ID A0A3B4XK94_SERLL Unreviewed; 935 AA.
AC A0A3B4XK94;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Peripheral plasma membrane protein CASK-like {ECO:0000313|Ensembl:ENSSLDP00000016696.1};
GN Name=CASK {ECO:0000313|Ensembl:ENSSLDP00000016696.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000016696.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000016696.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the MAGUK family.
CC {ECO:0000256|ARBA:ARBA00007014}.
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DR AlphaFoldDB; A0A3B4XK94; -.
DR Ensembl; ENSSLDT00000017294.1; ENSSLDP00000016696.1; ENSSLDG00000013074.1.
DR GeneTree; ENSGT00940000155600; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd12081; SH3_CASK; 1.
DR CDD; cd14094; STKc_CASK; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 6.10.140.620; -; 1.
DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR Gene3D; 1.10.287.650; L27 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035473; CASK_SH3.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23122; MEMBRANE-ASSOCIATED GUANYLATE KINASE MAGUK; 1.
DR PANTHER; PTHR23122:SF40; PERIPHERAL PLASMA MEMBRANE PROTEIN CASK; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF101288; L27 domain; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 14..278
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 339..394
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 398..451
FT /note="L27"
FT /evidence="ECO:0000259|PROSITE:PS51022"
FT DOMAIN 486..567
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 621..691
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 748..920
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 454..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 935 AA; 106260 MW; D8C8A79B428A4F97 CRC64;
MTMADDDVLF EDVYELCEVI GKGPFSVVRR CINRDTGQQF AVKIVDVASF TSSPGLSTED
LKREASICHM LKHPHIVELL ETYSSDGMLY MVFEFMDGAD LCFEIVKRAD AGFVYSEAVA
SHYMRQILEA LRYCHDNNVI HRDVKPHCVL LASKENSAPV KLGGFGVAIQ LGESGLVAGG
RVGTPHFMAP EVVKREPYGK PVDVWGCGVI LFILLSGCLP FYGTKERLFE AIIKGKYKMN
PRQWAHISES AKDLVRRMLM LDPAERITVY EALNHPWLKE RDRYAYKIHL PETVEQLRKF
NARRKLKGAV LAAVSSHKFN SYYGDPPEEL HDFSDDPTSS GAVSQVLDSL EEIHALTDCS
EKDMDFLHSV FQDQHLHTLL DLYDKINTRS SPQIRNPPSD GVQRAKEVLE TISCYPENME
AKELRRILTQ PHFMALLQTH DVVAHEVYSD EALRVTPPPT SPYLNGDSPD STNGDMDLEN
VTRVRLVQFQ KNTDEPMGIT LKMNDLNHCI VARIMHGGMI HRQGTLHVGD EIREINGISV
ANQTVEQLQK MLREMRGSIT FKIVPSYRSQ SMSCEKESPD LSRQSPANGH ASITSSILDL
PSTIQPKGRQ ITRPAIKDKL SIKIYVRAQF EYDPAKDDLI PCKEAGVRFR VGDIIQIISK
DDHNWWQGKL ENTKNGTAGL IPSPELQEWR VACIAMEKTK QEQQASCTWF GKKKKQYKDK
YLAKHNAVFD QLDLVTYEEV VKVPSFKRKT LVLLGAHGVG RRHIKNTLIT KHPDRFAYPI
PHTTRPPKKD EENGKNYYFV SHEQMMQDIS NNDYLEYGSH EDAMYGTRLE TIRQIHTQGM
ISILDVEPQA LKILRTAEFA PYVVFIAAPT ITPGMTEDDS LQRLQKESEM LQRTYAHYFD
QTVINNEIDD TIRLLEEAVD LVSTASQWVP VSWVY
//