ID A0A151P8H6_ALLMI Unreviewed; 2447 AA.
AC A0A151P8H6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Thyroglobulin {ECO:0000256|ARBA:ARBA00017326};
GN Name=TG {ECO:0000313|EMBL:KYO45209.1};
GN ORFNames=Y1Q_0014663 {ECO:0000313|EMBL:KYO45209.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO45209.1};
RN [1] {ECO:0000313|EMBL:KYO45209.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO45209.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000256|ARBA:ARBA00005964}.
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:KYO45209.1}.
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DR EMBL; AKHW03000629; KYO45209.1; -; Genomic_DNA.
DR STRING; 8496.A0A151P8H6; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00191; TY; 7.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 10.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR14093; HLA CLASS II GAMMA CHAIN; 1.
DR PANTHER; PTHR14093:SF19; THYROGLOBULIN; 1.
DR Pfam; PF00135; COesterase; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00086; Thyroglobulin_1; 8.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00211; TY; 10.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 11.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 7.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 10.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500}; Hormone {ECO:0000256|ARBA:ARBA00022702};
KW Iodination {ECO:0000256|ARBA:ARBA00022653};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW Thyroid hormone {ECO:0000256|ARBA:ARBA00022920};
KW Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534}.
FT DOMAIN 50..111
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 112..179
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 343..403
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 635..688
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 689..756
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 757..952
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1059..1105
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1106..1180
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1181..1245
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1547..1601
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DISULFID 82..89
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 91..111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 150..157
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 159..179
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 383..403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 668..688
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1074..1081
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1216..1223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1225..1245
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 2447 AA; 270984 MW; C51287A2B73E22A7 CRC64;
MSENRRGAFD DGENTLEQNT VLIGQLFCTS LGNSELLEKN GKYQAESQPL RPCELRREKA
FLEGEDHVPQ CSEDGQFRTV QCSKNNLSCW CVDDKGAEVP GSKQNGVPIS CLSFCQLQKQ
QVLVSRYINS STISYIPQCL DSGEFAPVQC DVGLGQCWCV DSEGMEIYGT RQTGKPTQCP
GSCEIRDRRI LHGVGDRSPP QCSADGEFLP VQCKFVNMTN MMVFDLVHSY NRDFAIAVHP
VQKVLSCDSD KQYHRTLRFP EAFQTFSSFR SMFPGVSGYC YCADSLGREL AETGLELLLE
EVYDTIFSAL EPALTFAETT MYRILQRRFL GVQLAALGRF RCPSKCEVER STAVRFGHTY
KPSCDDHGDY NPLQCQQDGQ CWCVGNKGQE FQGTRRQGQL PVCGEEQTCI SERRQALSKL
FYGPVGHFSQ HSLFNTQEMK AEEIGRFSKS CPPSFKELFV DSGLLSPLTE RPGLNQQLEL
ESILSEAVRG MFPSRELAQV ALQFTSNPKR FQENLFGGKF LKNLIQFNFT GALGTRGKFN
IGQFSQQGGM DSGESVAKLA EEPSLETSEE SFITSKPLVD SFGRTVSLQD NQNAMKFLAS
VLELPEFFTF LQHVIFVPED ISEDLGEVVR IVLRSKDCTE ESSNLFVPTC TKEGRYEEIQ
CYAAECWCVD SQGREVPGSR VQGKRPRCAT TCEKQRSRLQ RLKQSQPAGS DPFIPTCTEE
GDFLPVQCHG PDCFCVDLDG RTIPGTKRKA GKPMQCPSPC QLTAGQVFLE TVQLLLSDTS
ALSQISRVYI PQCSTDGNWR PVQCSGPPEQ AFEWYQRWIS ENNEGKTLPV TDLFNILTEY
KETSSQRFAA FVKNLYEAGH QNIFPAFTKY PSFNALPVEV LDGSITTESE NILLDPYTFW
QLLQGQLNYY PGSYADFSAL LGHFELRNCW CVDDKGEELQ GTKTEVNKVP ACPGACESMK
KEAMQLIDEA EQLIVASNGS HFPFGESFLM AKGIQLMDHD LLHFTQSFQS GTMFSEKILT
GSDYAIRLAA QSTLHFYWRN RFISRSSAGE AMLLGFHPYI PQCDGLGNWE PVQCYESTGH
CWCVDKRGRY VTGSLRARSA QLPTCQTSCQ RSRANALISS WKQSGVPCNT APADLFIPSC
LETGEYTLLQ KLDSDAQCVD PMSGDVLQRS SQDSDGNPQC PALCSMLKPK MSSREIGKGY
IPQCEGNNGS FSPVQCSQDE KSCWCVFESG EEVPGSRVSG ERPACESPQC VLPFNVSHVV
NGVIFCETVS DQNRNSQQCQ LVCRRGFQSA FSSKRFLCDV ESRRWISDPP LSQTCQKLQL
FQTVQAQTQF QLLLPSGKAC SSDYSGLLQA FQIFILDELK ARGFCHIQVN AFGNSRPVSL
CDDSTVLVNC LTVDRLGVNI TWKAQLEDIP AASLPDLHDI ENTIVGDNLI GRFVKLIKSG
GFLLHLDSKQ FPAATSISFL RDEDFDLSPS VQLGCRSGFR RSSSPGTAIS NSQGCVVCPL
GSYFQNGECT PCPHGSYQLQ TGSPSCIKCP SGKTTVSTGA FTADHCITDC QQNRQSLQCD
EEGQYRPSQQ DPITKKSFCV DNLGTRLGWT ETDDLLTDSQ CLVLRKFERV PTSKIIYSME
DAEVFRSKTV QGDLQSPFWQ CISDCVQEES CSFVTVSTTG SKVLCELYRA VETNFNCTTS
GLMQGALGNS AASSIAHLSC LLKIRNQEKD EVAIYLKKGQ EFTTSGLKTF EMTDFQNVFS
GIYSSMVLSA ASTSLTDVHL LCRQACSQDP CCDGFILSQM TLHGGTILCG LMSYPDVLIC
NTNDWSQTSI PGTDGICKGV NCDEKDKKFS FSLGGQVFTG TCELPEGPEG FFTSFQRVYL
WRESAGELFS VMDNNLIQID RSRSLPAQEY WLFKHKFSLK QATRWCLTRC TQEGAFCQLV
DLQNTTGTYF VCTLYPEAQV CDNSINKIPD SCQTILPREP QIVHYKRVTL GATVKNFYTR
LPFRKVTGIA VRNKIDLSGK AISDGFFECE RWCDADPCCM GFGLLNGLQS TGGKVLCLTL
NGLGIQTCAE ETRSAWQVSD CSSSDAEANT YPFGWYQKPA NLKRTIPSVC PPVLLPLQPE
TVSLDMWQLL DASSVLVDSS LVNFDVVQVS RDNSGNFTAA RDICLSACSK SQSCIVVTLE
IQLSTIRCIF YPDTKICTHG LQGHSCRILL KEPATYIYRR QDLFLPISEP GVTSVNIPSQ
GVLIGRSRAI RIGAEWRSVS WFLGIPYAAP PVAENRFRPP APFTWLESWN ATMARAACWQ
PGDGAVQAST VSEDCLYLNV FVPADTVRNT SVLLFFHNGG NDGTEKGNAA IDGSYLAAVS
DVIVVIASYR VGIFGFLSTG SQVATGNWGL LDQVAALRWV KKNIASFGGD PRQISIAADR
SGADITSIHL LAKSVDSNLF ERAVLMVSPI LLYFISQVPI KDILMKG
//
