MAP1_MIZYE
ID MAP1_MIZYE Reviewed; 331 AA.
AC A0ZSF4;
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 P1;
DE EC=4.2.1.1;
DE Flags: Fragment;
OS Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC Mizuhopecten.
OX NCBI_TaxID=6573;
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; AB252481; BAF42331.1; -; mRNA.
DR AlphaFoldDB; A0ZSF4; -.
DR SMR; A0ZSF4; -.
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..>331
FT /note="Nacrein-like protein P1"
FT /id="PRO_0000379793"
FT DOMAIN 1..331
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..229
FT /note="23"
FT REPEAT 231..233
FT /note="24"
FT REGION 138..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..233
FT /note="24 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..231
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 298..299
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 331
SQ SEQUENCE 331 AA; 36918 MW; 48E96EDDB73DCDAB CRC64;
QSPINIVSYD AKFRQRLPKL KFKPHMEKLK TEVTNHQNRA PEFEPEDGEN LYVKLNNLVD
GHYKFHNLHV HNGRTRRKGS EHSVNGRFTP MEAHLVFHHD DQTHFEPTRT KLGGAFPGHN
DFVVVGVFLE VGDDGFGDEP DDEECKRILK GHHPDNNENG NGDNGNNGYN GDNGNNGDNG
NNGYNGDNGN NGDNGNNGYN GDNGNNGDNG NNGENGNNGE NGNNGENGNN GENGHKHGCR
VKKAKHLSTI LECAYRNDKV REFKKVGEEE GLDVHLTPEM PLPPLKNRHY YTYEGSLTTP
PCTESVLWVV QKCHVQVSRR VLHALRNVEG Y
