829|PDB:6T3O"
FT STRAND 1282..1284
FT /evidence="ECO:0007829|PDB:6T3O"
FT STRAND 1286..1289
FT /evidence="ECO:0007829|PDB:6T3O"
FT STRAND 1291..1294
FT /evidence="ECO:0007829|PDB:6T3O"
FT TURN 1296..1298
FT /evidence="ECO:0007829|PDB:6T3O"
FT STRAND 1300..1306
FT /evidence="ECO:0007829|PDB:6T3O"
FT HELIX 1310..1312
FT /evidence="ECO:0007829|PDB:6T3O"
FT STRAND 1314..1322
FT /evidence="ECO:0007829|PDB:6T3O"
FT STRAND 1325..1333
FT /evidence="ECO:0007829|PDB:6T3O"
FT HELIX 1336..1354
FT /evidence="ECO:0007829|PDB:6T3O"
FT STRAND 1357..1369
FT /evidence="ECO:0007829|PDB:3RBS"
FT TURN 1370..1372
FT /evidence="ECO:0007829|PDB:3RBS"
FT STRAND 1373..1382
FT /evidence="ECO:0007829|PDB:3RBS"
FT STRAND 1388..1393
FT /evidence="ECO:0007829|PDB:3RBS"
FT STRAND 1396..1398
FT /evidence="ECO:0007829|PDB:3RBS"
FT STRAND 1407..1415
FT /evidence="ECO:0007829|PDB:3RBS"
FT HELIX 1420..1422
FT /evidence="ECO:0007829|PDB:3RBS"
FT STRAND 1424..1432
FT /evidence="ECO:0007829|PDB:3RBS"
FT STRAND 1435..1443
FT /evidence="ECO:0007829|PDB:3RBS"
FT HELIX 1446..1460
FT /evidence="ECO:0007829|PDB:2Y25"
FT STRAND 1467..1470
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1472..1483
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1489..1494
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1503..1510
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1513..1520
FT /evidence="ECO:0007829|PDB:2R15"
FT HELIX 1523..1525
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1527..1534
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1539..1546
FT /evidence="ECO:0007829|PDB:2R15"
FT HELIX 1548..1570
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1573..1577
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1580..1585
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1590..1597
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1603..1608
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1611..1613
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1617..1624
FT /evidence="ECO:0007829|PDB:2R15"
FT TURN 1625..1627
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1628..1635
FT /evidence="ECO:0007829|PDB:2R15"
FT HELIX 1638..1640
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1642..1650
FT /evidence="ECO:0007829|PDB:2R15"
FT STRAND 1653..1664
FT /evidence="ECO:0007829|PDB:2R15"
SQ SEQUENCE 1685 AA; 187627 MW; F0DBB25EB6323DF8 CRC64;
MSLPFYQRCH QHYDLSYRNK DVRSTVSHYQ REKKRSAVYT QGSTAYSSRS SAAHRRESEA
FRRASASSSQ QQASQHALSS EVSRKAASAY DYGSSHGLTD SSLLLDDYSS KLSPKPKRAK
HSLLSGEEKE NLPSDYMVPI FSGRQKHVSG ITDTEEERIK EAAAYIAQRN LLASEEGITT
SKQSTASKQT TASKQSTASK QSTASKQSTA SRQSTASRQS VVSKQATSAL QQEETSEKKS
RKVVIREKAE RLSLRKTLEE TETYHAKLNE DHLLHAPEFI IKPRSHTVWE KENVKLHCSI
AGWPEPRVTW YKNQVPINVH ANPGKYIIES RYGMHTLEIN GCDFEDTAQY RASAMNVKGE
LSAYASVVVK RYKGEFDETR FHAGASTMPL SFGVTPYGYA SRFEIHFDDK FDVSFGREGE
TMSLGCRVVI TPEIKHFQPE IQWYRNGVPL SPSKWVQTLW SGERATLTFS HLNKEDEGLY
TIRVRMGEYY EQYSAYVFVR DADAEIEGAP AAPLDVKCLE ANKDYIIISW KQPAVDGGSP
ILGYFIDKCE VGTDSWSQCN DTPVKFARFP VTGLIEGRSY IFRVRAVNKM GIGFPSRVSE
PVAALDPAEK ARLKSRPSAP WTGQIIVTEE EPSEGIVPGP PTDLSVTEAT RSYVVLSWKP
PGQRGHEGIM YFVEKCEAGT ENWQRVNTEL PVKSPRFALF DLAEGKSYCF RVRCSNSAGV
GEPSEATEVT VVGDKLDIPK APGKIIPSRN TDTSVVVSWE ESKDAKELVG YYIEASVAGS
GKWEPCNNNP VKGSRFTCHG LVTGQSYIFR VRAVNAAGLS EYSQDSEAIE VKAAIGGGVS
PDVCPALSDE PGGLTASRGR VHEASPPTFQ KDALLGSKPN KPSLPSSSQN LGQTEVSKVS
ETVQEELTPP PQKAAPQGKS KSDPLKKKTD RAPPSPPCDI TCLESFRDSM VLGWKQPDKI
GGAEITGYYV NYREVIDGVP GKWREANVKA VSEEAYKISN LKENMVYQFQ VAAMNMAGLG
APSAVSECFK CEEWTIAVPG PPHSLKCSEV RKDSLVLQWK PPVHSGRTPV TGYFVDLKEA
KAKEDQWRGL NEAAIKNVYL KVRGLKEGVS YVFRVRAINQ AGVGKPSDLA GPVVAETRPG
TKEVVVNVDD DGVISLNFEC DKMTPKSEFS WSKDYVSTED SPRLEVESKG NKTKMTFKDL
GMDDLGIYSC DVTDTDGIAS SYLIDEEELK RLLALSHEHK FPTVPVKSEL AVEILEKGQV
RFWMQAEKLS GNAKVNYIFN EKEIFEGPKY KMHIDRNTGI IEMFMEKLQD EDEGTYTFQL
QDGKATNHST VVLVGDVFKK LQKEAEFQRQ EWIRKQGPHF VEYLSWEVTG ECNVLLKCKV
ANIKKETHIV WYKDEREISV DEKHDFKDGI CTLLITEFSK KDAGIYEVIL KDDRGKDKSR
LKLVDEAFKE LMMEVCKKIA LSATDLKIQS TAEGIQLYSF VTYYVEDLKV NWSHNGSAIR
YSDRVKTGVT GEQIWLQINE PTPNDKGKYV MELFDGKTGH QKTVDLSGQA YDEAYAEFQR
LKQAAIAEKN RARVLGGLPD VVTIQEGKAL NLTCNVWGDP PPEVSWLKNE KALASDDHCN
LKFEAGRTAY FTINGVSTAD SGKYGLVVKN KYGSETSDFT VSVFIPEEEA RMAALESLKG
GKKAK
