MANA_PINFU
ID MANA_PINFU Reviewed; 447 AA.
AC Q27908;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Nacrein;
DE EC=4.2.1.1;
DE Flags: Precursor;
OS Pinctada fucata (Akoya pearl oyster) (Pinctada imbricata fucata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX NCBI_TaxID=50426;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-32, FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RC TISSUE=Mantle, and Nacre;
RX PubMed=8790386; DOI=10.1073/pnas.93.18.9657;
RA Miyamoto H., Miyashita T., Okushima M., Nakano S., Morita T.,
RA Matsushiro A.;
RT "A carbonic anhydrase from the nacreous layer in oyster pearls.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9657-9660(1996).
RN [2]
RP GLYCOSYLATION.
RX PubMed=18253795; DOI=10.1007/s10126-007-9063-8;
RA Takakura D., Norizuki M., Ishikawa F., Samata T.;
RT "Isolation and characterization of the N-linked oligosaccharides in nacrein
RT from Pinctada fucata.";
RL Mar. Biotechnol. 10:290-296(2008).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Mantle, and Shell;
RX PubMed=15795493; DOI=10.2108/zsj.22.311;
RA Miyamoto H., Miyoshi F., Kohno J.;
RT "The carbonic anhydrase domain protein nacrein is expressed in the
RT epithelial cells of the mantle and acts as a negative regulator in
RT calcification in the mollusc Pinctada fucata.";
RL Zool. Sci. 22:311-315(2005).
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. {ECO:0000269|PubMed:15795493,
CC ECO:0000269|PubMed:8790386}.
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; Evidence={ECO:0000269|PubMed:8790386};
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.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:8790386}.
CC -!- TISSUE SPECIFICITY: Expressed at whole regions of the mantle epithelium
CC tissue. Is found in the aragonitic nacreous and calcitic prismatic and
CC foliated layers. {ECO:0000269|PubMed:15795493,
CC ECO:0000269|PubMed:8790386}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18253795}.
CC -!- MISCELLANEOUS: Two hypotheses for calcium binding are proposed. Either
CC the Gly-Xaa-Asn repeat domain bind calcium or sulfite and sialic acid
CC provide the necessary negative charge in the N-glycan to promote
CC calcium uptake.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; D83523; BAA11940.1; -; mRNA.
DR AlphaFoldDB; Q27908; -.
DR SMR; Q27908; -.
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 CDD; cd03124; alpha_CA_prokaryotic_like; 1.
DR Gene3D; 3.10.200.10; -; 2.
DR InterPro; IPR041891; Alpha_CA_prokaryot-like.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR InterPro; IPR008160; Collagen.
DR PANTHER; PTHR18952; PTHR18952; 2.
DR Pfam; PF00194; Carb_anhydrase; 2.
DR Pfam; PF01391; Collagen; 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..17
FT /evidence="ECO:0000269|PubMed:8790386"
FT CHAIN 18..447
FT /note="Nacrein"
FT /id="PRO_0000379792"
FT DOMAIN 50..446
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REPEAT 242..244
FT /note="1"
FT REPEAT 245..247
FT /note="2"
FT REPEAT 248..250
FT /note="3"
FT REPEAT 251..253
FT /note="4"
FT REPEAT 254..256
FT /note="5"
FT REPEAT 257..259
FT /note="6"
FT REPEAT 260..262
FT /note="7"
FT REPEAT 263..265
FT /note="8"
FT REPEAT 266..268
FT /note="9"
FT REPEAT 269..271
FT /note="10"
FT REPEAT 272..274
FT /note="11"
FT REPEAT 275..277
FT /note="12"
FT REPEAT 278..280
FT /note="13"
FT REPEAT 281..283
FT /note="14"
FT REPEAT 284..286
FT /note="15"
FT REPEAT 287..289
FT /note="16"
FT REPEAT 290..292
FT /note="17"
FT REPEAT 293..295
FT /note="18"
FT REPEAT 296..298
FT /note="19"
FT REPEAT 299..301
FT /note="20"
FT REPEAT 302..304
FT /note="21"
FT REPEAT 305..307
FT /note="22"
FT REPEAT 308..310
FT /note="23"
FT REPEAT 311..313
FT /note="24"
FT REPEAT 314..316
FT /note="25"
FT REPEAT 317..318
FT /note="26"
FT REPEAT 320..322
FT /note="27"
FT REGION 218..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..322
FT /note="27 X 3 AA approximate tandem repeats of G-X-N"
FT COMPBIAS 221..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 387..388
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 447 AA; 50114 MW; 334191045E91AB8C CRC64;
MYLHLTALCV VIPLCYGASM FKHDHYMDNG VRYPNGDGIC KQLNETKCDA GFSYDRSICE
GPHYWHTISK CFIACGIGQR QSPINIVSYD AKFRQRLPKL KFKPHMEKLK TEVTNHQNRA
PEFEPEDGEN LYVKLNNLVD GHYKFHNLHV HNGRTRRKGS EHSVNGRFTP MEAHLVFHHD
DQTHFEPTRT KLGGAFPGHN DFVVVGVFLE VGDDGFGDEP DDEECKHILK GHHPDNNENG
NGDNGNNGYN GDNGNNGDNG NNSYNGDNGN NGVNGNNGYN GDNGNNGDNG NNGYNGDNGN
NGDNGNNGEN GNNGENGNNG ENGHKHGCRV KKAKHLSRIL ECAYRNDKVR EFKKVGEEEG
LDVHLTPEMA LPPLKYRHYY TYEGSLTTPP CTESVLWVVQ KCHVQVSRRV LHALRNVEGY
KDGTTLRKYG TRRPTQKNKV TVYKSFK
