LOCUS 547975 1937 aa 01-JUN-1994

DEFINITION MYOSIN HEAVY CHAIN, PERINATAL SKELETAL MUSCLE. ACCESSION 547975 PID g547975 DBSOURCE SWISS-PROT: locus MYSP_HUMAN, accession P13535 class: standard. created: Jan 1, 1990. sequence updated: Jun 1, 1994. annotation updated: Jun 1, 1994. xrefs: gi: 189033, gi: 189034, gi: 29465, gi: 29466, gi: 34863, gi: 34864, gi: 107143 xrefs (non-sequence databases): HSSP P03034, MIM 160741 KEYWORDS MYOSIN; MUSCLE PROTEIN; COILED COIL; THICK FILAMENT; ACTIN-BINDING; ATP-BINDING; METHYLATION; ALKYLATION; HEPTAD REPEAT PATTERN; MULTIGENE FAMILY.

SOURCE human. ORGANISM Homo sapiens Eukaryotae; Metazoa; Chordata; Vertebrata; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.

REFERENCE 1 (residues 1 to 1937) AUTHORS Karsch-Mizrachi,I., Feghali,R., Shows,T.B. and Leinwand,L.A. TITLE Generation of a full-length human perinatal myosin heavy-chain-encoding cDNA JOURNAL Gene 89 (2), 289-294 (1990) MEDLINE 90323631 REMARK SEQUENCE FROM N.A. TISSUE=SKELETAL MUSCLE REFERENCE 2 (residues 1 to 1937)

AUTHORS Bober,E., Buchberger-Seidl,A., Braun,T., Singh,S., Goedde,H.W. and Arnold,H.H. TITLE Identification of three developmentally controlled isoforms of human myosin heavy chains JOURNAL Eur. J. Biochem. 189 (1), 55-65 (1990) MEDLINE 90235862 REMARK SEQUENCE OF 502-1937 FROM N.A. TISSUE=SKELETAL MUSCLE REFERENCE 3 (residues 1 to 1937)

AUTHORS Feghali,R. and Leinwand,L.A. TITLE Molecular genetic characterization of a developmentally regulated human perinatal myosin heavy chain JOURNAL J. Cell Biol. 108 (5), 1791-1797 (1989) MEDLINE 89234168 REMARK SEQUENCE OF 860-1937. COMMENT [FUNCTION] MUSCLE CONTRACTION. [SUBUNIT] MUSCLE MYOSIN IS A HEXAMERIC PROTEIN THAT CONSISTS OF 2 HEAVY CHAIN SUBUNITS (MHC), 2 ALKALI LIGHT CHAIN SUBUNITS (MLC) AND 2 REGULATORY LIGHT CHAIN SUBUNITS (MLC-2). [SUBCELLULAR LOCATION] THICK FILAMENTS OF THE MYOFIBRILS. [DOMAIN] THE RODLIKE TAIL SEQUENCE IS HIGHLY REPETITIVE, SHOWING CYCLES OF A 28-RESIDUE REPEAT PATTERN COMPOSED OF 4 HEPTAPEPTIDES, CHARACTERISTIC FOR ALPHA-HELICAL COILED COILS. [PTM] TWO CYSTEINE RESIDUES IN THE S1 DOMAIN ARE SELECTIVELY ALKYLATED AND ARE REQUIRED FOR MYOSIN ATPASE ACTIVITY. EACH MYOSIN HEAVY CHAIN CAN BE SPLIT INTO 1 LIGHT MEROMYOSIN (LMM) AND 1 HEAVY MEROMYOSIN (HMM). IT CAN LATTER BE SPLIT FURTHER INTO 2 GLOBULAR SUBFRAGMENTS (S1) AND 1 ROD-SHAPED SUBFRAGMENT (S2). [SIMILARITY] THE PERIODICITIES OF HYDROPHOBIC AND CHARGED RESIDUES, WHICH DICTATE THE ALPHA-HELICAL COILED-COIL STRUCTURE, ARE CONSERVED. FEATURES Location/Qualifiers source 1..1937 /organism="Homo sapiens" /db_xref="taxon:9606" 1..1937 Region 1..841 /note="GLOBULAR HEAD (S1)." /region_name="Domain" Protein 1..1937 /product="MYOSIN HEAVY CHAIN, PERINATAL SKELETAL MUSCLE" Site 132 /note="(TRI-)." /site_type="methylation" Site 181..188 /note="ATP." /site_type="np-binding" Region 658..680 /note="ACTIN-BINDING." /region_name="Domain" Site 698 /note="ALKYLATION (SH-1)." /site_type="modified" Site 708 /note="ALKYLATION (SH-2)." /site_type="modified" Region 760..774 /note="ACTIN-BINDING." /region_name="Domain" Region 842..1937 /note="RODLIKE TAIL (S2 AND LMM DOMAINS)." /region_name="Domain" Region 970 /note="Q -> E (IN REF. 2)." /region_name="Conflict" Region 1072 /note="M -> N (IN REF. 2)." /region_name="Conflict" Region 1247 /note="H -> N (IN REF. 2)." /region_name="Conflict" Region 1251..1252 /note="MC -> DGG (IN REF. 2)." /region_name="Conflict" Region 1261 /note="G -> E (IN REF. 2)." /region_name="Conflict" Region 1297 /note="Q -> K (IN REF. 2)." /region_name="Conflict" Region 1377..1378 /note="KY -> NT (IN REF. 2)." /region_name="Conflict" Region 1504..1505 /note="AH -> EN (IN REF. 2)." /region_name="Conflict" Region 1847 /note="D -> E (IN REF. 2)." /region_name="Conflict"

ORIGIN 1 msassdaema vfgeaapylr ksekerieaq nkpfdaktsv fvaepkesyv kstiqskegg

61 kvtvktegga tltvredqvf pmnppkydki edmammthlh epgvlynlke ryaawmiyty

121 sglfcvtvnp ykwlpvykpe vvaayrgkkr qeapphifsi sdnayqfmlt drenqsilit

181 gesgagktvn tkrviqyfat iavtgekkkd esgkmqgtle dqiisanpll eafgnaktvr

241 ndnssrfgkf irihfgttgk lasadietyl leksrvtfql kaersyhify qitsnkkpdl

301 iemllittnp ydyafvsqge itvpsiddqe elmatdsaid ilgftpeekv siykltgavm

361 hygnmkfkqk qreeqaepdg tevadkaayl qslnsadllk alcyprvkvg neyvtkgqtv

421 qqvynavgal akavyekmfl wmvtrinqql dtkqprqyfi gvldiagfei fdfnsleqlc

481 inftneklqq ffnhhmfvle qeeykkegie wtfidfgmdl aacieliekp lgifsileee

541 cmfpkatdts fknklydqhl gksanfqkpk vvkgkaeahf slihyagtvd ynitgwldkn

601 kdplndtvvg lyqksamktl aslfstyasa eadssakkga kkkgssfqtv salfrenlnk

661 lmtnlrsthp hfvrciipne tktpgamehe lvlhqlrcng vlegiricrk gfpsrilygd

721 fkqrykvlna saipegqfid skkaseklla sididhtqyk fghtkvffka gllglleemr

781 deklaqiitr tqavcrgflm rveyqkmlqr realfciqyn vrafmnvkhw pwmklffkik

841 pllksaetek ematmkeefq ktkdelakse akrkeleekm vtllkekndl qlqvqseads

901 ladaeerceq liknkiqlea kikevterae eeeeinaelt akkrkledec selkkdiddl

961 eltlakvekq khatenkvkn lteemaglde tiaklskekk alqethqqtl ddlqaeedkv

1021 niltkaktkl eqqvddlegs leqekklrmd lerakrkleg dlklaqestm dmendkqqld

1081 eklekkefei snliskiede qaveiqlqkk ikelqariee lgeeieaera srakaekqrs

1141 dlsreleeis erleeaggat saqvelnkkr eaefqklrrd leeatlqhea mvaalrkkha

1201 dsmaelgeqi dnlqrvkqkl ekekselkme tddlssnaea iskakghlek mcrsledqvs

1261 glktkeeeqq rlindltaqr arlqteagey srqldeqdal vsqlsrskqa stqqieelkh

1321 qleeetkakn alahalqssr hdcdllreqy eeeqegkael qralskanse vaqwrtkyet

1381 daiqrteele eakkklaqrl qeaeehveav nakcaslekt kqrlqneved lmldversna

1441 acaaldkkqr nfdkvlsewk qkyeetqael easqkesrsl stelfkvknv yeesldqlet

1501 lrrahknlqq eisdlteqia eggkqihele kikkqveqek ceiqaaleea easleheegk

1561 ilriqlelnq vksevdrkia ekdeeidqlk rnhtrvvetm qstldaeirs rndalrvkkk

1621 megdlnemei qlnhanrlaa eslrnyrntq gilketqlhl ddalrgqedl keqlaiverr

1681 anllqaeiee lwatleqter srkiaeqell daservqllh tqntslintk kklendvsql

1741 qseveeviqe srnaeekakk aitdaammae elkkeqdtsa hlermkknle qtvkdlqhrl

1801 deaeqlalkg gkkqiqklea rvrelegeve neqkrnaeav kglrkhdrrv keltyqteed

1861 rknvlrlqdl vdklqakvks ykrqaeeaee qsnanlskfr klqheleeae eradiaesqv

1921 nklrvksrev htkisae //