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 27-MAR-2024, entry version 81.
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; Alpha carbonic anhydrase; 2.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR PANTHER; PTHR18952:SF268; AGAP002359-PA; 1.
DR PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR Pfam; PF00194; Carb_anhydrase; 2.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 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
//
