ID A0A096NYA9_PAPAN Unreviewed; 2153 AA.
AC A0A096NYA9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Alpha kinase 2 {ECO:0000313|Ensembl:ENSPANP00000018071.3};
GN Name=ALPK2 {ECO:0000313|Ensembl:ENSPANP00000018071.3};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000018071.3, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000018071.3, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000018071.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000256|ARBA:ARBA00008651}.
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 STRING; 9555.ENSPANP00000018071; -.
DR Ensembl; ENSPANT00000019903.3; ENSPANP00000018071.3; ENSPANG00000018740.3.
DR eggNOG; ENOG502QPP5; Eukaryota.
DR GeneTree; ENSGT00940000160524; -.
DR HOGENOM; CLU_002011_0_0_1; -.
DR Proteomes; UP000028761; Chromosome 19.
DR Bgee; ENSPANG00000018740; Expressed in skeletal muscle tissue and 11 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd20951; IgI_titin_I1-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR InterPro; IPR004166; a-kinase_dom.
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; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR47091:SF2; ALPHA-PROTEIN KINASE 2; 1.
DR PANTHER; PTHR47091; ALPHA-PROTEIN KINASE 2-RELATED; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00811; Alpha_kinase; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 3: Inferred from homology;
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 92..196
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1798..1886
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1913..2153
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1479..1551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..1625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1676..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1763..1794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1143..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2153 AA; 236100 MW; B65B84FC2B616C44 CRC64;
MQLNVLQCTG HPRNTEGSSP PTSSTTAWKG CPDLQSVHQP AYNELPGRHP VVSGIPKKAR
EIPEQMVMSG IFFFFRFMWH ERMTDSEAPQ RPPLCFLSTL LSQKVPEKSD AVLRCIISGQ
PKPEVTWYKN GQAMNESGIV SSYEFFKKQY IHVLHLSCCT KNDAAVYQIS AKNSFGIICC
SASVEVECSS ENPQLSPNLE DDRDTGWKHE TGTCEEESAN QIDEKEHLYK EEESISPGTP
RSNHSLSLQS LGNLDISVSS SENPLGVKGT RHPGEAYDPS NTEEIADSLL FLNSSHVYEK
QDELCHKTVH STASKFTGGG LNNDGPHEEG LHSSQQNPKV QKYISLSLPL SEATAHIYPG
DNAVAKKQPS PQVSSEDSDS DYELCPEITL TYTEEFSDDD LEYLECSDVM TDYSNAVWQR
NLLGTEHVFL LESDDEEMEF GMTLTLGPHQ DGMSSVTEQR RCKLPTAPEA AENDYPGIQG
ETRDSHQARE EFASDNLLNM DESVRETEMK PLSGESENSG MSQCWETAAE KRVGGKDLWS
ERGSQQPARV RQLGMKGNPK KPNANLRENT TEGTLHLCYA KESAKHPLTQ SDKRETSHST
AAATGRNSHA DAGECAISTQ AEQEAKTLQT STDSPSKEGN TNCKGEGMQV NSLFETSQVP
DWSDHPQVQI QETVRERISC SQMPAFSEPA GEESPFTGTT TISFSNLGGV HKENASLAQH
LEVKPCTYDP QQEEKQDRDG NTPDNFREDL KHELRTSEAN DENTFPGVFS RHLPKDARAD
FREPVAVSVA SPETTDTVLT LENVCDGPRD REAVCAIQCF EAGDQGTCFD TIDSLVGAPA
DKYLPQEICS VDLELAEGQR KVSDLCSPNG KTLEVLFQTQ VSETSVSTYK SSKDGDSVMS
PLFISTFTLN ISHTASEGAT EENLAKVENS TCPLASTVHA GQERSSPNNS GRLEETQLLS
SENNPLVQFE EGGDKSPSPS AADTTDTLAS YSSVVSFPWE KTSTLTANNG FQVTRETEDT
STVTTATKVH PAKYLAVSIP EDKHASGTEE RFPRASHEKV SQFPSQVQLG HILSGATTKS
TKELLCTAPS VPGVPHHVLQ LPEGEDFFSN SPLQVDNLSG DKSQTVERAD FRSHEENFQE
RGSETKQGLQ QQSLSHQGSL SAPDFQESLP TTSAAQEEIN LVPSAHSPAS SREGAGQRSV
WGMRVSVVAE TAGEEDSQAL SNVPSLSDII LEESKEYRPG NWEAGNKLKI ITLEASASEI
RPPRQRTNSE SKASDGGPVI PDKVWAVPDS LKADTVVPEL APSEIAASAH SPEDADSALA
DSRESHKGDK PAISAHWRSL SSWGFSQPRL LESSVDPVDG KELCVTDSLS VASETGGKEN
VNNVSQDQEE KQLKMDHTAF FKKFLTCSKI LESSVDPIDE TSVIEYTRAG KPEPSESTPE
GAREGSQSND GNVGHGAKIQ PAILQVPCLQ GTILTENRIS RSQEGSMKRE AEQSQPDEAK
TTIWQVLQPS EGGERIPSGC SIGQTQESSD GSLGEAEQSK KDKAELISPT SSLSSCLPIM
THASLGVDAH DSTGQIHDVP ENDLVEPRNR QYVFPVSQKR GTIENERGKP LPSSPHLTRL
PCTSSPEGNV TNFLISHKME EPKIEVLQTG ETKPPSSSSS SAKTLAFISG EDELEKAPKL
LQDPHPKGTL RCVKKSRERE KSLEAQAGKS PGALTAVTGS EEVKRKPEAP GSGHLAEGVK
KKILSKVAAL RLKLEEKENA RKNSAFLKKM PKLETSLSRT EEKQDPKKPS CKGEGRAPVL
LKKIQAEMFP EHSGNVKLSC QFAEIHEDST ICWTKDSKSI AQVQRSAGDN STVSFAIVQA
SLKDQGLYYC CIKNSYGKVT AEFNLTAEVL KQLSSRQDTK GCEEIEFSQL IFKEDFLHDS
YFGGRLRGQI ATEELHFGEG VHRKAFRSTV MHGLTPVFKP GHACVLKVHN AVAYGTRNND
ELIQRNYKLA AQECYVQNTA RYYAKIYAAE AQPLEGFGEV PEIIPIFLIH RPENNIPYAT
VEEELIGEFV KYSIRDGKEI NFLRRESEAG QKCCTFQHWV YQKTSGCLLV TDMQGVGMKL
TDVGIATLAK GLQHLKSETS ERMLSQWSWY LSPGRILWWA RGCAGPFRAG RWS
//
