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Protein

Thyroglobulin

Gene

Tg

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3).

GO - Molecular functioni

  • anion binding Source: RGD
  • chaperone binding Source: RGD
  • protein complex binding Source: RGD
  • protein homodimerization activity Source: RGD
  • receptor binding Source: RGD

GO - Biological processi

  • hormone biosynthetic process Source: UniProtKB-KW
  • response to lipopolysaccharide Source: RGD
  • response to pH Source: RGD
  • thyroid hormone generation Source: RGD
  • transcytosis Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hormone, Thyroid hormone

Keywords - Biological processi

Thyroid hormones biosynthesis

Protein family/group databases

ESTHERiratno-thyro. Thyroglobulin.
MEROPSiS09.978.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroglobulin
Short name:
Tg
Gene namesi
Name:Tg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3848. Tg.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: RGD
  • extracellular space Source: RGD
  • Golgi apparatus Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Defects in Tg are a cause of a form of hypothyroidism in rdw rat.

Keywords - Diseasei

Disease mutation

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 27682748ThyroglobulinPRO_0000008638Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Sulfotyrosine; alternateBy similarity
Modified residuei25 – 251Thyroxine; alternateBy similarity
Disulfide bondi35 ↔ 53PROSITE-ProRule annotation
Disulfide bondi64 ↔ 71PROSITE-ProRule annotation
Disulfide bondi73 ↔ 93PROSITE-ProRule annotation
Disulfide bondi97 ↔ 121PROSITE-ProRule annotation
Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence analysis
Disulfide bondi132 ↔ 139PROSITE-ProRule annotation
Disulfide bondi141 ↔ 161PROSITE-ProRule annotation
Disulfide bondi165 ↔ 184PROSITE-ProRule annotation
Disulfide bondi195 ↔ 236PROSITE-ProRule annotation
Glycosylationi199 – 1991N-linked (GlcNAc...)Sequence analysis
Disulfide bondi302 ↔ 320PROSITE-ProRule annotation
Disulfide bondi331 ↔ 337PROSITE-ProRule annotation
Disulfide bondi339 ↔ 365PROSITE-ProRule annotation
Glycosylationi484 – 4841N-linked (GlcNAc...)Sequence analysis
Glycosylationi496 – 4961N-linked (GlcNAc...)Sequence analysis
Glycosylationi545 – 5451N-linked (GlcNAc...)Sequence analysis
Disulfide bondi608 ↔ 620PROSITE-ProRule annotation
Disulfide bondi631 ↔ 636PROSITE-ProRule annotation
Disulfide bondi638 ↔ 658PROSITE-ProRule annotation
Disulfide bondi662 ↔ 687PROSITE-ProRule annotation
Disulfide bondi698 ↔ 703PROSITE-ProRule annotation
Disulfide bondi705 ↔ 726PROSITE-ProRule annotation
Disulfide bondi730 ↔ 763PROSITE-ProRule annotation
Glycosylationi748 – 7481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi774 ↔ 899PROSITE-ProRule annotation
Glycosylationi817 – 8171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi901 ↔ 922PROSITE-ProRule annotation
Glycosylationi948 – 9481N-linked (GlcNAc...)Sequence analysis
Glycosylationi1017 – 10171N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1043 ↔ 1050PROSITE-ProRule annotation
Disulfide bondi1052 ↔ 1074PROSITE-ProRule annotation
Disulfide bondi1078 ↔ 1109PROSITE-ProRule annotation
Disulfide bondi1127 ↔ 1146PROSITE-ProRule annotation
Glycosylationi1141 – 11411N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1150 ↔ 1170PROSITE-ProRule annotation
Disulfide bondi1182 ↔ 1189PROSITE-ProRule annotation
Disulfide bondi1191 ↔ 1211PROSITE-ProRule annotation
Glycosylationi1349 – 13491N-linked (GlcNAc...)Sequence analysis
Glycosylationi1365 – 13651N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1513 ↔ 1522PROSITE-ProRule annotation
Disulfide bondi1542 ↔ 1564PROSITE-ProRule annotation
Glycosylationi1715 – 17151N-linked (GlcNAc...)Sequence analysis
Glycosylationi1773 – 17731N-linked (GlcNAc...)Sequence analysis
Glycosylationi1866 – 18661N-linked (GlcNAc...)Sequence analysis
Glycosylationi1937 – 19371N-linked (GlcNAc...)Sequence analysis
Glycosylationi2012 – 20121N-linked (GlcNAc...)Sequence analysis
Glycosylationi2122 – 21221N-linked (GlcNAc...)Sequence analysis
Glycosylationi2251 – 22511N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2265 ↔ 2282PROSITE-ProRule annotation
Glycosylationi2296 – 22961N-linked (GlcNAc...)Sequence analysis
Glycosylationi2445 – 24451N-linked (GlcNAc...)Sequence analysis
Modified residuei2574 – 25741ThyroxineBy similarity
Glycosylationi2583 – 25831N-linked (GlcNAc...)Sequence analysis
Modified residuei2588 – 25881ThyroxineBy similarity
Modified residuei2766 – 27661TriiodothyronineBy similarity

Post-translational modificationi

Sulfated tyrosines are desulfated during iodination.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Iodination, Sulfation

Proteomic databases

PaxDbiP06882.
PRIDEiP06882.

Expressioni

Tissue specificityi

Thyroid gland specific.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
Hspa5P067616EBI-1549657,EBI-916036
Pdia4P386593EBI-1549657,EBI-917435

GO - Molecular functioni

  • chaperone binding Source: RGD
  • protein complex binding Source: RGD
  • protein homodimerization activity Source: RGD
  • receptor binding Source: RGD

Protein-protein interaction databases

IntActiP06882. 3 interactions.
STRINGi10116.ENSRNOP00000009241.

Structurei

3D structure databases

ProteinModelPortaliP06882.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 9362Thyroglobulin type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini94 – 16168Thyroglobulin type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 298137Thyroglobulin type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini299 – 35961Thyroglobulin type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini605 – 65854Thyroglobulin type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini659 – 72668Thyroglobulin type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini727 – 922196Thyroglobulin type-1 7PROSITE-ProRule annotationAdd
BLAST
Domaini923 – 1074152Thyroglobulin type-1 8PROSITE-ProRule annotationAdd
BLAST
Domaini1075 – 114672Thyroglobulin type-1 9PROSITE-ProRule annotationAdd
BLAST
Domaini1147 – 121165Thyroglobulin type-1 10PROSITE-ProRule annotationAdd
BLAST
Repeati1455 – 146814Type IIAdd
BLAST
Repeati1469 – 148517Type IIAdd
BLAST
Repeati1486 – 150217Type IIAdd
BLAST
Domaini1510 – 156455Thyroglobulin type-1 11PROSITE-ProRule annotationAdd
BLAST
Repeati1602 – 1722121Type IIIAAdd
BLAST
Repeati1723 – 1891169Type IIIBAdd
BLAST
Repeati1892 – 1994103Type IIIAAdd
BLAST
Repeati1995 – 2127133Type IIIBAdd
BLAST
Repeati2128 – 218558Type IIIAAdd
BLAST

Sequence similaritiesi

Contains 11 thyroglobulin type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IG6K. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000128427.
HOVERGENiHBG017929.
InParanoidiP06882.
PhylomeDBiP06882.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
4.10.800.10. 12 hits.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR016324. Thyroglobulin.
IPR000716. Thyroglobulin_1.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
PF07699. Ephrin_rec_like. 1 hit.
PF00086. Thyroglobulin_1. 10 hits.
[Graphical view]
PIRSFiPIRSF001831. Thyroglobulin. 1 hit.
SMARTiSM01411. Ephrin_rec_like. 1 hit.
SM00211. TY. 10 hits.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF57610. SSF57610. 13 hits.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 9 hits.
PS51162. THYROGLOBULIN_1_2. 11 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P06882-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMTLVLWVST LLSSVCLVAA NIFEYQVDAQ PLRPCELQRE KAFLKQDEYV
60 70 80 90 100
PQCSEDGSFQ TVQCQNDGQS CWCVDSDGTE VPGSRQLGRP TACLSFCQLH
110 120 130 140 150
KQRILLSSYI NSTDALYLPQ CQDSGNYAPV QCDLQQVQCW CVDTEGMEVY
160 170 180 190 200
GTRQQGRPTR CPRSCEIRSR RLLHGVGDKS PPQCDADGEF MPVQCKFVNT
210 220 230 240 250
TDMMIFDLIH NYNRFPDAFV TFSAFRNRFP EVSGYCYCAD SQGRELAETG
260 270 280 290 300
LELLLDEIYD TIFAGLDQAS TFTQSTMYRI LQRRFLAIQL VISGRFRCPT
310 320 330 340 350
KCEVEQFTAT SFGHPYIPSC HRDGHYQTVQ CQMERMCWCV DAQGIEIPGT
360 370 380 390 400
RQQGQPLFCA KDQSCASERQ QALSRLYFET PGYFSPQDLL SSEDRLVPVS
410 420 430 440 450
GARLDISCPP RIKELFVDSG LLRSIAVERY QQLSESRSLL REAIRAIFPS
460 470 480 490 500
RELAGLALQF TTNPKRLQQN LFGGTFLVNA AQLNLSGALG TRSTFNFSQF
510 520 530 540 550
FQQFGLPGFL VRDRATDLAK LLPVSLDSSP TPVPLRVPEK RVAMNKSVVG
560 570 580 590 600
TFGFKVNLQE NQDALKFLVS LMELPEFLVF LQRAVSVPED RARDLGDVME
610 620 630 640 650
MVFSAQACKQ TSGRFFVPSC TAEGSYEDIQ CYAGECWCVN SQGKEVEGSR
660 670 680 690 700
VSGGHPRCPT KCEKQRAQMQ NLAGAQPAGS SFFVPTCTSE GYFLPVQCFN
710 720 730 740 750
SECYCVDAEG QVIPGTQSTI GEPKLCPSVC QLQAEQAFLG VVGVLLSNSS
760 770 780 790 800
MVPPISSVYI PQCSTSGQWM PVQCDGPHEQ VFEWYERWNT QNSDGQELTT
810 820 830 840 850
ATLLMKLMSY REVASTNFSL FLQSLYDAGQ QSIFPVLAQY PSLQDVPQVV
860 870 880 890 900
LEGATIQPGE NIFLDPYIFW QILNGQLSQY PGPYSDFSMP LEHFNLRSCW
910 920 930 940 950
CVDEAGQELD GTRTRAGEIP ACPGPCEEVK FRVLKFIKET EEIVSASNAS
960 970 980 990 1000
SFPLGESFLV AKGIQLTSEE LGLPPLYPSR EAFSEKFLRG SEYAIRLAAQ
1010 1020 1030 1040 1050
STLTFYQKLR ASLGESNGTA SLLWSGPYMP QCNTIGGWEP VQCHPGTGQC
1060 1070 1080 1090 1100
WCVDGWGELI PGSLMARSSQ MPQCPTSCEL SRANGLISAW KQAGHQRNPG
1110 1120 1130 1140 1150
PGDLFTPVCL QTGEYVRQQT SGTGAWCVDP SSGEGVPTNT NSSAQCPGLC
1160 1170 1180 1190 1200
DALKSRVLSR KVGLGYTPVC EALDGGFSPV QCDLAQGSCW CVLASGEEVP
1210 1220 1230 1240 1250
GTRVVGTQPA CESPQCPLPF SGSDVTDGVV FCETASSSGV TTVQQCQLFC
1260 1270 1280 1290 1300
RQGLRNVFSP GPLICNLESQ RWVTLPLPRA CQRPQLWQTM QTQAHFQLLL
1310 1320 1330 1340 1350
PPGKMCSIDY SGLLQAFQVF ILDELITRGF CQIQVKTFGT LVSRTVCDNS
1360 1370 1380 1390 1400
SIQVGCLTAE RLGVNATWKL QLEDISVGSL PNLHSIERAL MGQDLLGRFA
1410 1420 1430 1440 1450
NLIQSGKFQL HLDSKTFSAD TILYFLNGDR FVTSPMTQLG CLEGFYRVST
1460 1470 1480 1490 1500
TSQDPLGCVK CPEGSFSQDG KCTPCPAGTY QGQAGSSACI PCPRGRTTTI
1510 1520 1530 1540 1550
TGAFSKTHCV TDCQRDEAGL QCDQNGQYQA NQKDMDSGEV FCVDSEGQRL
1560 1570 1580 1590 1600
QWLQTEAGLS ESQCLMMRKF EKAPESKVIF DASSPVIVKS RVPSANSPLV
1610 1620 1630 1640 1650
QCLADCADDE ACSFVTVSSM SSEVSCDLYS WTRDNFACVT SDQEEDAVDS
1660 1670 1680 1690 1700
LKETSFGSLR CQVKVRNSGK DSLAVYVKKG HEFTASGQKS FEPTGFQNVL
1710 1720 1730 1740 1750
SGLYSSVVFS ALGTNLTDTH LFCLLACDQD SCCDGFIVTQ VKEGPTICGL
1760 1770 1780 1790 1800
LSAPDILVCH INDWRDASDT QANGTCAGVT YDQGSRQMTM SLGGQEFLQG
1810 1820 1830 1840 1850
LTLLEGTQDS FISFQQVYLW KDSDIGSRPE SMGCGRGMVP KSEAPEGADM
1860 1870 1880 1890 1900
ATELFSPVDI TQVIVNTSHS LPSQQYWLST HLFSAEQANL WCLSRCAQEP
1910 1920 1930 1940 1950
VFCQLADIME SSSLYFTCSL YPEAQVCDND VESNAKNCSQ ILPRQPTALF
1960 1970 1980 1990 2000
QRKVVLNDRV KNFYTRLPFQ KLSGISIRDR IPMSEKLISN GFFECERLCD
2010 2020 2030 2040 2050
RDPCCTGFGF LNVSQMQGGE MTCLTLNSMG IQTCSEENGA TWRILDCGSE
2060 2070 2080 2090 2100
DTEVHTYPFG WYQKPAVWSD APSFCPSAAL QSLTEEKVAL DSWQTLALSS
2110 2120 2130 2140 2150
VIIDPSIKHF DVAHISISAT RNFSLAQDFC LQECSRHQDC LVTTLQIQQG
2160 2170 2180 2190 2200
VVRCVFYPDI QSCEHSLRSK TCWLLLHEEA AYIYRKSGAP LHQSDGISTP
2210 2220 2230 2240 2250
SVHIDSFGQL QGGSQVVKVG TAWKQVYQFL GVPYAAPPLA ENRFQAPEVL
2260 2270 2280 2290 2300
NWTGSWDATK LRSSCWQPGT RTPTPPQISE DCLYLNVFVP ENLVSNASVL
2310 2320 2330 2340 2350
VFFHNTVEME GSGGQLNIDG SILAAVGNLI VVTANYRLGV FGFLSSGSDE
2360 2370 2380 2390 2400
VAGNWGLLDQ VAALTWVQTH IGAFGGDPQR VTLAADRGGA DVASIHLLIT
2410 2420 2430 2440 2450
RPTRLQLFRK ALLMGGSALS PAAIISPDRA QQQAAALAKE VGCPNSSVQE
2460 2470 2480 2490 2500
VVSCFRQKPA NILNEAQTKL LAVSGPFHYW GPVVDGQYLR ELPSRRLKRP
2510 2520 2530 2540 2550
LPVKVDLLIG GSQDDGLINR AKAVKQFEES QGRTNSKTAF YQALQNSLGG
2560 2570 2580 2590 2600
EDSDARILAA AIWYYSLEHS TDDYASFSRA LENATRDYFI ICPIVNMASL
2610 2620 2630 2640 2650
WARRTRGNVF MYHVPESYGH GSLELLADVQ YAFGLPFYSA YQGYFSTEEQ
2660 2670 2680 2690 2700
SLSLKVMQYF SNFIRSGNPN YPHEFSQKAA EFATPWPDFV PGAGGESYKE
2710 2720 2730 2740 2750
LSAQLPNRQG LKKADCSFWS KYIQTLKDAD GAKDAQLTKS GEEDLEVGPG
2760
SEEDFSGSLE PVPKSYSK
Length:2,768
Mass (Da):304,645
Last modified:January 11, 2001 - v4
Checksum:i290DD6943FF23F3D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441L → V in AAA50379 (PubMed:3455768).Curated
Sequence conflicti678 – 6781A → V in AAF34909 (Ref. 2) Curated
Sequence conflicti1492 – 14921C → F in AAF34909 (Ref. 2) Curated
Sequence conflicti1732 – 17332CC → KS in AAF34909 (Ref. 2) Curated
Sequence conflicti1914 – 19141L → F in CAA26183 (PubMed:3838512).Curated
Sequence conflicti2043 – 20431R → A in CAA26183 (PubMed:3838512).Curated
Sequence conflicti2081 – 20811Q → K in CAA26183 (PubMed:3838512).Curated
Sequence conflicti2126 – 21261A → V in CAA26183 (PubMed:3838512).Curated
Sequence conflicti2153 – 21531R → K in CAA26183 (PubMed:3838512).Curated
Sequence conflicti2169 – 21691S → N in CAA26183 (PubMed:3838512).Curated
Sequence conflicti2611 – 26111M → I in CAA26183 (PubMed:3838512).Curated
Sequence conflicti2658 – 26581Q → H in CAA26183 (PubMed:3838512).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2320 – 23201G → R in hypothyroidism; suppress secretion of Tg. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035201 mRNA. Translation: BAA96132.1.
AF221622 mRNA. Translation: AAF34909.1.
M35965 mRNA. Translation: AAA42089.1. Different termination.
M12559, M12558 Genomic DNA. Translation: AAA50379.1.
X02318 mRNA. Translation: CAA26183.1.
PIRiA22016. UIRT.
UniGeneiRn.10429.

Genome annotation databases

UCSCiRGD:3848. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035201 mRNA. Translation: BAA96132.1.
AF221622 mRNA. Translation: AAF34909.1.
M35965 mRNA. Translation: AAA42089.1. Different termination.
M12559, M12558 Genomic DNA. Translation: AAA50379.1.
X02318 mRNA. Translation: CAA26183.1.
PIRiA22016. UIRT.
UniGeneiRn.10429.

3D structure databases

ProteinModelPortaliP06882.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP06882. 3 interactions.
STRINGi10116.ENSRNOP00000009241.

Protein family/group databases

ESTHERiratno-thyro. Thyroglobulin.
MEROPSiS09.978.

Proteomic databases

PaxDbiP06882.
PRIDEiP06882.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:3848. rat.

Organism-specific databases

RGDi3848. Tg.

Phylogenomic databases

eggNOGiENOG410IG6K. Eukaryota.
COG2272. LUCA.
HOGENOMiHOG000128427.
HOVERGENiHBG017929.
InParanoidiP06882.
PhylomeDBiP06882.

Miscellaneous databases

NextBioi604540.
PROiP06882.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
4.10.800.10. 12 hits.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR016324. Thyroglobulin.
IPR000716. Thyroglobulin_1.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
PF07699. Ephrin_rec_like. 1 hit.
PF00086. Thyroglobulin_1. 10 hits.
[Graphical view]
PIRSFiPIRSF001831. Thyroglobulin. 1 hit.
SMARTiSM01411. Ephrin_rec_like. 1 hit.
SM00211. TY. 10 hits.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF57610. SSF57610. 13 hits.
PROSITEiPS00941. CARBOXYLESTERASE_B_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 9 hits.
PS51162. THYROGLOBULIN_1_2. 11 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A novel missense mutation (G2320R) in thyroglobulin causes hypothyroidism in rdw rats."
    Hishinuma A., Furudate S., Oh-Ishi M., Nagakubo N., Namatame T., Ieiri T.
    Endocrinology 141:4050-4055(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HYPOTHYROIDISM ARG-2320.
    Strain: Wistar Imamichi.
  2. "A missense mutation in the thyroglobulin gene causes hypothyroidism and dwarfism not associated with goiter in the WIC-rdw rat."
    Ding M., Jung C.-C., Cheng J.-M., Miyamoto T., Furudate S.I., Agui T.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer 344.
  3. "A second thyroglobulin messenger RNA species (rTg-2) in rat thyrocytes."
    Graves P.N., Davies T.F.
    Mol. Endocrinol. 4:155-161(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-213.
    Strain: Fischer.
    Tissue: Thymocyte.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
  5. "The sequence of 967 amino acids at the carboxyl-end of rat thyroglobulin. Location and surroundings of two thyroxine-forming sites."
    di Lauro R., Obici S., Condliffe D., Ursini V.M., Musti A.M., Moscatelli C., Avvedimento V.E.
    Eur. J. Biochem. 148:7-11(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1802-2768.

Entry informationi

Entry nameiTHYG_RAT
AccessioniPrimary (citable) accession number: P06882
Secondary accession number(s): Q9JKY6, Q9JM94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 11, 2001
Last modified: May 11, 2016
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

It is not certain whether this thyroglobulin plays any role in the formation of triiodothyronine.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.