MYPC2_CHICK
ID MYPC2_CHICK Reviewed; 1132 AA.
AC P16419; Q90606;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Myosin-binding protein C, fast-type;
DE Short=Fast MyBP-C;
DE AltName: Full=C-protein, skeletal muscle fast isoform;
GN Name=MYBPC2;
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 2-25; 183-199 AND
RP 1031-1045.
RC TISSUE=Skeletal muscle;
RX PubMed=8227129; DOI=10.1083/jcb.123.3.619;
RA Okagaki T., Weber F.E., Fischman D.A., Vaughan K.T., Mikawa T.,
RA Reinach F.C.;
RT "The major myosin-binding domain of skeletal muscle MyBP-C (C protein)
RT resides in the COOH-terminal, immunoglobulin C2 motif.";
RL J. Cell Biol. 123:619-626(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 140-1132.
RC TISSUE=Skeletal muscle;
RX PubMed=2315308; DOI=10.1073/pnas.87.6.2157;
RA Einheber S., Fischman D.A.;
RT "Isolation and characterization of a cDNA clone encoding avian skeletal
RT muscle C-protein: an intracellular member of the immunoglobulin
RT superfamily.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2157-2161(1990).
CC -!- FUNCTION: Thick filament-associated protein located in the crossbridge
CC region of vertebrate striated muscle a bands. In vitro it binds MHC, F-
CC actin and native thin filaments, and modifies the activity of actin-
CC activated myosin ATPase. It may modulate muscle contraction or may play
CC a more structural role.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. MyBP family.
CC {ECO:0000305}.
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DR EMBL; U00922; AAC59644.1; -; mRNA.
DR EMBL; U00923; AAC04307.1; -; mRNA.
DR EMBL; M31209; AAA49068.1; -; mRNA.
DR PIR; A48668; A35089.
DR RefSeq; NP_001038124.1; NM_001044659.1.
DR AlphaFoldDB; P16419; -.
DR PRIDE; P16419; -.
DR GeneID; 425457; -.
DR CTD; 4606; -.
DR VEuPathDB; HostDB:geneid_425457; -.
DR InParanoid; P16419; -.
DR OrthoDB; 67092at2759; -.
DR PhylomeDB; P16419; -.
DR PRO; PR:P16419; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0031672; C:A band; IDA:AgBase.
DR GO; GO:0014705; C:C zone; IDA:UniProtKB.
DR GO; GO:0032982; C:myosin filament; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030241; P:skeletal muscle myosin thick filament assembly; IDA:UniProtKB.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 10.
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 InterPro; IPR040849; MyBP-C_THB.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 7.
DR Pfam; PF18362; THB; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 7.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Actin-binding; Cell adhesion; Direct protein sequencing;
KW Immunoglobulin domain; Muscle protein; Reference proteome; Repeat;
KW Thick filament.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8227129"
FT CHAIN 2..1132
FT /note="Myosin-binding protein C, fast-type"
FT /id="PRO_0000072692"
FT DOMAIN 48..149
FT /note="Ig-like C2-type 1"
FT DOMAIN 249..338
FT /note="Ig-like C2-type 2"
FT DOMAIN 339..429
FT /note="Ig-like C2-type 3"
FT DOMAIN 430..530
FT /note="Ig-like C2-type 4"
FT DOMAIN 531..630
FT /note="Ig-like C2-type 5"
FT DOMAIN 633..729
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 731..826
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 830..923
FT /note="Ig-like C2-type 6"
FT DOMAIN 926..1022
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1039..1132
FT /note="Ig-like C2-type 7"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1132 AA; 126943 MW; 0A7D8B3141BAF901 CRC64;
MPEPSKAAPK KEAKKKEEKK EEKKEAPPPQ EHKDEAPDDV HPPETPDPEG LFLSKPQNVM
VESGRDVTVS ARVAGAALPC APAVKWFKGK WAELGDKSAR CRLRHSVDDD KVHTFELTIT
KVAMGDRGDY RCEVTAKEQK DSCSFSIDVE APRSSEGNVL QAFKRTGEGK DDTAGELDFS
GLLKKREVQV EEKKKKKDED DQFPPEIWEL LKGVTKKSEY ERIAFQYGIT DLRGMLKRLK
KVHVEPKKSE AFIRKLDPAY QVDKGNKIKL VVELSDPDLP LKWYKNGQLL KPSTKYVFEN
VGLKRILTIH KCSLADDAAY ECRVNDEKCF TEVFVKEPPV TVVRGLEDQQ VVVGDRVVLE
AEVSEEGAQV MWLKDGVDVT RDDAFKYRFK KDGKKHFLII NEAELSDSAH YKIMTNGGES
EAELSVEEKQ LEVLQDMADL TVKASEQAVF KCEVSDEKVT GRWFRNGVEV KPSKRIHISH
NGRFHKLVID DVRPEDEGDY TFIPDGYALS LSAKLNFLEI KVEYVPKQEP PKIHLDCSGK
AAENTIVVVA GNKVRLDVPI SGEPAPTVTW KRGDQLFTAT EGRVHIDSQA DLSSFVIESA
ERSDEGRYCI TVTNPVGEDS ATLHVRVVDV PDPPQSVRVT SVGEDWAVLS WEAPPFDGGM
PITGYLMERK KKGSMRWMKL NFEVFPDTTY ESTKMIEGVF YEMRVFAVNA IGVSQPSLNT
QPFMPIAPTS EPTHVVLEDV TDTTATIKWR PPERIGAGGV DGYLVEWCRE GSNEWVAANT
ELVERCGLTA RGLPTGERLL FRVISVNMAG KSPPATMAQP VTIREIVERP KIRLPRHLRQ
TYIRRVGEQV NLVIPFQGKP RPQVTWSREG GALPAEVQTR TSDVDSVFFI RSAARPLSGN
YEMRVRIDNM EDCATLRLRV VERPGPPQAV RVMEVWGSNA LLQWEPPKDD GNAEISGYTV
QKADTRTMEW FTVLEHSRPT RCTVSELVMG NEYRFRVYSE NVCGTSQEPA TSHNTARIAK
EGLTLKMVPY KERDLRAAPQ FLTPLVDRSV VAGYTVTLNC AVRGHPKPKV TWLKNSVEIG
ADPKFLSRHG LGVLSLLIRR PGPFDGGTYG CRAVNEMGEA TTECRLDVRV PQ
