CAMKV_RAT
ID CAMKV_RAT Reviewed; 504 AA.
AC Q63092;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=CaM kinase-like vesicle-associated protein;
DE AltName: Full=1G5;
GN Name=Camkv; Synonyms=1G5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP COFACTOR, INTERACTION WITH CALMODULIN, AND SUBCELLULAR LOCATION.
RC TISSUE=Hypothalamus;
RX PubMed=8283228; DOI=10.1523/jneurosci.14-01-00001.1994;
RA Godbout M., Erlander M.G., Hasel K.W., Danielson P.E., Wong K.K.,
RA Battenberg E.L., Foye P.E., Bloom F.E., Sutcliffe J.G.;
RT "1G5: a calmodulin-binding, vesicle-associated, protein kinase-like protein
RT enriched in forebrain neurites.";
RL J. Neurosci. 14:1-13(1994).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-438, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Has no detectable kinase activity in vitro.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:8283228};
CC -!- SUBUNIT: Interacts with calmodulin, in the presence of calcium.
CC {ECO:0000269|PubMed:8283228}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8283228};
CC Peripheral membrane protein {ECO:0000269|PubMed:8283228}. Cytoplasmic
CC vesicle membrane {ECO:0000269|PubMed:8283228}; Peripheral membrane
CC protein {ECO:0000269|PubMed:8283228}. Note=Predominantly observed in
CC association with the plasma membrane of soma and in neurites, both
CC axons and dendrites. May be associated with vesicular structures.
CC -!- TISSUE SPECIFICITY: Expressed in brain and weakly in eye. Not detected
CC in liver, kidney, spleen, thymus, bladder, aorta, lung, intestine,
CC esophagus, stomach, skeletal muscle, heart, diaphragm, uterus, tail
CC skin, submaxillary gland, prostate, ear, epididymis, placenta,
CC pancreas, ovary, testis, adrenal gland, parathyroid gland, thyroid
CC gland, pineal gland, pituitary and sciatic nerve. In adult hippocampus,
CC predominantly expressed in caudate nucleus, cortex, hypothalamus,
CC olfactory bulb, and midbrain and faintly in pons, brainstem and spinal
CC cord. {ECO:0000269|PubMed:8283228}.
CC -!- DEVELOPMENTAL STAGE: Expressed from day 16 dpc, but accumulation was
CC primarily postnatal with maximal steady state levels reached at
CC postnatal day 10. {ECO:0000269|PubMed:8283228}.
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; L22557; AAA16633.1; -; mRNA.
DR PIR; I56542; I56542.
DR RefSeq; NP_076490.1; NM_024000.1.
DR AlphaFoldDB; Q63092; -.
DR SMR; Q63092; -.
DR BioGRID; 249391; 5.
DR IntAct; Q63092; 1.
DR MINT; Q63092; -.
DR STRING; 10116.ENSRNOP00000025311; -.
DR iPTMnet; Q63092; -.
DR PhosphoSitePlus; Q63092; -.
DR SwissPalm; Q63092; -.
DR PaxDb; Q63092; -.
DR PRIDE; Q63092; -.
DR GeneID; 79011; -.
DR KEGG; rno:79011; -.
DR CTD; 79012; -.
DR RGD; 621488; Camkv.
DR eggNOG; KOG0032; Eukaryota.
DR InParanoid; Q63092; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; Q63092; -.
DR PRO; PR:Q63092; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IDA:RGD.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0099159; P:regulation of modification of postsynaptic structure; ISO:RGD.
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 1: Evidence at protein level;
KW Calmodulin-binding; Cell membrane; Cytoplasmic vesicle; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..504
FT /note="CaM kinase-like vesicle-associated protein"
FT /id="PRO_0000250096"
FT DOMAIN 24..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 378..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHL1"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 462
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHL1"
SQ SEQUENCE 504 AA; 54106 MW; DF31E414B213B54E CRC64;
MPFGCVTLGD KKNYNQPSEV TDRYDLGQVV KTEEFCEIFR AKDKTTGKLH TCKKFQKRDG
RKVRKAAKNE IGILKMVKHP NILQLVDVFV TRKEYFIFLE LATGREVFDW ILDQGYYSER
DTSNVVRQVL EAVAYLHSLK IVHRNLKLEN LVYYNRLKNS KIVISDFHLA KLENGLIKEP
CGTPEYLAPE VVGRQRYGRP VDCWAIGVIM YILLSGNPPF YEEVEEDDYE NHDKNLFRKI
LAGDYEFDSP YWDDISQAAK DLVTRLMEVE QDQRITAEEA ISHEWISGNA ASDKNIKDGV
CAQIEKNFAR AKWKKAVRVT TLMKRLRAPE QSGTAATSDA ATPGAAGGAV AAAAGGAAPA
SGASATVGTG GDAGCAAKSD DMASADRSAT PATDGSATPA TDGSVTPATD GSITPATDGS
VTPATDRSAT PATDGRATPA TEESTVPAAQ SSAAPAAKAA ATPEPAVAQP DSTALEGATG
QAPPSSKGEE ATGCAQESQR VETS
