ID   FND2_PINMG              Reviewed;         624 AA.
AC   H2A0L8;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Fibronectin type III domain-containing protein 2;
DE   Flags: Precursor;
OS   Margaritifera margaritifera (Freshwater pearl mussel).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pterioida; Pterioidea; Pteriidae; Pinctada.
OX   NCBI_TaxID=102329;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RC   TISSUE=Mantle;
RX   PubMed=21040589; DOI=10.1186/1471-2164-11-613;
RA   Joubert C., Piquemal D., Marie B., Manchon L., Pierrat F.,
RA   Zanella-Cleon I., Cochennec-Laureau N., Gueguen Y., Montagnani C.;
RT   "Transcriptome and proteome analysis of Pinctada margaritifera calcifying
RT   mantle and shell: focus on biomineralization.";
RL   BMC Genomics 11:613-613(2010).
RN   [2]
RP   PROTEIN SEQUENCE OF 56-65; 164-170; 291-303; 509-519; 523-532 AND 568-576,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Shell;
RX   PubMed=23213212; DOI=10.1073/pnas.1210552109;
RA   Marie B., Joubert C., Tayale A., Zanella-Cleon I., Belliard C.,
RA   Piquemal D., Cochennec-Laureau N., Marin F., Gueguen Y., Montagnani C.;
RT   "Different secretory repertoires control the biomineralization processes of
RT   prism and nacre deposition of the pearl oyster shell.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:20986-20991(2012).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23213212}.
CC   -!- TISSUE SPECIFICITY: Prismatic layer of shell (at protein level).
CC       {ECO:0000269|PubMed:23213212}.
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DR   EMBL; HE610385; CCE46159.1; -; mRNA.
DR   AlphaFoldDB; H2A0L8; -.
DR   SMR; H2A0L8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   CDD; cd00063; FN3; 5.
DR   Gene3D; 2.60.40.10; -; 4.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF00041; fn3; 2.
DR   SMART; SM00060; FN3; 4.
DR   SUPFAM; SSF49265; SSF49265; 3.
DR   PROSITE; PS50853; FN3; 5.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..624
FT                   /note="Fibronectin type III domain-containing protein 2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000417949"
FT   DOMAIN          131..236
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          240..330
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          334..430
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          431..524
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          527..624
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
SQ   SEQUENCE   624 AA;  69566 MW;  F55D48897C3A607B CRC64;
     MREQFSVLVI SLLFSSSYGQ VGQMGPPPGQ SGQPWTLAEF DAIDTHLKNI QMYARSLQDI
     VYQERMKQYP FMPNSTAGQP NMGYSTFAND VINRLTKIEF ETGELVTQYP LCPSGGTGGN
     PYPVIPPNAP PPQNVMIQSE TIGNSSSVIV SWDRPNVVGT DVRLDDLQYK VYFAPLDEYG
     QQTAEAIVFS ICSVNQTVAS ITDLYPRSFY KVSVGTVICS TSESSSGAKS LKTPDIIPSE
     PTNLRVDGTK PNAIALRWDL PLLMGTLANY TIYVTSENGT GFEVAVDPTQ VNAILYDLIE
     GTRYVISVSA FSDNGESPKS SSIEVMTDVF VPDMPRFFQV IFVNTTSVHL VWEPPNPGAG
     MIRYYSINYT DSLYSQFFNF KTPNAKITTA IITGLQPATT YYFRAFAHTG RRAGAGSAVI
     MQDTDITVPT VPRELYAQKA KNDPPRARLQ WLPPAKTYGS LKNYSIHWGV KNGATRKEEI
     EPGLLEWYSD FLDDNTEHEF KLYAQNEKGY GPAATVTHRT PKRDTVVPPN VKVDRKKGKN
     NETVLVVSWN PITQPGKQVS GFRILYRKFE WVYTGRWSLK EIPDPNARSA TIGVENSNYS
     FIVVVRGYRN PRPNMQVNPP WPGR