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Database: UniProt
Entry: G3SCK0_GORGO
LinkDB: G3SCK0_GORGO
Original site: G3SCK0_GORGO 
ID   G3SCK0_GORGO            Unreviewed;       542 AA.
AC   G3SCK0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Testis associated actin remodelling kinase 2 {ECO:0000313|Ensembl:ENSGGOP00000025828.2};
GN   Name=TESK2 {ECO:0000313|Ensembl:ENSGGOP00000025828.2};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000025828.2, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000025828.2, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000025828.2, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000025828.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   EMBL; CABD030002903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030002904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030002905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G3SCK0; -.
DR   Ensembl; ENSGGOT00000026110.2; ENSGGOP00000025828.2; ENSGGOG00000003296.3.
DR   GeneTree; ENSGT00940000158765; -.
DR   HOGENOM; CLU_018577_1_1_1; -.
DR   Proteomes; UP000001519; Chromosome 1.
DR   Bgee; ENSGGOG00000003296; Expressed in testis and 6 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR46485:SF6; DUAL SPECIFICITY TESTIS-SPECIFIC PROTEIN KINASE 2; 1.
DR   PANTHER; PTHR46485; LIM DOMAIN KINASE 1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT   DOMAIN          58..312
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          490..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   542 AA;  60350 MW;  F34131A240950516 CRC64;
     MDRSKRNSIA GFPPRVERLE EFEGGGGGEG NVSQVGRVWP SSYRALISAF SRLTRLDDFT
     CEKIGSGFFS EVFKVQHRAS GQVMALKMNT LSSNRANMLK EVQLMNRLSH PNILRFMGVC
     VHQGQLHALT EYINSGNLEQ LLDSNLHLPW TVRVKLAYDI AVGLSYLHFK GVFHRDLTSK
     NCLIKRDENG YSAVVADFGL AEKIPDVSMG SEKLAVVGSP FWMAPEVLRD EPYNEKADVF
     SYGIILCEII ARIQADPDYL PRTEMDPKLR PSFVEIGKTL EEILSRLQEE EQERDRKLQP
     TARGLLEKAP GVKRLSSLDD KIPHKSPCPR RTIWLSRSQS DIFSRKPPRT VSVLDPYYRP
     RDGAARTPKV NPFSARQDLM GGKIKFFDLP SKSVISLVFD LDAPGPGTMP LADWQEPLAP
     PIRRWRSLPG SPEFLHQEAC PFVGREESLS DGPPPRLSSL KYRVKEIPPF RASALPAAQA
     HEAMDYSILQ EENGFGSRPQ GTSPCPAGAS EEMEVEERPA GSTPATFSTS GIGLQTQGKQ
     DG
//
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