ORCH_CRYCV
ID ORCH_CRYCV Reviewed; 128 AA.
AC Q9XYT4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Orchestin;
DE Flags: Precursor;
OS Cryptorchestia cavimana (Amphipod) (Orchestia cavimana).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Peracarida; Amphipoda; Senticaudata;
OC Talitrida; Talitroidea; Talitridae; Cryptorchestia.
OX NCBI_TaxID=1577145;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD32571.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP PROTEIN SEQUENCE OF 109-119 AND 125-128, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INDUCTION.
RX PubMed=11772404; DOI=10.1042/0264-6021:3610327;
RA Testeniere O., Hecker A., Le Gurun S., Quennedey B., Graf F., Luquet G.;
RT "Characterization and spatiotemporal expression of orchestin, a gene
RT encoding an ecdysone-inducible protein from a crustacean organic matrix.";
RL Biochem. J. 361:327-335(2002).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 23-35, AND CALCIUM-BINDING.
RX PubMed=8620040; DOI=10.1016/0167-4838(95)00266-9;
RA Luquet G., Testeniere O., Graf F.;
RT "Characterization and N-terminal sequencing of a calcium binding protein
RT from the calcareous concretion organic matrix of the terrestrial crustacean
RT Orchestia cavimana.";
RL Biochim. Biophys. Acta 1293:272-276(1996).
RN [3] {ECO:0000305}
RP PHOSPHORYLATION, AND CALCIUM-BINDING.
RX PubMed=12560077; DOI=10.1016/s0014-5793(02)03856-5;
RA Hecker A., Testeniere O., Marin F., Luquet G.;
RT "Phosphorylation of serine residues is fundamental for the calcium-binding
RT ability of orchestin, a soluble matrix protein from crustacean calcium
RT storage structures.";
RL FEBS Lett. 535:49-54(2003).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP CALCIUM-BINDING.
RX PubMed=15099573; DOI=10.1016/j.jsb.2004.01.009;
RA Hecker A., Quennedey B., Testeniere O., Quennedey A., Graf F., Luquet G.;
RT "Orchestin, a calcium-binding phosphoprotein, is a matrix component of two
RT successive transitory calcified biomineralizations cyclically elaborated by
RT a terrestrial crustacean.";
RL J. Struct. Biol. 146:310-324(2004).
CC -!- FUNCTION: Plays a role in cuticle calcification. May induce
CC precipitation of the calcium stored in the posterior caeca as calcium
CC carbonate. {ECO:0000269|PubMed:15099573}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15099573}.
CC Note=During the premolt period, localizes to microvilli-rich apical
CC regions and to the subnuclear region. During the postmolt period,
CC localizes to the intercellular space, basal region of cells and calcium
CC reabsorption spherules.
CC -!- TISSUE SPECIFICITY: Posterior caeca epithelium of the gut.
CC {ECO:0000269|PubMed:11772404, ECO:0000269|PubMed:15099573}.
CC -!- DEVELOPMENTAL STAGE: Expression is detected at the start of the premolt
CC period and accumulates during this period from D1'b to D3. After
CC ecdysis, expressed in the postmolt period but at much lower levels. Not
CC detected in the intermolt period. {ECO:0000269|PubMed:11772404,
CC ECO:0000269|PubMed:15099573}.
CC -!- INDUCTION: Indirectly by 20-hydroxyecdysone.
CC {ECO:0000269|PubMed:11772404}.
CC -!- PTM: Phosphorylated on Ser and Tyr residues. Calcium-binding activity
CC is dependent on serine phosphorylation but not on tyrosine
CC phosphorylation. {ECO:0000269|PubMed:12560077}.
CC -!- MISCELLANEOUS: Binds calcium. {ECO:0000269|PubMed:12560077,
CC ECO:0000269|PubMed:8620040}.
CC -!- CAUTION: N-terminal sequence obtained in PubMed:8620040 was later shown
CC to be incomplete at the N-terminus. {ECO:0000305|PubMed:11772404}.
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DR EMBL; AF124526; AAD32571.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9XYT4; -.
DR SMR; Q9XYT4; -.
DR GO; GO:0045178; C:basal part of cell; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; NAS:UniProtKB.
DR GO; GO:0048589; P:developmental growth; IDA:UniProtKB.
DR GO; GO:0009725; P:response to hormone; IDA:UniProtKB.
DR GO; GO:0031215; P:shell calcification; NAS:UniProtKB.
PE 1: Evidence at protein level;
KW Biomineralization; Calcium; Direct protein sequencing; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:11772404"
FT CHAIN 21..128
FT /note="Orchestin"
FT /evidence="ECO:0000269|PubMed:11772404"
FT /id="PRO_0000233934"
FT REGION 23..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 25
FT /note="S -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="D -> DD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="L -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 14578 MW; 92896EFAF797CF70 CRC64;
MNKVFIIGVC LFIVSQAVLA VPWDSDESSD ERLSDRSDES REEPRKLVVS DDDSREDSNE
SAEVRRRDDS RESEEEPRKL SADTSDEDSD DSQESPLDLF FKTLRDSKIS RAQRAALLKA
LLSRYAGY
