ID B2R5T5_HUMAN Unreviewed; 381 AA.
AC B2R5T5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit {ECO:0000256|ARBA:ARBA00039637};
GN Name=PRKAR1A {ECO:0000313|EMBL:EAW89060.1};
GN ORFNames=hCG_28462 {ECO:0000313|EMBL:EAW89060.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG35232.1};
RN [1] {ECO:0000313|EMBL:EAW89060.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11181995; DOI=10.1126/science.1058040;
RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT "The sequence of the human genome.";
RL Science 291:1304-1351(2001).
RN [2] {ECO:0000313|EMBL:BAG53489.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:BAG53489.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M.,
RA Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S.,
RA Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S.,
RA Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H.,
RA Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M.,
RA Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M.,
RA Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y.,
RA Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N.,
RA Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S.,
RA Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T.,
RA Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M.,
RA Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y.,
RA Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y.,
RA Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T.,
RA Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3] {ECO:0000313|EMBL:EAW89060.1}
RP NUCLEOTIDE SEQUENCE.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:BAG35232.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:BAG35232.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y.,
RA Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R.,
RA Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N.,
RA Isogai T.;
RT "NEDO functional analysis of protein and research application project.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:ADO22565.1}
RP NUCLEOTIDE SEQUENCE.
RA Hoernsten L., Su C., Osbourn A.E., Hellman U., Wernstedt C., Oliw E.H.;
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
CC involved in cAMP signaling in cells. {ECO:0000256|ARBA:ARBA00037751}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000256|ARBA:ARBA00005753}.
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 EMBL; GQ901048; ADO22565.1; -; mRNA.
DR EMBL; AK312307; BAG35232.1; -; mRNA.
DR EMBL; AK097580; BAG53489.1; -; mRNA.
DR EMBL; CH471099; EAW89060.1; -; Genomic_DNA.
DR RefSeq; NP_001263218.1; NM_001276289.1.
DR RefSeq; NP_001265362.1; NM_001278433.1.
DR RefSeq; NP_002725.1; NM_002734.4.
DR RefSeq; NP_997636.1; NM_212471.2.
DR RefSeq; NP_997637.1; NM_212472.2.
DR RefSeq; XP_011523285.1; XM_011524983.2.
DR RefSeq; XP_011523286.1; XM_011524984.2.
DR RefSeq; XP_011523287.1; XM_011524985.2.
DR SMR; B2R5T5; -.
DR Antibodypedia; 31783; 422 antibodies from 35 providers.
DR DNASU; 5573; -.
DR GeneID; 5573; -.
DR KEGG; hsa:5573; -.
DR CTD; 5573; -.
DR PharmGKB; PA33754; -.
DR VEuPathDB; HostDB:ENSG00000108946; -.
DR HOGENOM; CLU_018310_1_0_1; -.
DR OMA; EHIVMAS; -.
DR OrthoDB; 55978at2759; -.
DR BioGRID-ORCS; 5573; 106 hits in 1172 CRISPR screens.
DR ChiTaRS; PRKAR1A; human.
DR GenomeRNAi; 5573; -.
DR ExpressionAtlas; B2R5T5; baseline and differential.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl.
DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097224; C:sperm connecting piece; IEA:Ensembl.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IEA:Ensembl.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IEA:Ensembl.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; IEA:Ensembl.
DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR CDD; cd00038; CAP_ED; 2.
DR CDD; cd12101; DD_RIalpha_PKA; 1.
DR Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1.
DR PANTHER; PTHR11635:SF129; CAMP-DEPENDENT PROTEIN KINASE TYPE I-ALPHA REGULATORY SUBUNIT; 1.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 1.
DR PIRSF; PIRSF000548; PK_regulatory; 1.
DR PRINTS; PR00103; CAMPKINASE.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 2.
DR SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
PE 2: Evidence at transcript level;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW cAMP {ECO:0000256|ARBA:ARBA00023149, ECO:0000256|PIRSR:PIRSR000548-1};
KW cAMP-binding {ECO:0000256|ARBA:ARBA00022566, ECO:0000256|PIRSR:PIRSR000548-
KW 1}; Kinase {ECO:0000313|EMBL:BAG35232.1};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000548-1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:BAG35232.1}.
FT DOMAIN 137..252
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT DOMAIN 255..376
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
FT REGION 64..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 202
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT BINDING 211
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT BINDING 326
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
FT BINDING 335
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000548-1"
SQ SEQUENCE 381 AA; 42982 MW; 2D04F08CE8857A6D CRC64;
MESGSTAASE EARSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL REYFERLEKE
EAKQIQNLQK AGTRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPK
DYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFSVSFIA GETVIQQGDE GDNFYVIDQG
ETDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL
RKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGSA
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLG
PCSDILKRNI QQYNSFVSLS V
//
