MAC1_CRANI
ID MAC1_CRANI Reviewed; 340 AA.
AC A0ZSF6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Nacrein-like protein C1;
DE EC=4.2.1.1;
DE Flags: Fragment;
OS Crassostrea nippona (Iwagaki oyster).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=121615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CRYSTALLIZATION.
RC TISSUE=Gill, and Mantle;
RX PubMed=18080162; DOI=10.1007/s10126-007-9061-x;
RA Norizuki M., Samata T.;
RT "Distribution and function of the nacrein-related proteins inferred from
RT structural analysis.";
RL Mar. Biotechnol. 10:234-241(2008).
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). Shows inhibitory activity of crystal
CC formation when present in free state but, when attached to the
CC insoluble matrix, may regulate the form and size of aragonite crystal.
CC {ECO:0000250, ECO:0000269|PubMed:18080162}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the mantle.
CC -!- DOMAIN: The Gly-Xaa-Asn repeat domain binds calcium. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC {ECO:0000305}.
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DR EMBL; AB252483; BAF42333.1; -; mRNA.
DR AlphaFoldDB; A0ZSF6; -.
DR SMR; A0ZSF6; -.
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 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; Disulfide bond; Extracellular matrix; Lyase; Metal-binding;
KW Repeat; Secreted; Zinc.
FT CHAIN <1..>340
FT /note="Nacrein-like protein C1"
FT /id="PRO_0000379797"
FT DOMAIN 1..340
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REPEAT 162..164
FT /note="1"
FT REPEAT 165..167
FT /note="2"
FT REPEAT 168..170
FT /note="3"
FT REPEAT 171..173
FT /note="4"
FT REPEAT 174..176
FT /note="5"
FT REPEAT 177..179
FT /note="6"
FT REPEAT 180..182
FT /note="7"
FT REPEAT 183..185
FT /note="8"
FT REPEAT 186..188
FT /note="9"
FT REPEAT 189..191
FT /note="10"
FT REPEAT 192..194
FT /note="11"
FT REPEAT 195..197
FT /note="12"
FT REPEAT 198..200
FT /note="13"
FT REPEAT 201..203
FT /note="14"
FT REPEAT 204..206
FT /note="15"
FT REPEAT 207..209
FT /note="16"
FT REPEAT 210..212
FT /note="17"
FT REPEAT 213..215
FT /note="18"
FT REPEAT 216..218
FT /note="19"
FT REPEAT 219..221
FT /note="20"
FT REPEAT 222..224
FT /note="21"
FT REPEAT 225..227
FT /note="22"
FT REPEAT 228..230
FT /note="23"
FT REPEAT 231..233
FT /note="24"
FT REPEAT 234..236
FT /note="25"
FT REPEAT 237..238
FT /note="26"
FT REPEAT 240..242
FT /note="27"
FT REGION 138..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..242
FT /note="27 X 3 AA approximate tandem repeats of G-X-N"
FT COMPBIAS 141..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 307..308
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 340
SQ SEQUENCE 340 AA; 37859 MW; 677200F61245D648 CRC64;
QSPINIVSYD AKFLRRLPKL KFKPHMEKLK TEVTNHQNRA PEFEPEDGEN LYVKLNNLVD
GHYKFHNLHV HNGRTRRKGS EHSVNGHFTP MEAHLVFHHD EQTHFEPTRT KLGGAFPGHN
DFVVVGVFLE VGDDGFGDEP DDEECKHILK GHHPDNNENG NGDNGNNGYN GDNGNNGDNG
NNGYNGDNGN NGVNGNNGYN GDNGNNGDNG NNGYNGDNGN NGDNGNNGEN GNNGENGNNG
ENGHKHGCRV KKAKHLSRIL ECAYRNDKVR EFKKVGEEEG LDVHLTPEMP LPPLKYRHYY
TYEGSLTTPP CTESVLWVVQ KCHVQVSRRV LHALRNVEGY
