ID   FND1_PINMG              Reviewed;         754 AA.
AC   H2A0L7;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Fibronectin type III domain-containing protein 1;
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 237-243; 290-309; 352-364; 400-408; 427-448; 557-564;
RP   672-682 AND 684-691, 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       Expressed primarily in the mantle with highest level in the outer
CC       epithelium of the mantle edge and lower level in the mantle pallium.
CC       {ECO:0000269|PubMed:23213212}.
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DR   EMBL; HE610384; CCE46158.1; -; mRNA.
DR   AlphaFoldDB; H2A0L7; -.
DR   SMR; H2A0L7; -.
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; 2.
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..754
FT                   /note="Fibronectin type III domain-containing protein 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000417948"
FT   DOMAIN          250..355
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          359..449
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          453..545
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          549..642
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          645..742
FT                   /note="Fibronectin type-III 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          40..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   754 AA;  83108 MW;  C1B027583584B5F0 CRC64;
     MKSWISISFL CMLFPLSNGQ LGSSGQVTLQ GAQISQATQS LQGTAPTSQY PQGGTQISQG
     GAQATQNYQG VAQGTQISQG LTQGAQISQG GGQGISQGAT QGTQFSQGTV PSGQFFQNIV
     QGTQAVLSGA QHSQAGAQGS QFPQSAAHTA QHHQGTAQPA QSGTHAILKE MEKSLAEFKA
     YVEYLENMVY KERMKYPSPY IQNFTASPSN FTYTTFENDV DMRLSSMERI SSELVKQMVN
     CPRGPVPPPP PQSVMVQSDT VDNSSNIYVS WDPPYFEGKP LTGENMHYKV YFSPSDQYGK
     ATGGEFIFRI CDANFTQASV TDLNPRSFYS IQVAATLCEA IESEGTSTSV KTPDLIPSAP
     LNLKLEGTKP NAFAVSWDPP TVKGTLTNYT IYATEESGKA TMVTIDPKLT SYALYNLYEG
     TMYTIRIAAS SDNGMSPKSE PLEVTTDKFI PMAPRNVRAI DNNLTSVTLE WDAPLPGRGM
     IRGYRINYTL DFTDYEEMLI SDPSITTATI TNLTPATEYY FQVFARTMKR LGYGSHLIMN
     KTKMDVPSEP MSVVHRIMDN GLQRIQVSWQ PPENTYGPII DYIIHWGVRG GATRKEFLTP
     YVLSWTSDFL DDNANHDFKL FAQNVVGIGK PVAFSVKTLP KPQILVPNVR VKRETSKNNI
     TSLTVTWGSP KVPVDGFFVL YRKYEGVYSD RWKFIEIPKP NARGTTITVT QENVPYVVVC
     KGFKRQKKPT SNLSSQQFSF PGQQVGQQQS NPWI