ID   MANL_MYTCA              Reviewed;         321 AA.
AC   P86856;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Nacrein-like protein {ECO:0000303|PubMed:21643827};
DE   Flags: Fragment;
OS   Mytilus californianus (California mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC   Mytilus.
OX   NCBI_TaxID=6549;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gracey A., Grimwood J., Schmutz J., Myers R.M.;
RT   "Expressed sequence tags from Mytilus californianus.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 68-82; 98-110; 213-221 AND 286-300, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Shell {ECO:0000269|PubMed:21643827};
RX   PubMed=21643827; DOI=10.1007/s00239-011-9451-6;
RA   Marie B., Le Roy N., Zanella-Cleon I., Becchi M., Marin F.;
RT   "Molecular evolution of mollusc shell proteins: insights from proteomic
RT   analysis of the edible mussel mytilus.";
RL   J. Mol. Evol. 72:531-546(2011).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21643827}.
CC   -!- TISSUE SPECIFICITY: Component of the organic matrix of calcified shell
CC       layers like nacre and prisms. {ECO:0000269|PubMed:21643827}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000255}.
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DR   EMBL; GE749008; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; GE751262; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P86856; -.
DR   SMR; P86856; -.
DR   PRIDE; P86856; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.10.200.10; -; 1.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR018347; CAH2.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   PANTHER; PTHR18952; PTHR18952; 2.
DR   PANTHER; PTHR18952:SF138; PTHR18952:SF138; 2.
DR   Pfam; PF00194; Carb_anhydrase; 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   Direct protein sequencing; Secreted.
FT   CHAIN           <1..321
FT                   /note="Nacrein-like protein"
FT                   /id="PRO_0000404087"
FT   DOMAIN          1..319
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        58
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:21643827"
SQ   SEQUENCE   321 AA;  37951 MW;  2E93B945FB37E765 CRC64;
     RGPKNWCKVH PCWTTCGSQM RQSPININTN QTIYKRYPRL KVENVHKRVI ATIRNNGHAP
     YFEVHEKFDD EIVLRNVPER PRRKEYNFAQ LHVQLGRDEK EGSEHSIDNK FKPMEAQMVF
     YDKDYEDVLE AKSKKNGLVV ISVMIEVYGR SKEHDDCACD GETCTVRYVR KLSKLMEKYY
     EKVRRYPLVS INPHFLTFIK LPRKCWYNKC GRTPSPDFIE KKCEKEEPET RPFFVFEGIT
     PLDVIPYDTN RFYTYAGSLT SPPCYETVQW VVFKCPIKVS SKAFRMLQLV QDSHLDPLEK
     LGVRRPLQTN KNVIVYRNHL K