ID F6YKM1_HORSE Unreviewed; 1194 AA.
AC F6YKM1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 3.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
GN Name=PHKA1 {ECO:0000313|Ensembl:ENSECAP00000021732.3,
GN ECO:0000313|VGNC:VGNC:21390};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000021732.3, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000021732.3, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000021732.3,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000021732.3}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000021732.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC serine in certain substrates, including troponin I. The alpha chain may
CC bind calmodulin. {ECO:0000256|ARBA:ARBA00002837}.
CC -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC {ECO:0000256|ARBA:ARBA00005131, ECO:0000256|RuleBase:RU364123}.
CC -!- SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha,
CC beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB)
CC are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic
CC subunit, and delta is calmodulin. {ECO:0000256|ARBA:ARBA00025890,
CC ECO:0000256|RuleBase:RU364123}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004342,
CC ECO:0000256|RuleBase:RU364123}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004342, ECO:0000256|RuleBase:RU364123};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342,
CC ECO:0000256|RuleBase:RU364123}. Membrane
CC {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004423}.
CC -!- PTM: Although the final Cys may be farnesylated, the terminal
CC tripeptide is probably not removed, and the C-terminus is not
CC methylated. {ECO:0000256|PIRSR:PIRSR608734-50}.
CC -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC family. {ECO:0000256|ARBA:ARBA00007128, ECO:0000256|RuleBase:RU364123}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; F6YKM1; -.
DR Ensembl; ENSECAT00000026083.4; ENSECAP00000021732.3; ENSECAG00000023809.4.
DR VGNC; VGNC:21390; PHKA1.
DR GeneTree; ENSGT00950000183118; -.
DR HOGENOM; CLU_004177_1_0_1; -.
DR TreeFam; TF313970; -.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000002281; Chromosome X.
DR Bgee; ENSECAG00000023809; Expressed in muscle tissue and 23 other cell types or tissues.
DR ExpressionAtlas; F6YKM1; baseline.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011613; GH15-like.
DR InterPro; IPR045583; KPBA/B_C.
DR InterPro; IPR008734; PHK_A/B_su.
DR PANTHER; PTHR10749; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR10749:SF4; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT ALPHA, SKELETAL MUSCLE ISOFORM; 1.
DR Pfam; PF00723; Glyco_hydro_15; 1.
DR Pfam; PF19292; KPBB_C; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860,
KW ECO:0000256|RuleBase:RU364123};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU364123};
KW Cell membrane {ECO:0000256|RuleBase:RU364123};
KW Glycogen metabolism {ECO:0000256|ARBA:ARBA00022600,
KW ECO:0000256|RuleBase:RU364123};
KW Lipoprotein {ECO:0000256|PIRSR:PIRSR608734-50,
KW ECO:0000256|RuleBase:RU364123}; Membrane {ECO:0000256|RuleBase:RU364123};
KW Prenylation {ECO:0000256|PIRSR:PIRSR608734-50,
KW ECO:0000256|RuleBase:RU364123};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F6YKM1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281}.
FT DOMAIN 8..905
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT DOMAIN 1008..1110
FT /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19292"
FT REGION 990..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1191
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR608734-50"
SQ SEQUENCE 1194 AA; 133948 MW; 05EB180501526B34 CRC64;
MRSRSNSGVR LDGYARLVQQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA
YRKNADRDED KAKAYELEQV DKVESFKYSQ STKDSLHAKY NTRTCATVVG DDQWGHLQLD
ATSVYLLFLA QMTASGLHII HSLDEVNFIQ NLVFYIESAY KTADFGIWER GDKTNQGISE
LNASSVGMAK AALEALDELD LFGVKGGPQS VIHVLADEVQ HCQSILNSIL PRASTSKEVD
ASLLSVVSFP AFAVEDNQLV ELTKQEIITK LQGRYGCCRF LRDGYKTPKE DPNRLYYEPA
ELKLFENIEC EWPLFWTYFI LDGVFSGNVE QVQEYREALE AVLIKGKNGV PLLPELYSVP
PDKVDEEYQN PHTVDRIPMG KLPHMWGQSL YILGSLMAEG FLAPGEIDPL NRRFSTVPKP
DVVVQVSILA ETEEIKAILK NKGIDVETIA EVYPIRVQPA RILSHIYSSL GCNSRMKLSG
RPYRHMGVLG TSKLYDIRKT IFTFTPQFID QQQFYLALDN KMIVEMLRTD LSYLCSRWRM
TGQPTITFPI SHTMLDEDGT SLNSSILAAL RKMQDGYFGG ARVQTGKLSQ FLTTSCRTHL
SFMDPGPEGK LYSEDYDDNY NELESGDWMD DYGSSSNARC GDEVARYLDH LLAHTPPHPK
LAPTSQKGGL NRFQAAVQTT RDLMSLVTKA KELHVQNVHM YLPTKIFQAS RPSFNLLDSL
HHPREDQVPS VRVEIHLPRD RSGEVDFKAL VSQLRETSSL QEQADILYML YTMKGPDWDT
GLYDEGSATV RELLTELYGK VGEIRHWGLI RYISGILRKK VEALDEACTD LLSHQKHLTV
GLPPEPREKT ISAPLPYEVL TRLIDEASEG DMNISILTQE IMVYLAMYMR TQPGLFAEMF
RLRIGLIIQV MATELAHSLR CSAEEATDGL MNLSPSAMKN LLHHILSGKE FGVERSVRPT
DSNVSPAISI HEIGAVGATK TERTGIMQLK SEIKQSPGTS LTPKNGSLTS TYGQHPSKDS
RQGQWQRRRR LDGALNRVPV GFYQKVWKVL QKCHGLSVEG FVLPSSTTRE MTPGEIKFSV
HVESVLNRVP QPEYRQLLVE AILVLTMMAD IEIHSIGSII AVEKIVHIAN DLFVQEQKTL
GADDIMLAKD PASGICTLLY DSAPSGRFGT MTYLSKAAAT YVQEFLPHSI CAMQ
//
