GenomeNet

Database: UniProt
Entry: Q90YK8
LinkDB: Q90YK8
Original site: Q90YK8 
ID   PRVB1_GADCH             Reviewed;         109 AA.
AC   Q90YK8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   22-FEB-2023, entry version 75.
DE   RecName: Full=Parvalbumin beta-1;
DE   AltName: Allergen=The c 1;
OS   Gadus chalcogrammus (Alaska pollock) (Theragra chalcogramma).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=1042646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALLERGEN.
RX   PubMed=15589323; DOI=10.1016/j.molimm.2004.09.001;
RA   Van Do T., Hordvik I., Endresen C., Elsayed S.;
RT   "Characterization of parvalbumin, the major allergen in Alaska pollack, and
RT   comparison with codfish Allergen M.";
RL   Mol. Immunol. 42:345-353(2005).
CC   -!- FUNCTION: In muscle, parvalbumin is thought to be involved in
CC       relaxation after contraction. It binds two calcium ions (By
CC       similarity). {ECO:0000250}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC       {ECO:0000269|PubMed:15589323}.
CC   -!- SIMILARITY: Belongs to the parvalbumin family. {ECO:0000305}.
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DR   EMBL; AY035586; AAK63088.1; -; mRNA.
DR   AlphaFoldDB; Q90YK8; -.
DR   SMR; Q90YK8; -.
DR   Allergome; 1084; The ch 1.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
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:SF18; PARVALBUMIN 4-RELATED; 1.
DR   PANTHER; PTHR11653; PARVALBUMIN ALPHA; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   PRINTS; PR01697; PARVALBUMIN.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Allergen; Calcium; Metal-binding; Muscle protein; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..109
FT                   /note="Parvalbumin beta-1"
FT                   /id="PRO_0000360373"
FT   DOMAIN          39..74
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          78..109
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:0000250|UniProtKB:P02621,
FT                   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:0000250|UniProtKB:P02621,
FT                   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:0000250|UniProtKB:P02621,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         58
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02621"
FT   BINDING         60
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02621"
FT   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P02621,
FT                   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:0000250|UniProtKB:P02621,
FT                   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:0000250|UniProtKB:P02621,
FT                   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:0000250|UniProtKB:P02621,
FT                   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:0000250|UniProtKB:P02621,
FT                   ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   109 AA;  11496 MW;  6C588EB1714F7FE5 CRC64;
     MSFAGVLADA DVKAALAGCA AADSFNYKTF FKACGLAAKS HEEVKKAFFV IDQDQSGFIE
     EDELKLFLQT FGAGARELTA AETKAFLAAG DEDGDGMIGV DEFVTLVKA
//
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