ID A0A1D2NAC8_ORCCI Unreviewed; 445 AA.
AC A0A1D2NAC8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Equistatin {ECO:0000313|EMBL:ODN02213.1};
GN ORFNames=Ocin01_04473 {ECO:0000313|EMBL:ODN02213.1};
OS Orchesella cincta (Springtail) (Podura cincta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Entomobryoidea; Orchesellidae; Orchesellinae; Orchesella.
OX NCBI_TaxID=48709 {ECO:0000313|EMBL:ODN02213.1, ECO:0000313|Proteomes:UP000094527};
RN [1] {ECO:0000313|EMBL:ODN02213.1, ECO:0000313|Proteomes:UP000094527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Mixed pool {ECO:0000313|EMBL:ODN02213.1};
RX PubMed=27289101; DOI=10.1093/gbe/evw134;
RA Faddeeva-Vakhrusheva A., Derks M.F., Anvar S.Y., Agamennone V., Suring W.,
RA Smit S., van Straalen N.M., Roelofs D.;
RT "Gene Family Evolution Reflects Adaptation to Soil Environmental Stressors
RT in the Genome of the Collembolan Orchesella cincta.";
RL Genome Biol. Evol. 8:2106-2117(2016).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ODN02213.1}.
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DR EMBL; LJIJ01000120; ODN02213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D2NAC8; -.
DR STRING; 48709.A0A1D2NAC8; -.
DR OrthoDB; 2944234at2759; -.
DR Proteomes; UP000094527; Unassembled WGS sequence.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 2.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR12352:SF32; AGAP005941-PA; 1.
DR PANTHER; PTHR12352; SECRETED MODULAR CALCIUM-BINDING PROTEIN; 1.
DR Pfam; PF00086; Thyroglobulin_1; 2.
DR SMART; SM00211; TY; 2.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 3.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500}; Reference proteome {ECO:0000313|Proteomes:UP000094527};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..445
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008905291"
FT DOMAIN 140..205
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 213..268
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DISULFID 236..243
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 445 AA; 50302 MW; 14E5B2C00E6BD071 CRC64;
MAIISRSFTT LTFVISLAVL LSVTSQNFKC PDLLSKIPDV CNNVKCQYEV NRHRCPKDTI
YSSAFSLCGC CPQCVKYISP GDEETPCVTN EADVVWTPDS NCQDDSHCPV KVNLCLPGLE
CNGTSMCVLP PPEKVFEHET EECMFRKSLY RLDLTHWDPD CESDGSFSPK QCKGAQYDGE
CFCMNRAGTR IFGREWRIQS ENQTCACSRK VYELRAQSLI STLHCSPDGN YEPLQCDTDS
GLCYCVDPKT GRMDGSAVPQ YHWKTLPCFS VNLTNWEEDG QYLRKCESAF AAGRELQIFG
KEHGTTVEMK EYKCDYDGSY APVQIASTNT ECVFKNGSRI LDYFKANDKA MTCNCARDSK
EYYPLHDRPL NLACQQRTGN YDIAYDFGSR ASCVDSDGFL YGDLAPSKYF CCLLKEGCST
VIENSCYTNV TDEGYKPCQY WRYRN
//
