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CAMKV_TAKRU
ID   CAMKV_TAKRU             Reviewed;         421 AA.
AC   Q9YGM4;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=CaM kinase-like vesicle-associated protein;
GN   Name=camkv;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=10025966; DOI=10.1016/s0014-5793(99)00011-3;
RA   Cottage A., Clark M., Hawker K., Umrania Y., Wheller D., Bishop M.,
RA   Elgar G.;
RT   "Three receptor genes for plasminogen related growth factors in the genome
RT   of the puffer fish Fugu rubripes.";
RL   FEBS Lett. 443:370-374(1999).
CC   -!- FUNCTION: Does not appear to have detectable kinase activity.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with calmodulin, in the presence of calcium.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane
CC       protein. Note=May be associated with vesicular structures.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:10025966}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000305}.
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DR   EMBL; AJ010348; CAA09101.1; -; Genomic_DNA.
DR   PIR; T30814; T30814.
DR   AlphaFoldDB; Q9YGM4; -.
DR   SMR; Q9YGM4; -.
DR   STRING; 31033.ENSTRUP00000026495; -.
DR   PRIDE; Q9YGM4; -.
DR   eggNOG; KOG0032; Eukaryota.
DR   InParanoid; Q9YGM4; -.
DR   Proteomes; UP000005226; Unplaced.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; Cytoplasmic vesicle; Membrane; Reference proteome.
FT   CHAIN           1..421
FT                   /note="CaM kinase-like vesicle-associated protein"
FT                   /id="PRO_0000250098"
FT   DOMAIN          24..284
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          326..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   421 AA;  47328 MW;  07C6A9EFE44C96E4 CRC64;
     MPFGCLTLGE KKDYNSPSEV TDKYDLGQVV KSEEFCEIFR AKDRNTLKMY TCKKFNKKDG
     RKVRKAAKNE IMILKMVKHH NILQLVDAFE TKKEYFIFLE LATGREVFDW ILDQGYYSER
     DTSNVMRQVL EAVAYLHSLK IVHRNLKNLV YFNRLKHSKI VISDFQLAKL ENGLIKDPCG
     TPEYLAPEVI GRQRYGRPVD CWAIGVIMYI LLSGNPPFYD DGDEEDSDSR DKNLFLKILS
     GDYEFDSPYW DDISDSAKTL VASLMEVDQD QRLTAQEAIA HEWISGNAAS DKNIKDGVCA
     QIEKNFAKAK WKKAVRVTTL MKRLRASEQG DTGASGLAAG ATGGPPDPNM PGGSLLAASI
     KTALSEKAAD AQTSTIPSLP QPPAARPEEQ QQAQQQQQAQ QQQQARCNGD VPQMLPQRKG
     Y
 
 
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