ID A0A151K190_9HYME Unreviewed; 1261 AA.
AC A0A151K190;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Thyroglobulin {ECO:0000313|EMBL:KYN45212.1};
DE Flags: Fragment;
GN ORFNames=ALC56_00334 {ECO:0000313|EMBL:KYN45212.1};
OS Trachymyrmex septentrionalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN45212.1, ECO:0000313|Proteomes:UP000078541};
RN [1] {ECO:0000313|EMBL:KYN45212.1, ECO:0000313|Proteomes:UP000078541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN45212.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN45212.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex septentrionalis WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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DR EMBL; KQ981191; KYN45212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151K190; -.
DR STRING; 34720.A0A151K190; -.
DR Proteomes; UP000078541; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00191; TY; 4.
DR CDD; cd00199; WAP; 1.
DR Gene3D; 4.10.75.10; Elafin-like; 2.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 6.
DR InterPro; IPR004094; Antistasin-like.
DR InterPro; IPR006150; Cys_repeat_1.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR011061; Hirudin/antistatin.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR028150; Lustrin_cystein.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR InterPro; IPR008197; WAP_dom.
DR PANTHER; PTHR12352:SF3; NIDOGEN-2; 1.
DR PANTHER; PTHR12352; SECRETED MODULAR CALCIUM-BINDING PROTEIN; 1.
DR Pfam; PF02822; Antistasin; 4.
DR Pfam; PF14625; Lustrin_cystein; 3.
DR Pfam; PF00086; Thyroglobulin_1; 6.
DR Pfam; PF00095; WAP; 2.
DR SMART; SM00211; TY; 6.
DR SMART; SM00217; WAP; 2.
DR SMART; SM00289; WR1; 3.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF57256; Elafin-like; 1.
DR SUPFAM; SSF57262; Leech antihemostatic proteins; 3.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 6.
DR PROSITE; PS51252; ANTISTASIN; 3.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 4.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 6.
DR PROSITE; PS51390; WAP; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500}; Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 18..95
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 95..121
FT /note="Antistasin-like"
FT /evidence="ECO:0000259|PROSITE:PS51252"
FT DOMAIN 214..262
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 264..331
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 463..531
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 541..566
FT /note="Antistasin-like"
FT /evidence="ECO:0000259|PROSITE:PS51252"
FT DOMAIN 601..647
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 649..717
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 723..749
FT /note="Antistasin-like"
FT /evidence="ECO:0000259|PROSITE:PS51252"
FT DOMAIN 895..962
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1006..1061
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DISULFID 59..66
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 302..309
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 311..331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 511..531
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 933..940
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 942..962
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KYN45212.1"
SQ SEQUENCE 1261 AA; 138096 MW; 486B064FD9B05C8D CRC64;
EERCCKTACG LRCAAGELTG CEQLELAAVR RSRALGARGP QQFIPRCNNE TGEFERIQCE
PHGRSCWCVD EIGAEIPGTR APSKSVVDCD KPHSCPAHSC RMLCPLGFEI NEITGCPKCE
CRDPCRGVTC PGIGQTCELI AVNCIREPCP PVPSCRKTRS LSTICPAGEP LQITDSPRPF
LCGDTPGKPT CPPMYSCLVE YKQEYGVCCP ASVKIQRPGM CPAEESTMSS CGPTCRYDLD
CPGPQKCCNN KNCGGNVCTI PGDLTACHRD RMLAEILSVS ERQGRGYIPQ CMEDGSFQSR
QCSRNGLVCW CVDGDGRKIS GSMGPAEKID CRSISKARSL PASCTSQQCA QVCQYGFKTD
ASGCSTCECD DPCEGFPCPE GQECILKQEN SCPDFLCPTK PECKPRKTYK SPCTVGAPLI
DQDGNAATCS TNETCPDDYK CTMVQEADQS VCCMETSNPA KAPTMCEYLR DFNDRMEGTR
EGMSLAIPAP QCEEDGGYKS LQCYNSTSCK CVNHRGVTLK SGLDSAASAD CEAIKELTQI
CKRLYCNLIC PYGYEVDATG CEQCHCHEPC RDVICGSHET CTMIDVNCGP NEYCPAVPAC
LTTKPGQCPY LVPSSSSCEL QCSNDQECSS GDKCCSTGCG TQCVAPVMAT ACQHARAVAE
HAARESGEPA RRTYIPRCDS NGAFEPVQCH NGMCWCVDEE GKEAAGTRVL EGIVPRCNTP
LRCPEIDCKL DCPDGFELDA DTGCPTCSCR DPCRSVTCRG ENEACRMVEV ACSAPPCPPV
PVCLPKKDNP CPNSSPLLEQ NGSIATCGPH GHHCPSTHKC ELSPLDEYAV CCPKPREVCF
EPPRRIPCNP SVGFNETERW FFDPERNECR RKNECTVGHN DFSSRLVCDT VCPVLSQCER
LREKNLKRSQ RLKQPTFLPK CNPDSGTWEP VQCLEHVGVC WCVNRKGQPI KGSLTRAAEP
KCNFRQARRG GRRPESQEID REIQAIMEDA LLNLETDERQ TGKILGTRCQ AMKNKGHVPT
ICDSQGRFEP TQCAGDTCWC VDEAGNQLIG SEPFVKGTNI CLPTPVEAVE VTLRFPGRFL
ASDEKRFARE AENFLHELGA RLRKDIRVEI NQDSAILSFE IVGTNKVDVA FHLEELTRIQ
KLSLLGSSAD ATTSRFTHRS TPVAMQSRIV TLEQREILTQ MESPFYQTAT IVLAASSAFI
ISSLMKLKDP SKMFPMDQHF LAYSQQPVYV ISGSEQNEKE KENAAHQKLE NIHTSDTIVG
A
//
