ID   CEM20_MEGRO             Reviewed;         202 AA.
AC   Q9GRC4;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Cement protein 20 {ECO:0000303|PubMed:31495314};
DE   AltName: Full=20 kDa cement protein {ECO:0000303|PubMed:11368778};
DE            Short=Mrcp-20k {ECO:0000303|PubMed:11368778};
DE   Flags: Precursor;
GN   Name=cp-20k {ECO:0000303|PubMed:11368778};
OS   Megabalanus rosa (Acorn barnacle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Cirripedia; Thoracica; Thoracicalcarea; Balanomorpha; Balanoidea;
OC   Balanidae; Megabalaninae; Megabalanus.
OX   NCBI_TaxID=6680 {ECO:0000312|EMBL:BAB18762.1};
RN   [1] {ECO:0000312|EMBL:BAB18762.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-56, FUNCTION,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11368778; DOI=10.1042/0264-6021:3560503;
RA   Kamino K.;
RT   "Novel barnacle underwater adhesive protein is a charged amino acid-rich
RT   protein constituted by a Cys-rich repetitive sequence.";
RL   Biochem. J. 356:503-507(2001).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18021251; DOI=10.1111/j.1742-4658.2007.06161.x;
RA   Mori Y., Urushida Y., Nakano M., Uchiyama S., Kamino K.;
RT   "Calcite-specific coupling protein in barnacle underwater cement.";
RL   FEBS J. 274:6436-6446(2007).
RN   [3] {ECO:0007744|PDB:6LEK}
RP   STRUCTURE BY NMR OF 19-202, AND DISULFIDE BONDS.
RX   PubMed=31495314; DOI=10.1098/rstb.2019.0198;
RA   Mohanram H., Kumar A., Verma C.S., Pervushin K., Miserez A.;
RT   "Three-dimensional structure of Megabalanus rosa Cement Protein 20 revealed
RT   by multi-dimensional NMR and molecular dynamics simulations.";
RL   Philos. Trans. R. Soc. Lond., B, Biol. Sci. 374:20190198-20190198(2019).
CC   -!- FUNCTION: Component of the insoluble proteinaceous cement which allows
CC       underwater adhesion to rocks and other surfaces (PubMed:11368778,
CC       PubMed:18021251). Shows specific adsorption on calcite substrates
CC       (PubMed:18021251). {ECO:0000269|PubMed:11368778,
CC       ECO:0000269|PubMed:18021251}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11368778,
CC       ECO:0000269|PubMed:18021251}.
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DR   EMBL; AB035415; BAB18762.1; -; mRNA.
DR   PDB; 6LEK; NMR; -; A=19-202.
DR   PDBsum; 6LEK; -.
DR   AlphaFoldDB; Q9GRC4; -.
DR   SMR; Q9GRC4; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0022608; P:multicellular organism adhesion; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000305"
FT   CHAIN           20..202
FT                   /note="Cement protein 20"
FT                   /evidence="ECO:0000269|PubMed:11368778"
FT                   /id="PRO_5004330620"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        51..64
FT                   /evidence="ECO:0000269|PubMed:31495314,
FT                   ECO:0007744|PDB:6LEK"
FT   DISULFID        120..126
FT                   /evidence="ECO:0000269|PubMed:31495314,
FT                   ECO:0007744|PDB:6LEK"
FT   DISULFID        149..167
FT                   /evidence="ECO:0000269|PubMed:31495314,
FT                   ECO:0007744|PDB:6LEK"
FT   DISULFID        172..178
FT                   /evidence="ECO:0000269|PubMed:31495314,
FT                   ECO:0007744|PDB:6LEK"
FT   STRAND          23..30
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   HELIX           36..42
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   HELIX           99..111
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   STRAND          116..119
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   HELIX           141..143
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   STRAND          157..159
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:6LEK"
FT   STRAND          173..176
FT                   /evidence="ECO:0007829|PDB:6LEK"
SQ   SEQUENCE   202 AA;  22467 MW;  3EDF48D4C6D9C0DF CRC64;
     MKWFLFLLTT AVLAAVVSAH EEDGVCNSNA PCYHCDANGE NCSCNCELFD CEAKKPDGSY
     AHPCRRCDAN NICKCSCTAI PCNEDHPCHH CHEEDDGDTH CHCSCEHSHD HHDDDTHGEC
     TKKAPCWRCE YNADLKHDVC GCECSKLPCN DEHPCYRKEG GVVSCDCKTI TCNEDHPCYH
     SYEEDGVTKS DCDCEHSPGP SE