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MYBPH_CHICK
ID   MYBPH_CHICK             Reviewed;         537 AA.
AC   Q05623;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Myosin-binding protein H;
DE            Short=MyBP-H;
DE   AltName: Full=86 kDa protein;
DE   AltName: Full=H-protein;
GN   Name=MYBPH;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-37.
RC   TISSUE=Pectoralis muscle;
RX   PubMed=7679114; DOI=10.1016/s0021-9258(18)53745-5;
RA   Vaughan K.T., Weber F.E., Einheber S., Fischman D.A.;
RT   "Molecular cloning of chicken myosin-binding protein (MyBP) H (86-kDa
RT   protein) reveals extensive homology with MyBP-C (C-protein) with conserved
RT   immunoglobulin C2 and fibronectin type III motifs.";
RL   J. Biol. Chem. 268:3670-3676(1993).
CC   -!- FUNCTION: Binds to myosin; probably involved in interaction with thick
CC       myofilaments in the A-band.
CC   -!- TISSUE SPECIFICITY: Skeletal muscle. Seems to be also expressed in the
CC       slow tonic ald muscle. Not detected in gizzard or heart.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC       {ECO:0000305}.
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DR   EMBL; L05605; AAA21418.1; -; mRNA.
DR   PIR; A46611; A46611.
DR   RefSeq; NP_001026199.1; NM_001031028.2.
DR   AlphaFoldDB; Q05623; -.
DR   SMR; Q05623; -.
DR   STRING; 9031.ENSGALP00000039903; -.
DR   GeneID; 421154; -.
DR   KEGG; gga:421154; -.
DR   CTD; 343263; -.
DR   VEuPathDB; HostDB:geneid_421154; -.
DR   eggNOG; ENOG502QVIQ; Eukaryota.
DR   HOGENOM; CLU_037185_0_0_1; -.
DR   InParanoid; Q05623; -.
DR   OrthoDB; 653839at2759; -.
DR   PhylomeDB; Q05623; -.
DR   PRO; PR:Q05623; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0031672; C:A band; IDA:AgBase.
DR   GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 2.
DR   Gene3D; 2.60.40.10; -; 4.
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; 2.
DR   Pfam; PF07679; I-set; 2.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SUPFAM; SSF48726; SSF48726; 2.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   Cell adhesion; Direct protein sequencing; Immunoglobulin domain;
KW   Muscle protein; Reference proteome; Repeat; Thick filament.
FT   CHAIN           1..537
FT                   /note="Myosin-binding protein H"
FT                   /id="PRO_0000072701"
FT   DOMAIN          137..232
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          236..324
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          333..428
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          444..528
FT                   /note="Ig-like C2-type 2"
FT   REGION          1..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..87
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        2
FT                   /note="T -> G (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        9
FT                   /note="A -> P (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        15
FT                   /note="A -> K (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   537 AA;  58679 MW;  06C4CF0EFE1DD233 CRC64;
     MTGKTAPAAA KKAPAAKKAP APASKKAPEP APKEKPAPTP KEGHAPTPKE EHAPPPKEEH
     APPPKEEHAP APAAETPPAP EHPPDAEQPA APAAEHAPTP THEAAPAHEE GPPPAAPAEA
     PAPEPEPEKP KEEPPSVPLS LAVEEVTENS VTLTWKAPEH TGKSSLDGYV VEICKDGSTD
     WTAVNKEPFL STRYKIHDLA SGEKVHVRVK AISASGTSDP ATLEQPVLIR EITDLPRIRL
     PRQLRQVYVR HVGEAVNLLI PFQGKPQPQV TWTKDNQPLD TSRVNIRNTD KDTIFFIRTA
     QRSDSGKYQL SVRINGAEDK AILDIRVIER PGPPQNLKLV DVWGFNVALE WSPPADNGNS
     EIKGYTVQKS DKKSGKWFTV LERCTRTSCT ISDLIIGNTY SFRVFSENAC GMSETAAVAA
     GVAHIKKTVY QPQKIPERDM MEPPKFTQPL TDRATTRGYS THLFCSVRGF PQPKIIWMKN
     KMEIREDPKY IAMIEQGVCS LEIRKPSPFD AGVYTCKAVN PLGEASVDCK LDVKMPK
 
 
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