ID F1LLZ7_RAT Unreviewed; 1224 AA.
AC F1LLZ7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 3.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Phosphorylase b kinase regulatory subunit {ECO:0000256|RuleBase:RU364123};
GN Name=Phka1 {ECO:0000313|Ensembl:ENSRNOP00000046508.5,
GN ECO:0000313|RGD:621522};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000046508.5, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000046508.5, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000046508.5,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000046508.5}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000046508.5};
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}.
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DR AlphaFoldDB; F1LLZ7; -.
DR jPOST; F1LLZ7; -.
DR PeptideAtlas; F1LLZ7; -.
DR Ensembl; ENSRNOT00000041138.6; ENSRNOP00000046508.5; ENSRNOG00000003063.9.
DR RGD; 621522; Phka1.
DR GeneTree; ENSGT00950000183118; -.
DR HOGENOM; CLU_004177_1_0_1; -.
DR TreeFam; TF313970; -.
DR UniPathway; UPA00163; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000003063; Expressed in skeletal muscle tissue and 19 other cell types or tissues.
DR ExpressionAtlas; F1LLZ7; baseline and differential.
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:F1LLZ7};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT DOMAIN 8..922
FT /note="GH15-like"
FT /evidence="ECO:0000259|Pfam:PF00723"
FT DOMAIN 1045..1141
FT /note="Phosphorylase b kinase regulatory subunit alpha/beta
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19292"
FT REGION 1039..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1221
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000256|PIRSR:PIRSR608734-50"
SQ SEQUENCE 1224 AA; 137222 MW; 6871D432DFD5818C CRC64;
MRSRSNSGVR LDGYARLVHQ TILCHQNPVT GLLPASYDEK DAWVRDNVYS ILAVWGLGLA
YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE SFKYSQSTKD SLHAKYNTKT
CATVVGDDQW GHLQLDATSV YLLFLAQMTA SGLHIIHSLD EVNFIQNLVF YIEAAYKTAD
FGIWERGDKT NQGISELNAS SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS
ILNSLLPRAS TSKEVDASLL SVVSFPAFAV EDSHLVEITK QEIITKLQGR YGCCRFLRDG
YKTPKEDPNR LYYEPAELKL FENIECEWPL FWTYFILDGI FSGNTEQVQE YREALDAVLI
KGKNGVPLLP ELYSVPPDRV DEEYQNPHTV DRVPMGKLPH MWGQSLYILG NLMAEGFLAP
GEIDPLNRRF STVPKPDVVV QVSILAETEE IKAILKDKGI DVETIAEVYP IRVQPARILS
HIYSSLGCNS RMKLSGRPYR LMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNQMIV
EMLRTDLSYL CSRWRMTGQP TITFPISHTM LDEDGASLNS SILAALRKMQ DGYFGGARIQ
TGKLSEFLTT SCCTHLSFMD PGPEGKLYSE DYDEDYDDEL DSGNWMDSYD STRNARCGDE
VARYLDHLLA HTGPHPKLTP TSRKGGLDRF RAAVQTTCDL MSLVAKAKEL HIQNVHMYLP
TKLFQPSRPS LNLLDSPESP QDSQVPSVRV EVHLPRDQSG EVDFQSLVSQ LKETSSLQEQ
ADILYMLYTM KGPDWNTELY EEGGSTVREL LSELYVKVGE IRHWGLIRYI SGILRKKVEA
LDEACTDLLS YQKHLTVGLP PEPREKTISA PLPYEALTKL IDEASEGDMN ISTLTQEIMV
YLAMYMRTQP GLFAEMFRLR IGLIIQVMAT ELAHSLRCSA EEATEGLMNL SPSAMKNLLH
HILSGKEFGV ERSVRPTDSN VSPAISIHEI GAVGATKTER TGIMQLKSEI KQVEFRRLSV
SPESQSPAAC ISASSGSFPT VCEPQTSKDS RQGQWQRRRR LDGALNRVPI GFYQKVWKIL
QKCHGLSVEG FVLPSSSTRE MTPGEIKFSV HVESVLNRVP QPEYRQLLVE AILVLTMLAD
IEIHSIGSII AVEKIVHIAN DLFLQEQKTL GADDIMLAKD PASGICTLLY DSAPSGRFGT
MTYLSKAAAT YVQEFLPHSL CAMQ
//
