ID G5ENA7_RAT Unreviewed; 2720 AA.
AC G5ENA7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Thyroglobulin {ECO:0000256|ARBA:ARBA00017326};
GN Name=Tg {ECO:0000313|EMBL:BAL14776.1, ECO:0000313|RGD:3848};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|EMBL:BAL14776.1};
RN [1] {ECO:0000313|EMBL:BAL14776.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BrlHan:WIST@Jcl {ECO:0000313|EMBL:BAL14776.1};
RA Sato A., Aoyama H.;
RT "A single nucleotide polymorphism in thyroglobulin gene causes dwarfism and
RT goiter in Wistar Hannover GALAS rats.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AB682739; BAL14776.1; -; mRNA.
DR ESTHER; ratno-thyro; Thyroglobulin.
DR MEROPS; I31.950; -.
DR RGD; 3848; Tg.
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; 9.
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; IPR016324; Thyroglobulin.
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; 10.
DR PIRSF; PIRSF001831; Thyroglobulin; 2.
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; 6.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 11.
PE 2: Evidence at transcript level;
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 Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW Thyroid hormone {ECO:0000256|ARBA:ARBA00022920};
KW Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..2720
FT /note="Thyroglobulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003476379"
FT DOMAIN 32..93
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 94..161
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 162..246
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 251..317
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 557..610
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 611..678
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 679..874
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 955..1026
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1027..1098
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1099..1163
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 1462..1516
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REGION 2683..2720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 64..71
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 73..93
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 132..139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 141..161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 165..184
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 590..610
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 995..1002
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1134..1141
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 1143..1163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 2720 AA; 299022 MW; B7771A22FD1CAC9F CRC64;
MMTLVLWVST LLSSVCLVAA NIFEYQVDAQ PLRPCELQRE KAFLKQDEYV PQCSEDGSFQ
TVQCQNDGQS CWCVDSDGTE VPGSRQLGRP TACLSFCQLH KQRILLSSYI NSTDALYLPQ
CQDSGNYAPV QCDLQQVQCW CVDTEGMEVY GTRQQGRPTR CPRSCEIRSR RLLHGVGDKS
PPQCDADGEF MPVQCKFVNT TDMMIFDLIH NYNRFPDAFV TFSAFRNRFP EVSGYCYCAD
SQGRELAETG PTKCEVEQFT ATSFGHPYIP SCHRDGHYQT VQCQMERMCW CVDAQGIEIP
GTRQQGQPLF CAKDQSCASE RQQALSRLYF ETPGYFSPQD LLSSEDRLVP VSGARLDISC
PPRIKELFVD SGLLRSIAVE RYQQLSESRS LLREAIRAIF PSRELAGLAL QFTTNPKRLQ
QNLFGGTFLV NAAQLNLSGA LGTRSTFNFS QFFQQFGLPG FLVRDRATDL AKLLPVSLDS
SPTPVPLRVP EKRVAMNKSV VGTFGFKVNL QENQDALKFL VSLMELPEFL VFLQRAVSVP
EDRARDLGDV MEMVFSAQAC KQTSGRFFVP SCTAEGSYED IQCYAGECWC VNSQGKEVEG
SRVSGGHPRC PTKCEKQRAQ MQNLAGAQPA GSSFFVPTCT SEGYFLPVQC FNSECYCVDA
EGQVIPGTQS TIGEPKLCPS VCQLQAEQAF LGVVGVLLSN SSMVPPISSV YIPQCSTSGQ
WMPVQCDGPH EQVFEWYERW NTQNSDGQEL TTATLLMKLM SYREVASTNF SLFLQSLYDA
GQQSIFPVLA QYPSLQDVPQ VVLEGATIQP GENIFLDPYI FWQILNGQLS QYPGPYSDFS
MPLEHFNLRS CWCVDEAGQE LDGTRTRAGE IPACPGPCEE VKFRVLKFIK ETEEIVSASN
ASSFPLGESF LVAKGIQLTS EELGLPPLYP SREAFSEKFL RGSEYAIRLA AQSTLTFYQK
LRASLGESNG TASLLWSGPY MPQCNTIGGW EPVQCHPGTG QCWCVDGWGE LIPGSLMARS
SQMPQCPTSC ELSRANGLIS AWKQAGHQRN PGPGDLFTPV CLQTGEYVRQ QTSGTGAWCV
DPSSGEGVPT NTNSSAQCPG LCDALKSRVL SRKVGLGYTP VCEALDGGFS PVQCDLAQGS
CWCVLGSGEE VPGTRVVGTQ PACESPQCPL PFSGSDVTDG VVFCETASSS GVTTVQQCQL
FCRQGLRNVF SPGPLICNLE SQRWVTLPLP RACQRPQLWQ TMQTQAHFQL LLPPGKMCSI
DYSGLLQAFQ VFILDELITR GFCQIQVKTF GTLVSRTVCD NSSIQVGCLT AERLGVNATW
KLQLEDISVG SLPNLHSIER ALMGQDLLGR FANLIQSGKF QLHLDSKTFS ADTILYFLNG
DRFVTSPMTQ LGCLEGFYRV STTSQDPLGC VKCPEGSFSQ DGKCTPCPAG TYQGQAGSSA
CIPCPRGRTT TITGAFSKTH CVTDCQRDEA GLQCDQNGQY QANQKDMDSG EVFCVDSEGQ
RLQWLQTEAG LSESQCLMMR KFEKAPESKV IFDASSPVIV KSRVPSANSP LVQCLADCAD
DEACSFVTVS SMSSEVSCDL YSWTRDNFAC VTSDQEEDAV DSLKETSFGS LRCQVKVRNS
GKDSLAVYVK KGHEFTASGQ KSFEPTGFQN VLSGLYSSVV FSALGTNLTD THLFCLLACD
QDSCCDGFIV TQVKEGPTIC GLLSAPDILV CHINDWRDAS DTQANGTCAG VTYDQGSRQM
TMSLGGQEFL QGLTLLEGTQ DSFISFQQVY LWKDSDIGSR PESMGCGRGM VPKSEAPEGA
DMATELFSPV DITQVIVNTS HSLPSQQYWL STHLFSAEQA NLWCLSRCAQ EPVFCQLADI
MESSSLYFTC SLYPEAQVCD NDVESNAKNC SQILPRQPTA LFQRKVVLND RVKNFYTRLP
FQKLSGISIR DRIPMSEKLI SNGFFECERL CDRDPCCTGF GFLNVSQMQG GEMTCLTLNS
MGIQTCSEEN GATWRILDCG SEDTEVHTYP FGWYQKPAVW SDAPSFCPSA ALQSLTEEKV
ALDSWQTLAL SSVIIDPSIK HFDVAHISIS ATRNFSLAQD FCLQECSRHQ DCLVTTLQIQ
QGVVRCVFYP DIQSCEHSLR SKTCWLLLHE EAAYIYRKSG APLHQSDGIS TPSVHIDSFG
QLQGGSQVVK VGTAWKQVYQ FLGVPYAAPP LAENRFQAPE VLNWTGSWDA TKLRSSCWQP
GTRTPTPPQI SEDCLYLNVF VPENLVSNAS VLVFFHNTVE MEGSGGQLNI DGSILAAVGN
LIVVTANYRL GVFGFLSSGS DEVAGNWGLL DQVAALTWVQ THIGAFGGDP QRVTLAADRG
GADVASIHLL ITRPTRLQLF RKALLMGGSA LSPAAIISPD RAQQQAAALA KEVGCPNSSV
QEVVSCFRQK PANILNEAQT KLLAVSGPFH YWGPVVDGQY LRELPSRRLK RPLPVKVDLL
IGGSQDDGLI NRAKAVKQFE ESQGRTNSKT AFYQALQNSL GGEDSDARIL AAAIWYYSLE
HSTDDYASFS RALENATRDY FIICPIVNMA SLWARRTRGN VFMYHVPESY GHGSLELLAD
VQYAFGLPFY SAYQGYFSTE EQSLSLKVMQ YFSNFIRSGN PNYPHEFSQK AAEFATPWPD
FVPGAGGESY KELSAQLPNR QGLKKADCSF WSKYIQTLKD ADGAKDAQLT KSGEEDLEVG
PGSEEDFSGS LEPVPKSYSK
//
