SGYQP_PINMG
ID SGYQP_PINMG Reviewed; 332 AA.
AC H2A0L9;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Serine, glycine, tyrosine and glutamine-rich protein;
DE AltName: Full=Cement-like protein;
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 106-150; 159-187 AND 300-322, SUBCELLULAR LOCATION, AND
RP 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 mantle edge
CC and lower level in the mantle pallium. {ECO:0000269|PubMed:23213212}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE610386; CCE46160.1; -; mRNA.
DR AlphaFoldDB; H2A0L9; -.
DR PRIDE; H2A0L9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..332
FT /note="Serine, glycine, tyrosine and glutamine-rich
FT protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000417944"
FT REGION 39..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 332 AA; 32498 MW; 700C424052262BC5 CRC64;
MMKTVLLLVV LVGVAYCDDD GWDMGNFFQQ YHQWQQQISS SSSSSSSSGG GGSSGGGASG
GGGGGGSSGG GGASGGGGGG SSGGGGLTKV VLKAGGGGRG GGGIVKSVGG GGGGVTKLVA
AGGASGGGSV SGGGGGGLAL LAGGSAAGGG RSGVVTVSKQ PIIINRQVTH VNTGGSGGGV
GGGFGGGRGG FGYGLYGGHH HYNPCGYGQV YSYYYGCQSI YKQPARQVYH QPIYQPVQTV
YQPVQYYQQP YQYQHSYGQA SHAYQPQTTK YISYSYPQYS SQGSYPIVAG GSAGGFASAR
SGGFGLSSGG IGGHSSYPLS VFKHAKGEKY KL