ID A0A3Q1CVW1_AMPOC Unreviewed; 2846 AA.
AC A0A3Q1CVW1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Striated muscle preferentially expressed protein kinase-like {ECO:0000313|Ensembl:ENSAOCP00000029958.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000029958.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000029958.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR STRING; 80972.ENSAOCP00000029958; -.
DR Ensembl; ENSAOCT00000024540.1; ENSAOCP00000029958.1; ENSAOCG00000020690.1.
DR GeneTree; ENSGT00940000163418; -.
DR OMA; GIVTYIM; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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 InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47633:SF7; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47633; IMMUNOGLOBULIN; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 7.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 6.
DR SMART; SM00220; S_TKc; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 7.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 16..101
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 504..591
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 604..692
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 724..814
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 820..918
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1020..1108
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1132..1384
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 2171..2260
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2267..2358
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2530..2782
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 142..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1642..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1748..1834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1867..2045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2065..2163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2356..2429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2493..2527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1556
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1661..1681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1758..1792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1867..1890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1938..1959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1984..2006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2021..2037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2068..2094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2106..2129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2130..2154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2356..2382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2394..2414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2493..2525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2846 AA; 314719 MW; AC3309C5A2DF9C2C CRC64;
QVDVTDESVH RSISEPTAPV FIRKLRKAAV GTGCDIRLRV SVSGYPKPSL AWYHNDELLP
PSEGQDSGGL WIRDCRTSDA GLYTCVATNE LGEADCSAVL AVMDLGEGNH KMMDYNPDAS
DRRATLPGSY DPVVERELRA LGSRPPGSHL DPSNPARQRF SSLSSPQPPL STHRNSISSQ
KQEPDKTKPS DPKASKTDQT SNSVVMTPKL ARAGPKIFDK VRAFEERRSS VDLPGRATSF
DSDDSGKKTG GPSKEEILQG AAQKRAAFKQ RASSLEDKTS YSQRVQSYQS KFAEELQRIK
KLVGKPSLKK SYSTEQLSQK DRFNTGKLEP IPPQVVKKLE ARERALEERR DVDRTLQIHP
QAQGKDLQNQ SNNPEKEKMT HPDPQGKPRA SPVLVREPGS QYPPKPPRLT PSPTPSISPL
QKRRKAEAGR TSPALKMNIP TILVEDEPME TESVADKSKT RRREGRVRKS KKGRSAEPRS
PEEGRKHFII STDKCICKNP GATPKTALRI TREVKDVAVR AGESAMFECH ATGPTDVDVD
WLSNGKLIQP ALLNCKMHFD GKRCRLMLNS VHEDDSGTYT CKLSTAKEEL TSSANLKVAP
SKEPLFTRKL DVLEVIEGRT ARFDCKVSGS PAPRVTWMHF ETQVEESDNV RILQEGGRHS
LVITHVSSDT EGFYTAVAQN VHGKSECTAE LYMQEPRAAI MPFCFFFNYF PEMLENEVEK
RTMPDFVKPL ADVEVIEGKE VVLKCKVSGL PYPTIAWYHN GKRIESSEER KMTQYRDVHN
LVIRSACHAH GGVYKAVISN KVGKAACYAH LYVTDIVPDP PDGPPLIEAI TGKTITLSWK
RPKRIDPSFD SSSLLYVVQQ QPLGSIQWSV VASSLRETNY TVPSLSKGVR YAFRVLTSTG
KTLSKPSPST DLVHLLDRGP YLRKAPVILE KPDIVYVVES QPASITITLN HVHAVVTWKR
RGVALVNRPG MFEMSMPDDD QHTLKLQRVK STDIGQLVVT ASNQFGSDLC TLQLAMAVAP
KFESIMEDVD VHVGETSRLA VVVEGKPDPD ILWYKDDELL SESSHFTFVY DDPEYSLVVL
NAHPDHSGVY TCTAKNLAGS NSCKAELTVH TAEPMEDEGT ILRKMRRLTD YYDIHKEIGR
GAYSYVKRVT HKKGKAEFAA KFISARRKRK ALALREMDLL SELDNERILY FHDAFEKKNM
VVLITELCHE ELLERMAKKT AVMELEVCVS SVQQVLEGLR YLHQKSIAHL DIKPENILMS
GPGSDHIRIC DFGNAIKLET SEEHYSKYGT PEYVAPEIVN QTPVTTATDI WPVGVITYLC
LTGVSPFAGE NDRATALNIR NYNVAFEESM FSDLCKEARG FVIKLLVVDR LRPSAIECLR
HPWFKVSYLG KLNNLTLSCV YFIQRSLINY KSKMVMRSIP ELLNDSCSHV SIAVARHLKE
GSPPASSSSD SDADVDELPF IPMPLSMVFS GSRVSLNEIP GDEDVSGLPS VCADGTRKLN
NMDVIGTRGG AGKRLTDEER SPDEEKMDKT KRAPLKKGSS VESDESQTKS RRATMRRGSS
ADSALLLHID PEEGNADEDS EASNKSLKKA VSMELPNRSP SPGAAKLSQE DYALKLELMR
QRLLRGGNVD KKMSGLRGPL FETLGMEDER QTGSLDRNLR RSRAGPSTLT RAASSDNTVD
DTPKTKVFRK SASFTQGDSE PMPLHRRFGA PLEIPSMGNG NVESKKLQEA TSMSSQSPSV
ITPIIVIEEE DDEEERSDDQ VLHINEKETK GNEKTLQNRK PSPDKAQSKD QKVKTTDAST
LPEHPAVFAK VAPADRSPAS VSSTSNPDLA IPRQPLLRTD IKDIDSEEVF EARFKKRESS
LTRGLRKLTR NKSEEKSPVL SRKVADGSEE VYRPGPRGAP LEIVSKGLQE KSKSVQDLRS
EDQETGLGLI GRLSLRAKRS TSTEKKGEKP KEEKQQNAQE SATSKRVSWA IGRSKSLDTK
ELNSAQRQLD DREQRKADES SVSAMRRKFE SKVAGISAKI RTQSEERKDK DSVESQKGLN
KVTDSPVVAL RNKFENKVAG ISTKLRSQSE ERIGDGEGKT TPLLTRHRHS QSEGRGLKGM
GIPENQLAKQ TCSAASKESV ESTSSIQSEK ASESDRRSRW DRWGLTRSKK DKTPSQSDLP
SAIPKEEDFA PVFHIKLKDH VLLEGEPVTL SCLPAGSPHP EITWMKDRKP LEVDDRMSLV
SHPDGRQLLM IMKSSHRDAG VYECVATNPI AAITTSCTLS IACIPKRPGT PEVPQTYNNT
ALVLWKPADT KSPCSYTLER KTEGDSSWLT VVTGVADCYY NVTDLPAGGA FRFRVCCVNK
AGQGPYSNTS ATVSLDSTGT SNNAPKTTVS MITSTSSPPK DAAVSPSSPP SKPPSEGTAT
TEDAPKISST LPSSPTIKAP PPFVLPKPQS PVNVVTPMTQ TPPVSPPPVL VTPPSTPTKP
VVASVPSYIP TSTATARVAP SPVSFSPPVL QTSSLSPIGE GASTPSRGTP SGRATPSTGS
LRQGVPQKPY TFLDEKGRGR FGVVRECREN ATGKIYMAKI VPYSQENKQE ILKEYEILKS
LHNERVMALH EAYVTPRYLV LVAEYCTGKE LLYSLIDRFR YSEDDVAGYL VQILQGVEYL
HSRRVLHLDL KPDNIVVTNL NAVKIVDFGS AQSFNPLNLK QQESGAGTLE YMAPEMVKGE
VVGPPADIWT VGVVTYIMLS GRLPFEDKDP QLVESKILMA KFEPTKLYSN VSQSASAFLK
KMLSSYPWAR PTTRDCFTQA WLQDSYLMKL RRQTLTFTSG RLKEFLVEQQ CRRTDSATKH
KVLLRTYQSS PQSLASGSAP HVPSTK
//
