HPCL4_RAT
ID HPCL4_RAT Reviewed; 191 AA.
AC P35332;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Hippocalcin-like protein 4;
DE AltName: Full=Neural visinin-like protein 2;
DE Short=NVL-2;
DE Short=NVP-2;
DE AltName: Full=Visinin-like protein 2;
DE Short=VILIP-2;
GN Name=Hpcal4;
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].
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).
CC -!- FUNCTION: May be involved in the calcium-dependent regulation of
CC rhodopsin phosphorylation.
CC -!- TISSUE SPECIFICITY: Neuron-specific in the central and peripheral
CC nervous system.
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; D13125; BAA02427.1; -; mRNA.
DR PIR; JH0815; JH0815.
DR RefSeq; NP_059053.1; NM_017357.1.
DR RefSeq; XP_006238891.1; XM_006238829.3.
DR AlphaFoldDB; P35332; -.
DR SMR; P35332; -.
DR STRING; 10116.ENSRNOP00000066655; -.
DR iPTMnet; P35332; -.
DR PhosphoSitePlus; P35332; -.
DR SwissPalm; P35332; -.
DR PaxDb; P35332; -.
DR PRIDE; P35332; -.
DR Ensembl; ENSRNOT00000074347; ENSRNOP00000066655; ENSRNOG00000050983.
DR GeneID; 50872; -.
DR KEGG; rno:50872; -.
DR UCSC; RGD:708491; rat.
DR CTD; 51440; -.
DR RGD; 708491; Hpcal4.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000161166; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; P35332; -.
DR OMA; RGHEDPI; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; P35332; -.
DR TreeFam; TF300009; -.
DR PRO; PR:P35332; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000050983; Expressed in frontal cortex and 8 other tissues.
DR Genevisible; P35332; RN.
DR GO; GO:0005246; F:calcium channel regulator activity; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0007165; P:signal transduction; 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 InterPro; IPR029534; VILIP-2.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR PANTHER; PTHR23055:SF84; PTHR23055:SF84; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 2: Evidence at transcript level;
KW Calcium; Lipoprotein; Metal-binding; Myristate; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..191
FT /note="Hippocalcin-like protein 4"
FT /id="PRO_0000073780"
FT DOMAIN 24..59
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
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 146..181
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 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 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 170
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"
SQ SEQUENCE 191 AA; 22245 MW; 23E500B4D871103A CRC64;
MGKNNSKLAP EELEDLVQNT EFSEQELKQW YKGFLKDCPS GILNLEEFQQ LYIKFFPYGD
ASKFAQHAFR TFDKNGDGTI DFREFICALS VTSRGSFEQK LNWAFEMYDL DGDGRITRLE
MLEIIEAIYK MVGTVIMMRM NQDGLTPQQR VDKIFKKMDQ DKDDQITLEE FKEAAKSDPS
IVLLLQCDMQ K
