CMYA5_HUMAN
ID CMYA5_HUMAN Reviewed; 4069 AA.
AC Q8N3K9; A0PJB7; Q05CT4; Q2NKX1; Q2T9G9; Q69YQ8; Q69YQ9; Q6P517; Q6P5U3;
AC Q7Z4I1; Q86T34; Q86T49; Q8N3S4; Q8N3S7; Q8NAG8; Q9UK88;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cardiomyopathy-associated protein 5;
DE AltName: Full=Dystrobrevin-binding protein 2;
DE AltName: Full=Genethonin-3;
DE AltName: Full=Myospryn {ECO:0000303|PubMed:14688250};
DE AltName: Full=SPRY domain-containing protein 2;
DE AltName: Full=Tripartite motif-containing protein 76;
GN Name=CMYA5; Synonyms=C5orf10, DTNBP2, SPRYD2, TRIM76;
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 MRNA] OF 1-1682 AND 2600-4069, AND
RP VARIANTS GLY-190; VAL-1295; GLU-3583 AND LEU-4063.
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-283; 1067-1340; 1604-2691 AND
RP 2754-4069, AND VARIANTS GLY-1920; LEU-2262; GLN-3358; GLU-3583 AND
RP GLN-3927.
RC TISSUE=Liver, and Skeletal muscle;
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 1067-1340.
RC TISSUE=Skeletal muscle;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1736-2539, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=11297942; DOI=10.1016/s0960-8966(00)00198-x;
RA Tkatchenko A.V., Pietu G., Cros N., Gannoun-Zaki L., Auffray C.,
RA Leger J.J., Dechesne C.A.;
RT "Identification of altered gene expression in skeletal muscles from
RT Duchenne muscular dystrophy patients.";
RL Neuromuscul. Disord. 11:269-277(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3113-4069, AND VARIANT GLN-3927.
RC TISSUE=Mammary gland;
RA Ding P., Han W., Wang L., Wang Y., Qiu X., Xu M., Ma D.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION.
RX PubMed=14688250; DOI=10.1074/jbc.m312664200;
RA Benson M.A., Tinsley C.L., Blake D.J.;
RT "Myospryn is a novel binding partner for dysbindin in muscle.";
RL J. Biol. Chem. 279:10450-10458(2004).
RN [8]
RP INTERACTION WITH DES.
RX PubMed=17872945; DOI=10.1074/jbc.m704733200;
RA Kouloumenta A., Mavroidis M., Capetanaki Y.;
RT "Proper perinuclear localization of the TRIM-like protein myospryn requires
RT its binding partner desmin.";
RL J. Biol. Chem. 282:35211-35221(2007).
RN [9]
RP INTERACTION WITH CAPN3 AND TTN, AND SUBCELLULAR LOCATION.
RX PubMed=20634290; DOI=10.1074/jbc.m110.108720;
RA Sarparanta J., Blandin G., Charton K., Vihola A., Marchand S., Milic A.,
RA Hackman P., Ehler E., Richard I., Udd B.;
RT "Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to
RT tibial and limb-girdle muscular dystrophies.";
RL J. Biol. Chem. 285:30304-30315(2010).
CC -!- FUNCTION: May serve as an anchoring protein that mediates the
CC subcellular compartmentation of protein kinase A (PKA) via binding to
CC PRKAR2A (By similarity). May function as a repressor of calcineurin-
CC mediated transcriptional activity. May attenuate calcineurin ability to
CC induce slow-fiber gene program in muscle and may negatively modulate
CC skeletal muscle regeneration (By similarity). Plays a role in the
CC assembly of ryanodine receptor (RYR2) clusters in striated muscle (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q70KF4}.
CC -!- SUBUNIT: Interacts with PRKAR2A. Interacts with ACTN2 and
CC DTNBP1/dysbindin (By similarity). Interacts with DES (PubMed:17872945).
CC Interacts with DMD/dystrophin (By similarity). Interacts with the
CC calcineurin catalytic subunit PPP3CA (By similarity). Interacts with
CC TTN (PubMed:20634290). Interacts with CAPN3; this interaction, which
CC results in CMYA5 proteolysis, may protect CAPN3 from autolysis
CC (PubMed:20634290). Interacts with FSD2 (By similarity). Identified in a
CC complex composed of FSD2, CMYA5 and RYR2 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q70KF4, ECO:0000269|PubMed:17872945,
CC ECO:0000269|PubMed:20634290}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A286XF80}.
CC Sarcoplasmic reticulum {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q70KF4}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:A0A286XF80}. Cytoplasm, myofibril, sarcomere, M
CC line {ECO:0000269|PubMed:20634290}. Note=Found predominantly at the
CC periphery of the nucleus but also throughout the cell. Localized in
CC lysosomes (By similarity). In skeletal muscles, localizes along
CC myofiber periphery, at costameres (By similarity). Predominantly flanks
CC Z-disks (By similarity). Occasionally present at the M-band level.
CC Colocalized with RYR2 in the sarcoplasmic reticulum (By similarity).
CC {ECO:0000250|UniProtKB:A0A286XF80}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle; at a strong level and
CC in heart. {ECO:0000269|PubMed:11297942}.
CC -!- INDUCTION: Down-regulated in muscle cell lines derived from patients
CC with Duchenne muscular dystrophy (DMD). {ECO:0000269|PubMed:11297942,
CC ECO:0000269|PubMed:14688250}.
CC -!- DOMAIN: Amphipathic helix regions act as an anchoring domain for PKA,
CC and appear to be responsible of the interaction between myospryn and
CC PRKAR2A.
CC -!- PTM: Phosphorylated by PKA. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55265.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH20856.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH22422.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH62664.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH63134.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI11530.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAQ09018.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH10406.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AC008482; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831966; CAD38607.1; -; mRNA.
DR EMBL; AL831968; CAD38609.2; -; mRNA.
DR EMBL; AL831986; CAD91143.1; -; mRNA.
DR EMBL; AL832347; CAH10406.1; ALT_SEQ; mRNA.
DR EMBL; AL832368; CAD91158.1; -; mRNA.
DR EMBL; AL832376; CAH10402.1; -; mRNA.
DR EMBL; AL834252; CAD38928.2; -; mRNA.
DR EMBL; BC020856; AAH20856.1; ALT_SEQ; mRNA.
DR EMBL; BC022422; AAH22422.1; ALT_SEQ; mRNA.
DR EMBL; BC062664; AAH62664.1; ALT_SEQ; mRNA.
DR EMBL; BC063134; AAH63134.1; ALT_SEQ; mRNA.
DR EMBL; BC111529; AAI11530.1; ALT_SEQ; mRNA.
DR EMBL; BC111530; AAI11531.1; -; mRNA.
DR EMBL; AK092699; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF177292; AAD55265.1; ALT_SEQ; mRNA.
DR EMBL; AF533705; AAQ09018.1; ALT_INIT; mRNA.
DR CCDS; CCDS47238.1; -.
DR RefSeq; NP_705838.3; NM_153610.4.
DR SMR; Q8N3K9; -.
DR BioGRID; 128427; 30.
DR IntAct; Q8N3K9; 13.
DR MINT; Q8N3K9; -.
DR STRING; 9606.ENSP00000394770; -.
DR iPTMnet; Q8N3K9; -.
DR PhosphoSitePlus; Q8N3K9; -.
DR BioMuta; CMYA5; -.
DR DMDM; 182627649; -.
DR EPD; Q8N3K9; -.
DR jPOST; Q8N3K9; -.
DR MassIVE; Q8N3K9; -.
DR MaxQB; Q8N3K9; -.
DR PaxDb; Q8N3K9; -.
DR PeptideAtlas; Q8N3K9; -.
DR PRIDE; Q8N3K9; -.
DR ProteomicsDB; 71818; -.
DR Antibodypedia; 24574; 35 antibodies from 16 providers.
DR DNASU; 202333; -.
DR Ensembl; ENST00000446378.3; ENSP00000394770.2; ENSG00000164309.15.
DR GeneID; 202333; -.
DR KEGG; hsa:202333; -.
DR MANE-Select; ENST00000446378.3; ENSP00000394770.2; NM_153610.5; NP_705838.3.
DR UCSC; uc003kgc.4; human.
DR CTD; 202333; -.
DR DisGeNET; 202333; -.
DR GeneCards; CMYA5; -.
DR HGNC; HGNC:14305; CMYA5.
DR HPA; ENSG00000164309; Group enriched (skeletal muscle, tongue).
DR MIM; 612193; gene.
DR neXtProt; NX_Q8N3K9; -.
DR OpenTargets; ENSG00000164309; -.
DR PharmGKB; PA37868; -.
DR VEuPathDB; HostDB:ENSG00000164309; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159696; -.
DR HOGENOM; CLU_000269_0_0_1; -.
DR InParanoid; Q8N3K9; -.
DR OMA; WMLEKPE; -.
DR OrthoDB; 22778at2759; -.
DR PhylomeDB; Q8N3K9; -.
DR TreeFam; TF331281; -.
DR PathwayCommons; Q8N3K9; -.
DR SignaLink; Q8N3K9; -.
DR BioGRID-ORCS; 202333; 20 hits in 1069 CRISPR screens.
DR ChiTaRS; CMYA5; human.
DR GenomeRNAi; 202333; -.
DR Pharos; Q8N3K9; Tbio.
DR PRO; PR:Q8N3K9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8N3K9; protein.
DR Bgee; ENSG00000164309; Expressed in tibialis anterior and 158 other tissues.
DR Genevisible; Q8N3K9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50853; FN3; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Sarcoplasmic reticulum.
FT CHAIN 1..4069
FT /note="Cardiomyopathy-associated protein 5"
FT /id="PRO_0000328722"
FT DOMAIN 3704..3805
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3806..3898
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 3880..4065
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 979..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1540..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1757..1809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1892..1988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2064..2175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2187..2259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2385..2412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2425..2463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2494..2527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2653..2706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2750..2862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3015..3037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3052..3365
FT /note="Required for RYR2 clustering"
FT /evidence="ECO:0000250|UniProtKB:Q70KF4"
FT REGION 3119..3156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3204..3231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3386..3421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3465..3495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3517..3544
FT /note="Amphipathic helix H1"
FT REGION 3545..3672
FT /note="B-box coiled-coil; BBC"
FT REGION 3631..3648
FT /note="Amphipathic helix H2"
FT REGION 3751..3767
FT /note="Amphipathic helix H3"
FT COILED 2964..2988
FT /evidence="ECO:0000255"
FT COILED 3544..3653
FT /evidence="ECO:0000255"
FT COMPBIAS 22..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1793..1809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1906..1928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1936..1950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1951..1982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2083..2127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2187..2211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2235..2251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2386..2400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2661..2685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2750..2773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2782..2800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2806..2825
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2831..2853
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3015..3035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3215..3231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3403..3421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3478..3495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q70KF4"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q70KF4"
FT MOD_RES 2404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q70KF4"
FT MOD_RES 2813
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q70KF4"
FT MOD_RES 3228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q70KF4"
FT VARIANT 64
FT /note="Y -> C (in dbSNP:rs16877109)"
FT /id="VAR_042471"
FT VARIANT 175
FT /note="Q -> H (in dbSNP:rs6895605)"
FT /id="VAR_042472"
FT VARIANT 190
FT /note="D -> G (in dbSNP:rs10942901)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_042473"
FT VARIANT 349
FT /note="G -> D (in dbSNP:rs1366271)"
FT /id="VAR_042474"
FT VARIANT 591
FT /note="G -> D (in dbSNP:rs16877124)"
FT /id="VAR_042475"
FT VARIANT 651
FT /note="S -> R (in dbSNP:rs57544556)"
FT /id="VAR_061611"
FT VARIANT 1006
FT /note="V -> A (in dbSNP:rs6893869)"
FT /id="VAR_042476"
FT VARIANT 1295
FT /note="A -> V (in dbSNP:rs4704585)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_042477"
FT VARIANT 1309
FT /note="I -> V (in dbSNP:rs16877133)"
FT /id="VAR_042478"
FT VARIANT 1333
FT /note="A -> V (in dbSNP:rs16877135)"
FT /id="VAR_042479"
FT VARIANT 1380
FT /note="I -> V (in dbSNP:rs13158477)"
FT /id="VAR_042480"
FT VARIANT 1567
FT /note="A -> E (in dbSNP:rs1428223)"
FT /id="VAR_042481"
FT VARIANT 1599
FT /note="S -> A (in dbSNP:rs1428224)"
FT /id="VAR_042482"
FT VARIANT 1669
FT /note="L -> S (in dbSNP:rs1019762)"
FT /id="VAR_042483"
FT VARIANT 1713
FT /note="I -> N (in dbSNP:rs16877141)"
FT /id="VAR_042484"
FT VARIANT 1721
FT /note="I -> V (in dbSNP:rs1428225)"
FT /id="VAR_042485"
FT VARIANT 1875
FT /note="A -> V (in dbSNP:rs16877147)"
FT /id="VAR_042486"
FT VARIANT 1917
FT /note="D -> G (in dbSNP:rs16877150)"
FT /id="VAR_042487"
FT VARIANT 1920
FT /note="S -> G (in dbSNP:rs16877151)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_042488"
FT VARIANT 2262
FT /note="V -> L (in dbSNP:rs6859595)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_042489"
FT VARIANT 2383
FT /note="K -> E (in dbSNP:rs7721884)"
FT /id="VAR_042490"
FT VARIANT 2693
FT /note="T -> I (in dbSNP:rs28362541)"
FT /id="VAR_042491"
FT VARIANT 2906
FT /note="K -> N (in dbSNP:rs2278239)"
FT /id="VAR_042492"
FT VARIANT 2935
FT /note="G -> R (in dbSNP:rs2278240)"
FT /id="VAR_042493"
FT VARIANT 3358
FT /note="H -> Q (in dbSNP:rs3828611)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_042494"
FT VARIANT 3583
FT /note="K -> E (in dbSNP:rs12514461)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_042495"
FT VARIANT 3927
FT /note="R -> Q (in dbSNP:rs1129770)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6"
FT /id="VAR_042496"
FT VARIANT 4063
FT /note="P -> L (in dbSNP:rs10043986)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_042497"
FT CONFLICT 79
FT /note="E -> D (in Ref. 2; CAH10406)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="A -> V (in Ref. 2; CAH10406)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="V -> I (in Ref. 2; CAH10402)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="S -> L (in Ref. 2; CAH10406)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="N -> D (in Ref. 2; CAH10402)"
FT /evidence="ECO:0000305"
FT CONFLICT 995
FT /note="A -> T (in Ref. 2; CAH10406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1283
FT /note="S -> P (in Ref. 2; CAH10406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1606
FT /note="F -> L (in Ref. 2; CAH10406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1681
FT /note="G -> E (in Ref. 2; CAH10406)"
FT /evidence="ECO:0000305"
FT CONFLICT 1855
FT /note="S -> G (in Ref. 3; AAH63134)"
FT /evidence="ECO:0000305"
FT CONFLICT 2038
FT /note="E -> K (in Ref. 3; AAH63134)"
FT /evidence="ECO:0000305"
FT CONFLICT 2148
FT /note="S -> A (in Ref. 5; AAD55265)"
FT /evidence="ECO:0000305"
FT CONFLICT 2538
FT /note="G -> D (in Ref. 5; AAD55265)"
FT /evidence="ECO:0000305"
FT CONFLICT 2782..2784
FT /note="MKE -> TKD (in Ref. 2; CAD38607)"
FT /evidence="ECO:0000305"
FT CONFLICT 2788
FT /note="S -> P (in Ref. 2; CAD38928)"
FT /evidence="ECO:0000305"
FT CONFLICT 2933
FT /note="P -> L (in Ref. 2; CAD38607)"
FT /evidence="ECO:0000305"
FT CONFLICT 3073..3113
FT /note="PQKLNVEEKLSKEVTEETISFPVSSVESALEHEYDLVKLDE -> SFKTIPL
FT PDDSETVACHKTLKSRLEDEKVTPLKENKQKETQ (in Ref. 3; AAH62664)"
FT /evidence="ECO:0000305"
FT CONFLICT 3131
FT /note="Q -> L (in Ref. 6; AAQ09018)"
FT /evidence="ECO:0000305"
FT CONFLICT 3291
FT /note="R -> W (in Ref. 2; CAD91143)"
FT /evidence="ECO:0000305"
FT CONFLICT 3321
FT /note="K -> R (in Ref. 2; CAD91143)"
FT /evidence="ECO:0000305"
FT CONFLICT 3331
FT /note="V -> A (in Ref. 2; CAD91158)"
FT /evidence="ECO:0000305"
FT CONFLICT 3348
FT /note="V -> A (in Ref. 2; CAD91158)"
FT /evidence="ECO:0000305"
FT CONFLICT 3361
FT /note="E -> G (in Ref. 2; CAD91158)"
FT /evidence="ECO:0000305"
FT CONFLICT 3803..3822
FT /note="APSTPVIRAEDCTVCWNTAT -> GKEMDAKGALEDNAQFFTDS (in
FT Ref. 2; CAD91143)"
FT /evidence="ECO:0000305"
FT CONFLICT 3852
FT /note="R -> S (in Ref. 2; CAD91158)"
FT /evidence="ECO:0000305"
FT CONFLICT 3880
FT /note="N -> S (in Ref. 2; CAD91158)"
FT /evidence="ECO:0000305"
FT CONFLICT 3929
FT /note="T -> A (in Ref. 2; CAD91158)"
FT /evidence="ECO:0000305"
FT CONFLICT 3948
FT /note="E -> K (in Ref. 2; CAD91158)"
FT /evidence="ECO:0000305"
FT CONFLICT 4050
FT /note="K -> E (in Ref. 2; CAD38607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4069 AA; 449211 MW; F5A25F1C53640EB8 CRC64;
MASRDSNHAG ESFLGSDGDE EATRELETEE ESEGEEDETA AESEEEPDSR LSDQDEEGKI
KQEYIISDPS FSMVTVQRED SGITWETNSS RSSTPWASEE SQTSGVCSRE GSTVNSPPGN
VSFIVDEVKK VRKRTHKSKH GSPSLRRKGN RKRNSFESQD VPTNKKGSPL TSASQVLTTE
KEKSYTGIYD KARKKKTTSN TPPITGAIYK EHKPLVLRPV YIGTVQYKIK MFNSVKEELI
PLQFYGTLPK GYVIKEIHYR KGKDASISLE PDLDNSGSNT VSKTRKLVAQ SIEDKVKEVF
PPWRGALSKG SESLTLMFSH EDQKKIYADS PLNATSALEH TVPSYSSSGR AEQGIQLRHS
QSVPQQPEDE AKPHEVEPPS VTPDTPATMF LRTTKEECEL ASPGTAASEN DSSVSPSFAN
EVKKEDVYSA HHSISLEAAS PGLAASTQDG LDPDQEQPDL TSIERAEPVS AKLTPTHPSV
KGEKEENMLE PSISLSEPLM LEEPEKEEIE TSLPIAITPE PEDSNLVEEE IVELDYPESP
LVSEKPFPPH MSPEVEHKEE ELILPLLAAS SPEHVALSEE EREEIASVST GSAFVSEYSV
PQDLNHELQE QEGEPVPPSN VEAIAEHAVL SEEENEEFEA YSPAAAPTSE SSLSPSTTEK
TSENQSPLFS TVTPEYMVLS GDEASESGCY TPDSTSASEY SVPSLATKES LKKTIDRKSP
LILKGVSEYM IPSEEKEDTG SFTPAVAPAS EPSLSPSTTE KTSECQSPLP STATSEHVVP
SEGEDLGSER FTPDSKLISK YAAPLNATQE SQKKIINEAS QFKPKGISEH TVLSVDGKEV
IGPSSPDLVV ASEHSFPPHT TEMTSECQAP PLSATPSEYV VLSDEEAVEL ERYTPSSTSA
SEFSVPPYAT PEAQEEEIVH RSLNLKGASS PMNLSEEDQE DIGPFSPDSA FVSEFSFPPY
ATQEAEKREF ECDSPICLTS PSEHTILSDE DTEEAELFSP DSASQVSIPP FRISETEKNE
LEPDSLLTAV SASGYSCFSE ADEEDIGSTA ATPVSEQFSS SQKQKAETFP LMSPLEDLSL
PPSTDKSEKA EIKPEIPTTS TSVSEYLILA QKQKTQAYLE PESEDLIPSH LTSEVEKGER
EASSSVAAIP AALPAQSSIV KEETKPASPH SVLPDSVPAI KKEQEPTAAL TLKAADEQMA
LSKVRKEEIV PDSQEATAHV SQDQKMEPQP PNVPESEMKY SVLPDMVDEP KKGVKPKLVL
NVTSELEQRK LSKNEPEVIK PYSPLKETSL SGPEALSAVK MEMKHDSKIT TTPIVLHSAS
SGVEKQVEHG PPALAFSALS EEIKKEIEPS SSTTTASVTK LDSNLTRAVK EEIPTDSSLI
TPVDRPVLTK VGKGELGSGL PPLVTSADEH SVLAEEDKVA IKGASPIETS SKHLAWSEAE
KEIKFDSLPS VSSIAEHSVL SEVEAKEVKA GLPVIKTSSS QHSDKSEEAR VEDKQDLLFS
TVCDSERLVS SQKKSLMSTS EVLEPEHELP LSLWGEIKKK ETELPSSQNV SPASKHIIPK
GKDEETASSS PELENLASGL APTLLLLSDD KNKPAVEVSS TAQGDFPSEK QDVALAELSL
EPEKKDKPHQ PLELPNAGSE FSSDLGRQSG SIGTKQAKSP ITETEDSVLE KGPAELRSRE
GKEENRELCA SSTMPAISEL SSLLREESQN EEIKPFSPKI ISLESKEPPA SVAEGGNPEE
FQPFTFSLKG LSEEVSHPAD FKKGGNQEIG PLPPTGNLKA QVMGDILDKL SEETGHPNSS
QVLQSITEPS KIAPSDLLVE QKKTEKALHS DQTVKLPDVS TSSEDKQDLG IKQFSLMREN
LPLEQSKSFM TTKPADVKET KMEEFFISPK DENWMLGKPE NVASQHEQRI AGSVQLDSSS
SNELRPGQLK AAVSSKDHTC EVRKQVLPHS AEESHLSSQE AVSALDTSSG NTETLSSKSY
SSEEVKLAEE PKSLVLAGNV ERNIAEGKEI HSLMESESLL LEKANTELSW PSKEDSQEKI
KLPPERFFQK PVSGLSVEQV KSETISSSVK TAHFPAEGVE PALGNEKEAH RSTPPFPEEK
PLEESKMVQS KVIDDADEGK KPSPEVKIPT QRKPISSIHA REPQSPESPE VTQNPPTQPK
VAKPDLPEEK GKKGISSFKS WMSSLFFGSS TPDNKVAEQE DLETQPSPSV EKAVTVIDPE
GTIPTNFNVA EKPADHSLSE VKLKTADEPR GTLVKSGDGQ NVKEKSMILS NVEDLQQPKF
ISEVSREDYG KKEISGDSEE MNINSVVTSA DGENLEIQSY SLIGEKLVME EAKTIVPPHV
TDSKRVQKPA IAPPSKWNIS IFKEEPRSDQ KQKSLLSFDV VDKVPQQPKS ASSNFASKNI
TKESEKPESI ILPVEESKGS LIDFSEDRLK KEMQNPTSLK ISEEETKLRS VSPTEKKDNL
ENRSYTLAEK KVLAEKQNSV APLELRDSNE IGKTQITLGS RSTELKESKA DAMPQHFYQN
EDYNERPKII VGSEKEKGEE KENQVYVLSE GKKQQEHQPY SVNVAESMSR ESDISLGHSL
GETQSFSLVK ATSVTEKSEA MLAEAHPEIR EAKAVGTQPH PLEESKVLVE KTKTFLPVAL
SCRDEIENHS LSQEGNLVLE KSSRDMPDHS EEKEQFRESE LSKGGSVDIT KETVKQGFQE
KAVGTQPRPL EESKVLVEKT KTFLPVVLSC HDEIENHSLS QEGNLVLEKS SRDMPDHSEE
KEQFKESELW KGGSVDITKE SMKEGFPSKE SERTLARPFD ETKSSETPPY LLSPVKPQTL
ASGASPEINA VKKKEMPRSE LTPERHTVHT IQTSKDDTSD VPKQSVLVSK HHLEAAEDTR
VKEPLSSAKS NYAQFISNTS ASNADKMVSN KEMPKEPEDT YAKGEDFTVT SKPAGLSEDQ
KTAFSIISEG CEILNIHAPA FISSIDQEES EQMQDKLEYL EEKASFKTIP LPDDSETVAC
HKTLKSRLED EKVTPLKENK QKETHKTKEE ISTDSETDLS FIQPTIPSEE DYFEKYTLID
YNISPDPEKQ KAPQKLNVEE KLSKEVTEET ISFPVSSVES ALEHEYDLVK LDESFYGPEK
GHNILSHPET QSQNSADRNV SKDTKRDVDS KSPGMPLFEA EEGVLSRTQI FPTTIKVIDP
EFLEEPPALA FLYKDLYEEA VGEKKKEEET ASEGDSVNSE ASFPSRNSDT DDGTGIYFEK
YILKDDILHD TSLTQKDQGQ GLEEKRVGKD DSYQPIAAEG EIWGKFGTIC REKSLEEQKG
VYGEGESVDH VETVGNVAMQ KKAPITEDVR VATQKISYAV PFEDTHHVLE RADEAGSHGN
EVGNASPEVN LNVPVQVSFP EEEFASGATH VQETSLEEPK ILVPPEPSEE RLRNSPVQDE
YEFTESLHNE VVPQDILSEE LSSESTPEDV LSQGKESFEH ISENEFASEA EQSTPAEQKE
LGSERKEEDQ LSSEVVTEKA QKELKKSQID TYCYTCKCPI SATDKVFGTH KDHEVSTLDT
AISAVKVQLA EFLENLQEKS LRIEAFVSEI ESFFNTIEEN CSKNEKRLEE QNEEMMKKVL
AQYDEKAQSF EEVKKKKMEF LHEQMVHFLQ SMDTAKDTLE TIVREAEELD EAVFLTSFEE
INERLLSAME STASLEKMPA AFSLFEHYDD SSARSDQMLK QVAVPQPPRL EPQEPNSATS
TTIAVYWSMN KEDVIDSFQV YCMEEPQDDQ EVNELVEEYR LTVKESYCIF EDLEPDRCYQ
VWVMAVNFTG CSLPSERAIF RTAPSTPVIR AEDCTVCWNT ATIRWRPTTP EATETYTLEY
CRQHSPEGEG LRSFSGIKGL QLKVNLQPND NYFFYVRAIN AFGTSEQSEA ALISTRGTRF
LLLRETAHPA LHISSSGTVI SFGERRRLTE IPSVLGEELP SCGQHYWETT VTDCPAYRLG
ICSSSAVQAG ALGQGETSWY MHCSEPQRYT FFYSGIVSDV HVTERPARVG ILLDYNNQRL
IFINAESEQL LFIIRHRFNE GVHPAFALEK PGKCTLHLGI EPPDSVRHK
