HPCL1_RAT
ID HPCL1_RAT Reviewed; 193 AA.
AC P62749; P35333;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Hippocalcin-like protein 1;
DE AltName: Full=Neural visinin-like protein 3;
DE Short=NVL-3;
DE Short=NVP-3;
DE AltName: Full=Visinin-like protein 3;
DE Short=VILIP-3;
GN Name=Hpcal1;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8360675; DOI=10.1111/j.1471-4159.1993.tb03624.x;
RA Kajimoto Y., Shirai Y., Mukai H., Kuno T., Tanaka C.;
RT "Molecular cloning of two additional members of the neural visinin-like
RT Ca(2+)-binding protein gene family.";
RL J. Neurochem. 61:1091-1096(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 8-17; 51-94; 119-130; 138-148; 164-171 AND 175-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
CC -!- FUNCTION: May be involved in the calcium-dependent regulation of
CC rhodopsin phosphorylation.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P37235}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P37235}.
CC -!- TISSUE SPECIFICITY: In neuronal cells, but not as specifically as
CC VILIP-1 or VILIP-2. {ECO:0000269|PubMed:8360675}.
CC -!- MISCELLANEOUS: Probably binds two or three calcium ions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; D13126; BAA02428.1; -; mRNA.
DR EMBL; BC088759; AAH88759.1; -; mRNA.
DR PIR; JH0816; JH0816.
DR RefSeq; NP_059052.1; NM_017356.2.
DR RefSeq; XP_006239976.1; XM_006239914.3.
DR RefSeq; XP_008762828.1; XM_008764606.2.
DR RefSeq; XP_017449815.1; XM_017594326.1.
DR RefSeq; XP_017449816.1; XM_017594327.1.
DR AlphaFoldDB; P62749; -.
DR SMR; P62749; -.
DR BioGRID; 248435; 1.
DR STRING; 10116.ENSRNOP00000007374; -.
DR iPTMnet; P62749; -.
DR PhosphoSitePlus; P62749; -.
DR jPOST; P62749; -.
DR PaxDb; P62749; -.
DR PRIDE; P62749; -.
DR Ensembl; ENSRNOT00000007374; ENSRNOP00000007374; ENSRNOG00000005492.
DR GeneID; 50871; -.
DR KEGG; rno:50871; -.
DR CTD; 3241; -.
DR RGD; 708375; Hpcal1.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000154645; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; P62749; -.
DR OMA; LEIVQXK; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; P62749; -.
DR TreeFam; TF300009; -.
DR PRO; PR:P62749; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000005492; Expressed in cerebellum and 20 other tissues.
DR Genevisible; P62749; RN.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P37235"
FT CHAIN 2..193
FT /note="Hippocalcin-like protein 1"
FT /id="PRO_0000073774"
FT DOMAIN 41..58
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 60..95
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 96..131
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 144..179
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P37235"
SQ SEQUENCE 193 AA; 22338 MW; B7251445F834F91D CRC64;
MGKQNSKLRP EVLQDLREHT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD
ASKFAEHVFR TFDTNSDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE
MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI KGAKSDPSIV
RLLQCDPSSA SQF
