EFCB_NEPCI
ID EFCB_NEPCI Reviewed; 687 AA.
AC G9M8X1;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Calcium-binding protein SP84 {ECO:0000303|PubMed:22019571};
DE AltName: Full=84 kDa salivary protein {ECO:0000303|PubMed:22019571};
DE Short=NcSP84 {ECO:0000303|PubMed:22019571};
DE Flags: Precursor;
OS Nephotettix cincticeps (Green rice leafhopper) (Selenocephalus cincticeps).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Membracoidea;
OC Cicadellidae; Deltocephalinae; Chiasmini; Nephotettix.
OX NCBI_TaxID=94400;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAL41365.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-37, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP CALCIUM-BINDING.
RC TISSUE=Saliva {ECO:0000269|PubMed:22019571}, and
RC Salivary gland {ECO:0000269|PubMed:22019571};
RX PubMed=22019571; DOI=10.1016/j.ibmb.2011.10.001;
RA Hattori M., Nakamura M., Komatsu S., Tsuchihara K., Tamura Y., Hasegawa T.;
RT "Molecular cloning of a novel calcium-binding protein in the secreted
RT saliva of the green rice leafhopper Nephotettix cincticeps.";
RL Insect Biochem. Mol. Biol. 42:1-9(2012).
CC -!- FUNCTION: Binds calcium. During feeding of the phloem sap, protein is
CC injected into sieve tubes of rice plants. This process may suppress the
CC sieve-element clogging and facilitate continuous ingestion from sieve
CC tubes. {ECO:0000269|PubMed:22019571, ECO:0000303|PubMed:22019571}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22019571}.
CC -!- TISSUE SPECIFICITY: Expressed in salivary glands where expression is
CC strongest in type III cells in the posterior lobe of the principal
CC glands (at protein level). Not expressed in midgut, Malpighian tubules
CC or epidermis. {ECO:0000269|PubMed:22019571}.
CC -!- DEVELOPMENTAL STAGE: Expressed on days 0-7 after adult emergence at
CC roughly constant level (at protein level).
CC {ECO:0000269|PubMed:22019571}.
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DR EMBL; AB618633; BAL41365.1; -; mRNA.
DR AlphaFoldDB; G9M8X1; -.
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 SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 5.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Metal-binding; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:22019571"
FT CHAIN 20..687
FT /note="Calcium-binding protein SP84"
FT /evidence="ECO:0000303|PubMed:22019571"
FT /id="PRO_0000416970"
FT DOMAIN 152..187
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 257..292
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 406..441
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 476..511
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 579..614
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 592
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 594
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 596
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 598
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 603
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 687 AA; 79605 MW; 6E75366A664CA6AC CRC64;
MMRAIYLLVV VCWAAAANAS SDTVPAEVQT IVKTPGHQYD LYKKMVATIS LPANANTEIH
KGLNIKRPDN KVTKADIELY YWHKDLKYAV TKFLHLINDD GNKEELTAEE FSNDLQKLAF
KVALVECHYQ LSPGLRQACY ADEILTYGAL VLESDDITKF YKHLDNDKDN ELKTEEVLKI
QHTHKNKDNK IVAEELGAYS GAKKDTVTPE EFEEYVTQES IVDDFRECRS KKATEGTTDY
DNVCLTNELV EYVNDDLTEI DISLLYRSVD TNNDNKIIID ELKAFTGITD DVKAKRILEL
LDMSATTPAN AKPVVDYGEW RTYLRSPTVL LQLERDCAMK HNDQLEEINC MYKLLKNLLI
DEHDPIWLEA WDLDHVILFE IFDADKDDGK VFKDDLKKIQ KNFHFKTEAT VTRYMVEADI
DKDSFICLEE FDEYMDIPHM VYGTGECILH SRTKPDERGD CFVEETSDVV DNFKFIENAA
FDTWFNHYDT NHNNKIEKEA DGLLAKFNND ANVLTMFLEE TGQGGLTVEP FEFNWYVKQQ
HLAHAYEDEK IVTALVQKFT AEQITKLHTE LIKYINDEMT ERDIEDLFDE LDHNDDHELT
QQDFPDCWND VKDLLTHIDA LIPEGDEDTT VNYLEFWAWI NHPNPKKPQE LIKKTFETDC
TTKHATQKEE VACYVKTFKT KDKFKTA