IMSP5_RUDPH
ID IMSP5_RUDPH Reviewed; 135 AA.
AC P86986;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Insoluble matrix shell protein 5 {ECO:0000303|PubMed:21221694};
DE Short=IMSP5 {ECO:0000303|PubMed:21221694};
DE Flags: Precursor;
OS Ruditapes philippinarum (Japanese littleneck clam) (Venerupis
OS philippinarum).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei;
OC Venerida; Veneroidea; Veneridae; Ruditapes.
OX NCBI_TaxID=129788;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Beck A.;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 32-40.
RC TISSUE=Shell {ECO:0000269|PubMed:21221694};
RX PubMed=21221694; DOI=10.1007/s10126-010-9357-0;
RA Marie B., Trinkler N., Zanella-Cleon I., Guichard N., Becchi M.,
RA Paillard C., Marin F.;
RT "Proteomic identification of novel proteins from the calcifying shell
RT matrix of the manila clam Venerupis Philippinarum.";
RL Mar. Biotechnol. 13:955-962(2011).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21221694}.
CC -!- TISSUE SPECIFICITY: Component of the acid-insoluble organic matrix of
CC the calcified shell. {ECO:0000269|PubMed:21221694}.
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; AM874357; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P86986; -.
DR SMR; P86986; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13202; EF-hand_5; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Metal-binding; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..135
FT /note="Insoluble matrix shell protein 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000413029"
FT DOMAIN 21..56
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 93..128
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 135 AA; 15606 MW; C561A06694EAB0EB CRC64;
MILVVTLACL IAVVCCQCPT TDQGQISKVF KAYDIDGNNK ISRVEGTMVF RDADLNRDGA
LDNNEFSSEW AFYHNDYYSP FFNVADRNHN GRIEFVEGNQ GFDHFDKNRD NEISSWEFTQ
TWMETVRPSS RPIDF