ID   S100_LEPPA              Reviewed;          75 AA.
AC   P82978;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Calhepatin;
OS   Lepidosiren paradoxus (South American lungfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Dipnomorpha; Ceratodontiformes; Lepidosirenoidei; Lepidosirenidae;
OC   Lepidosiren.
OX   NCBI_TaxID=7883;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, ACETYLATION AT SER-1, AND
RP   3D-STRUCTURE MODELING.
RC   TISSUE=Liver;
RX   PubMed=12135482; DOI=10.1046/j.1432-1033.2002.03023.x;
RA   Di Pietro S.M., Santome J.A.;
RT   "Structural and biochemical characterization of calhepatin, an S100-like
RT   calcium-binding protein from the liver of lungfish (Lepidosiren
RT   paradoxa).";
RL   Eur. J. Biochem. 269:3433-3441(2002).
CC   -!- FUNCTION: Binds both calcium and copper, but not zinc. May be involved
CC       in calcium signal transduction. {ECO:0000269|PubMed:12135482}.
CC   -!- SUBUNIT: Monomer and homodimer.
CC   -!- TISSUE SPECIFICITY: Liver, and to a much lower level intestine.
CC   -!- MASS SPECTROMETRY: Mass=8672; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12135482};
CC   -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P82978; -.
DR   SMR; P82978; -.
DR   iPTMnet; P82978; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
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; Copper; Direct protein sequencing; Metal-binding;
KW   Repeat.
FT   CHAIN           1..75
FT                   /note="Calhepatin"
FT                   /id="PRO_0000144035"
FT   DOMAIN          2..37
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          38..73
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         15
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         17
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         19
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         21
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         26
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         51
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         53
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         55
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         57
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:12135482"
SQ   SEQUENCE   75 AA;  8628 MW;  A349C704FDD6D753 CRC64;
     SADEQKLRER FEALDKDKSG TLSVDELYEG VHAVHPKVSR NDIVKIIEKV DTNKDGQVSW
     QEFIEAFKRL ADLKL