ID   MA66_PINMA              Reviewed;         568 AA.
AC   Q9NL38;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=N66 matrix protein;
DE            EC=4.2.1.1;
DE   Flags: Precursor;
OS   Pinctada maxima (Silver-lipped pearl oyster) (White-lipped pearl oyster).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=104660;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 23-39, SUBUNIT, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Mantle, and Nacre;
RX   PubMed=10694502; DOI=10.1006/bbrc.2000.2274;
RA   Kono M., Hayashi N., Samata T.;
RT   "Molecular mechanism of the nacreous layer formation in Pinctada maxima.";
RL   Biochem. Biophys. Res. Commun. 269:213-218(2000).
CC   -!- FUNCTION: Acts as a negative regulator for calcification in the shells
CC       of mollusks. May function both as a calcium concentrator and as a
CC       carbonic anhydrase required for production of carbonate ions, which are
CC       assembled to CaCO(3) at mineralization sites. Is important for shell
CC       formation in both the calcitic prismatic layer and the aragonitic
CC       nacreous layer (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544; EC=4.2.1.1;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homooligomer; disulfide-linked. May also be disulfide-linked
CC       to insoluble organic matrix. {ECO:0000269|PubMed:10694502}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000269|PubMed:10694502}.
CC   -!- TISSUE SPECIFICITY: Expressed in both the dorsal region of the mantle
CC       and the mantle edge. Is dispersed in calcium carbonate and also linked
CC       by disulfide bonds to the organic core of nacre.
CC       {ECO:0000269|PubMed:10694502}.
CC   -!- MISCELLANEOUS: Sulfite and sialic acid may provide the necessary
CC       negative charge in the N-glycan to promote calcium uptake.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; AB032613; BAA90540.1; -; mRNA.
DR   PIR; JC7210; JC7210.
DR   AlphaFoldDB; Q9NL38; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.10.200.10; -; 2.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   PANTHER; PTHR18952; PTHR18952; 2.
DR   Pfam; PF00194; Carb_anhydrase; 2.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; SSF51069; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Lyase; Metal-binding; Repeat; Secreted; Signal; Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:10694502"
FT   CHAIN           23..568
FT                   /note="N66 matrix protein"
FT                   /id="PRO_0000379791"
FT   DOMAIN          55..567
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   REGION          259..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         154
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   BINDING         506..507
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        389
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        34..37
FT                   /note="MDQT -> GRQW (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   568 AA;  62376 MW;  4AD9242A96EB642F CRC64;
     MWRMTTLLHL TALLVLIPLC HCASMHRHDH YMDMDQTYPN GLGYCEPSGE SSCKAGFSYN
     RDICQGPYHW HTISSCYKAC GHKRRQSPIN IWSHKAVFLP YLPRLKFKPH MKSLDTDVTN
     HQNRAPEFEP EDGDKLHVKL KNLVDGHYKF HNLHIHNGKS RRKGSEHSVN RHFTPMEAHL
     VFHHDDKKEI KPPRVKLGGV YAGRNKFVVV GVFLEVGDEG YGDEPDDDEC KRILKGHCEN
     NGDNGNNCDN GNNGNNDNNG NNGNNGNGNN GYNGNNGDNG NNGNGNGNNG YNGNNGYNGN
     NGNNGNGNND NNGNDNNGNN GGNGNNGNNG NGNNGNNGNG NNGNNGGNGN NGNNGNSNNG
     NNGNGNNGNN GGNGNNGNNG NGNNENNGNG SNGNNGGNGN NGNNGDNGNG DNGYNGDNGN
     SDGRLRRWDL ANVRRMHAER YHFSGGCIVK KAKRLSRILE CAYRHKKVRE FKRNGEEKGL
     DVDITPEMVL PPMKYRHYYT YEGSLTTPPC NETVLWVVEK CHVQVSRRVL DALRNVEGYE
     DGTTLSKYGT RRPTQRNKHP LRVYKNSI