PRVA_RABIT
ID PRVA_RABIT Reviewed; 110 AA.
AC P02624;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Parvalbumin alpha;
GN Name=PVALB;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE OF 2-110, AND ACETYLATION AT ALA-2.
RX PubMed=1055405; DOI=10.1073/pnas.72.4.1309;
RA Enfield D.L., Ericsson L.H., Blum H.E., Fischer E.H., Neurath H.;
RT "Amino-acid sequence of parvalbumin from rabbit skeletal muscle.";
RL Proc. Natl. Acad. Sci. U.S.A. 72:1309-1313(1975).
RN [2]
RP PROTEIN SEQUENCE OF 2-110, AND ACETYLATION AT ALA-2.
RX PubMed=1009923; DOI=10.1111/j.1432-1033.1976.tb10963.x;
RA Capony J.-P., Pina C., Pechere J.-F.;
RT "Parvalbumin from rabbit muscle. Isolation and primary structure.";
RL Eur. J. Biochem. 70:123-135(1976).
RN [3]
RP CALCIUM-BINDING.
RX PubMed=113029; DOI=10.1021/bi00580a010;
RA Haiech J., Derancourt J., Pechere J.-F., Demaille J.G.;
RT "Magnesium and calcium binding to parvalbumins: evidence for differences
RT between parvalbumins and an explanation of their relaxing function.";
RL Biochemistry 18:2752-2758(1979).
CC -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC relaxation after contraction. It binds two calcium ions.
CC -!- MISCELLANEOUS: This parvalbumin has an isoelectric point of 5.50.
CC -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR PIR; A93795; PVRB.
DR RefSeq; XP_002711455.1; XM_002711409.3.
DR RefSeq; XP_008255298.1; XM_008257076.1.
DR AlphaFoldDB; P02624; -.
DR SMR; P02624; -.
DR STRING; 9986.ENSOCUP00000016160; -.
DR iPTMnet; P02624; -.
DR Ensembl; ENSOCUT00000026448; ENSOCUP00000016160; ENSOCUG00000027416.
DR GeneID; 100343964; -.
DR KEGG; ocu:100343964; -.
DR CTD; 5816; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000159653; -.
DR HOGENOM; CLU_157356_0_0_1; -.
DR InParanoid; P02624; -.
DR OMA; ETKRMMA; -.
DR OrthoDB; 1435392at2759; -.
DR Proteomes; UP000001811; Chromosome 4.
DR Bgee; ENSOCUG00000027416; Expressed in skeletal muscle tissue and 14 other tissues.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR008080; Parvalbumin.
DR PANTHER; PTHR11653; PTHR11653; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Direct protein sequencing; Metal-binding;
KW Muscle protein; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1009923,
FT ECO:0000269|PubMed:1055405"
FT CHAIN 2..110
FT /note="Parvalbumin alpha"
FT /id="PRO_0000073591"
FT DOMAIN 39..74
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 78..110
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 52
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 97
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:1009923,
FT ECO:0000269|PubMed:1055405"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02625"
SQ SEQUENCE 110 AA; 12065 MW; 8A1CFF36CDB3300E CRC64;
MAMTELLNAE DIKKAIGAFA AAESFDHKKF FQMVGLKKKS TEDVKKVFHI LDKDKSGFIE
EEELGFILKG FSPDARDLSV KETKTLMAAG DKDGDGKIGA DEFSTLVSES
