MAF_PINFU
ID MAF_PINFU Reviewed; 415 AA.
AC A0ZSF2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Nacrein-like protein F;
DE EC=4.2.1.1;
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], 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 -!- 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; AB252479; BAF42329.1; -; mRNA.
DR AlphaFoldDB; A0ZSF2; -.
DR SMR; A0ZSF2; -.
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; Glycoprotein; Lyase;
KW Metal-binding; Repeat; Secreted; Zinc.
FT CHAIN 1..415
FT /note="Nacrein-like protein F"
FT /id="PRO_0000379795"
FT DOMAIN 33..414
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT REPEAT 225..227
FT /note="1"
FT REPEAT 228..230
FT /note="2"
FT REPEAT 231..233
FT /note="3"
FT REPEAT 234..236
FT /note="4"
FT REPEAT 237..239
FT /note="5"
FT REPEAT 240..242
FT /note="6"
FT REPEAT 243..245
FT /note="7"
FT REPEAT 246..248
FT /note="8"
FT REPEAT 249..251
FT /note="9"
FT REPEAT 252..254
FT /note="10"
FT REPEAT 255..257
FT /note="11"
FT REPEAT 258..260
FT /note="12"
FT REPEAT 261..263
FT /note="13"
FT REPEAT 264..266
FT /note="14"
FT REPEAT 267..269
FT /note="15"
FT REPEAT 270..272
FT /note="16"
FT REPEAT 273..275
FT /note="17"
FT REPEAT 276..278
FT /note="18"
FT REPEAT 279..281
FT /note="19"
FT REPEAT 282..284
FT /note="20"
FT REPEAT 285..286
FT /note="21"
FT REPEAT 288..290
FT /note="22"
FT REGION 201..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..290
FT /note="22 X 3 AA approximate tandem repeats of G-X-N"
FT COMPBIAS 204..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT BINDING 355..356
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 415 AA; 46753 MW; F1F96C9EA0E5846C CRC64;
ASMFKHDHYM DNGVRYPNGD GICKQLNETK CDAGFSYDRS ICEGPRYWQT ISKCFIACGI
GQRQSPINIV SYDAKFRQRL PKLKFKPHME KLKTEVTNHQ NRAPEFEPED GENLYVKLNN
LVDGHYKFHN LHVHNGRTRR KGSEHSVNGR FTPMEAHLVF HHDEQTHFEP TRTKLGGAFP
GHNDFVVVGV FLEVGDDGFG DEPDDEECKH ILKGHHPDNN ENGNGDNGNN GYNGDNGNNG
DNGNNGYNGD NGNNGVNGNN GYNGDNGNNG DNGNNGENGN NGENGNNGEN GHKHGCRVKK
AKHLSRILEC AYRNDKVREF KKVGEEEGLD VHLTPEMALP PLKYRHYYTY EGSLTTPPCT
ESVLWVVQKC HVQVSRRVLH ALRKVEGYKD GTTLRKYGTR RPTQKNKVTV YKSFK
