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P06882 (THYG_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thyroglobulin

Short name=Tg
Gene names
Name:Tg
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length2768 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Homodimer.

Subcellular location

Secreted.

Tissue specificity

Thyroid gland specific.

Post-translational modification

Sulfated tyrosines are desulfated during iodination By similarity.

Involvement in disease

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

Miscellaneous

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

Sequence similarities

Belongs to the type-B carboxylesterase/lipase family.

Contains 11 thyroglobulin type-1 domains.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 27682748Thyroglobulin
PRO_0000008638

Regions

Domain32 – 9362Thyroglobulin type-1 1
Domain94 – 16168Thyroglobulin type-1 2
Domain162 – 298137Thyroglobulin type-1 3
Domain299 – 35961Thyroglobulin type-1 4
Domain605 – 65854Thyroglobulin type-1 5
Domain659 – 72668Thyroglobulin type-1 6
Domain727 – 922196Thyroglobulin type-1 7
Domain923 – 1074152Thyroglobulin type-1 8
Domain1075 – 114672Thyroglobulin type-1 9
Domain1147 – 121165Thyroglobulin type-1 10
Repeat1455 – 146814Type II
Repeat1469 – 148517Type II
Repeat1486 – 150217Type II
Domain1510 – 156455Thyroglobulin type-1 11
Repeat1602 – 1722121Type IIIA
Repeat1723 – 1891169Type IIIB
Repeat1892 – 1994103Type IIIA
Repeat1995 – 2127133Type IIIB
Repeat2128 – 218558Type IIIA

Amino acid modifications

Modified residue251Sulfotyrosine; alternate By similarity
Modified residue251Thyroxine; alternate By similarity
Modified residue25741Thyroxine By similarity
Modified residue25881Thyroxine By similarity
Modified residue27661Triiodothyronine By similarity
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1991N-linked (GlcNAc...) Potential
Glycosylation4841N-linked (GlcNAc...) Potential
Glycosylation4961N-linked (GlcNAc...) Potential
Glycosylation5451N-linked (GlcNAc...) Potential
Glycosylation7481N-linked (GlcNAc...) Potential
Glycosylation8171N-linked (GlcNAc...) Potential
Glycosylation9481N-linked (GlcNAc...) Potential
Glycosylation10171N-linked (GlcNAc...) Potential
Glycosylation11411N-linked (GlcNAc...) Potential
Glycosylation13491N-linked (GlcNAc...) Potential
Glycosylation13651N-linked (GlcNAc...) Potential
Glycosylation17151N-linked (GlcNAc...) Potential
Glycosylation17731N-linked (GlcNAc...) Potential
Glycosylation18661N-linked (GlcNAc...) Potential
Glycosylation19371N-linked (GlcNAc...) Potential
Glycosylation20121N-linked (GlcNAc...) Potential
Glycosylation21221N-linked (GlcNAc...) Potential
Glycosylation22511N-linked (GlcNAc...) Potential
Glycosylation22961N-linked (GlcNAc...) Potential
Glycosylation24451N-linked (GlcNAc...) Potential
Glycosylation25831N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 53 By similarity
Disulfide bond64 ↔ 71 By similarity
Disulfide bond73 ↔ 93 By similarity
Disulfide bond97 ↔ 121 By similarity
Disulfide bond132 ↔ 139 By similarity
Disulfide bond141 ↔ 161 By similarity
Disulfide bond165 ↔ 184 By similarity
Disulfide bond195 ↔ 236 By similarity
Disulfide bond302 ↔ 320 By similarity
Disulfide bond331 ↔ 337 By similarity
Disulfide bond339 ↔ 365 By similarity
Disulfide bond608 ↔ 620 By similarity
Disulfide bond631 ↔ 636 By similarity
Disulfide bond638 ↔ 658 By similarity
Disulfide bond662 ↔ 687 By similarity
Disulfide bond698 ↔ 703 By similarity
Disulfide bond705 ↔ 726 By similarity
Disulfide bond730 ↔ 763 By similarity
Disulfide bond774 ↔ 899 By similarity
Disulfide bond901 ↔ 922 By similarity
Disulfide bond1043 ↔ 1050 By similarity
Disulfide bond1052 ↔ 1074 By similarity
Disulfide bond1078 ↔ 1109 By similarity
Disulfide bond1127 ↔ 1146 By similarity
Disulfide bond1150 ↔ 1170 By similarity
Disulfide bond1182 ↔ 1189 By similarity
Disulfide bond1191 ↔ 1211 By similarity
Disulfide bond1513 ↔ 1522 By similarity
Disulfide bond1542 ↔ 1564 By similarity
Disulfide bond2265 ↔ 2282 Potential

Natural variations

Natural variant23201G → R in hypothyroidism; suppress secretion of Tg. Ref.1

Experimental info

Sequence conflict441L → V in AAA50379. Ref.4
Sequence conflict6781A → V in AAF34909. Ref.2
Sequence conflict14921C → F in AAF34909. Ref.2
Sequence conflict1732 – 17332CC → KS in AAF34909. Ref.2
Sequence conflict19141L → F in CAA26183. Ref.5
Sequence conflict20431R → A in CAA26183. Ref.5
Sequence conflict20811Q → K in CAA26183. Ref.5
Sequence conflict21261A → V in CAA26183. Ref.5
Sequence conflict21531R → K in CAA26183. Ref.5
Sequence conflict21691S → N in CAA26183. Ref.5
Sequence conflict26111M → I in CAA26183. Ref.5
Sequence conflict26581Q → H in CAA26183. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P06882 [UniParc].

Last modified January 11, 2001. Version 4.
Checksum: 290DD6943FF23F3D

FASTA2,768304,645
        10         20         30         40         50         60 
MMTLVLWVST LLSSVCLVAA NIFEYQVDAQ PLRPCELQRE KAFLKQDEYV PQCSEDGSFQ 

        70         80         90        100        110        120 
TVQCQNDGQS CWCVDSDGTE VPGSRQLGRP TACLSFCQLH KQRILLSSYI NSTDALYLPQ 

       130        140        150        160        170        180 
CQDSGNYAPV QCDLQQVQCW CVDTEGMEVY GTRQQGRPTR CPRSCEIRSR RLLHGVGDKS 

       190        200        210        220        230        240 
PPQCDADGEF MPVQCKFVNT TDMMIFDLIH NYNRFPDAFV TFSAFRNRFP EVSGYCYCAD 

       250        260        270        280        290        300 
SQGRELAETG LELLLDEIYD TIFAGLDQAS TFTQSTMYRI LQRRFLAIQL VISGRFRCPT 

       310        320        330        340        350        360 
KCEVEQFTAT SFGHPYIPSC HRDGHYQTVQ CQMERMCWCV DAQGIEIPGT RQQGQPLFCA 

       370        380        390        400        410        420 
KDQSCASERQ QALSRLYFET PGYFSPQDLL SSEDRLVPVS GARLDISCPP RIKELFVDSG 

       430        440        450        460        470        480 
LLRSIAVERY QQLSESRSLL REAIRAIFPS RELAGLALQF TTNPKRLQQN LFGGTFLVNA 

       490        500        510        520        530        540 
AQLNLSGALG TRSTFNFSQF FQQFGLPGFL VRDRATDLAK LLPVSLDSSP TPVPLRVPEK 

       550        560        570        580        590        600 
RVAMNKSVVG TFGFKVNLQE NQDALKFLVS LMELPEFLVF LQRAVSVPED RARDLGDVME 

       610        620        630        640        650        660 
MVFSAQACKQ TSGRFFVPSC TAEGSYEDIQ CYAGECWCVN SQGKEVEGSR VSGGHPRCPT 

       670        680        690        700        710        720 
KCEKQRAQMQ NLAGAQPAGS SFFVPTCTSE GYFLPVQCFN SECYCVDAEG QVIPGTQSTI 

       730        740        750        760        770        780 
GEPKLCPSVC QLQAEQAFLG VVGVLLSNSS MVPPISSVYI PQCSTSGQWM PVQCDGPHEQ 

       790        800        810        820        830        840 
VFEWYERWNT QNSDGQELTT ATLLMKLMSY REVASTNFSL FLQSLYDAGQ QSIFPVLAQY 

       850        860        870        880        890        900 
PSLQDVPQVV LEGATIQPGE NIFLDPYIFW QILNGQLSQY PGPYSDFSMP LEHFNLRSCW 

       910        920        930        940        950        960 
CVDEAGQELD GTRTRAGEIP ACPGPCEEVK FRVLKFIKET EEIVSASNAS SFPLGESFLV 

       970        980        990       1000       1010       1020 
AKGIQLTSEE LGLPPLYPSR EAFSEKFLRG SEYAIRLAAQ STLTFYQKLR ASLGESNGTA 

      1030       1040       1050       1060       1070       1080 
SLLWSGPYMP QCNTIGGWEP VQCHPGTGQC WCVDGWGELI PGSLMARSSQ MPQCPTSCEL 

      1090       1100       1110       1120       1130       1140 
SRANGLISAW KQAGHQRNPG PGDLFTPVCL QTGEYVRQQT SGTGAWCVDP SSGEGVPTNT 

      1150       1160       1170       1180       1190       1200 
NSSAQCPGLC DALKSRVLSR KVGLGYTPVC EALDGGFSPV QCDLAQGSCW CVLASGEEVP 

      1210       1220       1230       1240       1250       1260 
GTRVVGTQPA CESPQCPLPF SGSDVTDGVV FCETASSSGV TTVQQCQLFC RQGLRNVFSP 

      1270       1280       1290       1300       1310       1320 
GPLICNLESQ RWVTLPLPRA CQRPQLWQTM QTQAHFQLLL PPGKMCSIDY SGLLQAFQVF 

      1330       1340       1350       1360       1370       1380 
ILDELITRGF CQIQVKTFGT LVSRTVCDNS SIQVGCLTAE RLGVNATWKL QLEDISVGSL 

      1390       1400       1410       1420       1430       1440 
PNLHSIERAL MGQDLLGRFA NLIQSGKFQL HLDSKTFSAD TILYFLNGDR FVTSPMTQLG 

      1450       1460       1470       1480       1490       1500 
CLEGFYRVST TSQDPLGCVK CPEGSFSQDG KCTPCPAGTY QGQAGSSACI PCPRGRTTTI 

      1510       1520       1530       1540       1550       1560 
TGAFSKTHCV TDCQRDEAGL QCDQNGQYQA NQKDMDSGEV FCVDSEGQRL QWLQTEAGLS 

      1570       1580       1590       1600       1610       1620 
ESQCLMMRKF EKAPESKVIF DASSPVIVKS RVPSANSPLV QCLADCADDE ACSFVTVSSM 

      1630       1640       1650       1660       1670       1680 
SSEVSCDLYS WTRDNFACVT SDQEEDAVDS LKETSFGSLR CQVKVRNSGK DSLAVYVKKG 

      1690       1700       1710       1720       1730       1740 
HEFTASGQKS FEPTGFQNVL SGLYSSVVFS ALGTNLTDTH LFCLLACDQD SCCDGFIVTQ 

      1750       1760       1770       1780       1790       1800 
VKEGPTICGL LSAPDILVCH INDWRDASDT QANGTCAGVT YDQGSRQMTM SLGGQEFLQG 

      1810       1820       1830       1840       1850       1860 
LTLLEGTQDS FISFQQVYLW KDSDIGSRPE SMGCGRGMVP KSEAPEGADM ATELFSPVDI 

      1870       1880       1890       1900       1910       1920 
TQVIVNTSHS LPSQQYWLST HLFSAEQANL WCLSRCAQEP VFCQLADIME SSSLYFTCSL 

      1930       1940       1950       1960       1970       1980 
YPEAQVCDND VESNAKNCSQ ILPRQPTALF QRKVVLNDRV KNFYTRLPFQ KLSGISIRDR 

      1990       2000       2010       2020       2030       2040 
IPMSEKLISN GFFECERLCD RDPCCTGFGF LNVSQMQGGE MTCLTLNSMG IQTCSEENGA 

      2050       2060       2070       2080       2090       2100 
TWRILDCGSE DTEVHTYPFG WYQKPAVWSD APSFCPSAAL QSLTEEKVAL DSWQTLALSS 

      2110       2120       2130       2140       2150       2160 
VIIDPSIKHF DVAHISISAT RNFSLAQDFC LQECSRHQDC LVTTLQIQQG VVRCVFYPDI 

      2170       2180       2190       2200       2210       2220 
QSCEHSLRSK TCWLLLHEEA AYIYRKSGAP LHQSDGISTP SVHIDSFGQL QGGSQVVKVG 

      2230       2240       2250       2260       2270       2280 
TAWKQVYQFL GVPYAAPPLA ENRFQAPEVL NWTGSWDATK LRSSCWQPGT RTPTPPQISE 

      2290       2300       2310       2320       2330       2340 
DCLYLNVFVP ENLVSNASVL VFFHNTVEME GSGGQLNIDG SILAAVGNLI VVTANYRLGV 

      2350       2360       2370       2380       2390       2400 
FGFLSSGSDE VAGNWGLLDQ VAALTWVQTH IGAFGGDPQR VTLAADRGGA DVASIHLLIT 

      2410       2420       2430       2440       2450       2460 
RPTRLQLFRK ALLMGGSALS PAAIISPDRA QQQAAALAKE VGCPNSSVQE VVSCFRQKPA 

      2470       2480       2490       2500       2510       2520 
NILNEAQTKL LAVSGPFHYW GPVVDGQYLR ELPSRRLKRP LPVKVDLLIG GSQDDGLINR 

      2530       2540       2550       2560       2570       2580 
AKAVKQFEES QGRTNSKTAF YQALQNSLGG EDSDARILAA AIWYYSLEHS TDDYASFSRA 

      2590       2600       2610       2620       2630       2640 
LENATRDYFI ICPIVNMASL WARRTRGNVF MYHVPESYGH GSLELLADVQ YAFGLPFYSA 

      2650       2660       2670       2680       2690       2700 
YQGYFSTEEQ SLSLKVMQYF SNFIRSGNPN YPHEFSQKAA EFATPWPDFV PGAGGESYKE 

      2710       2720       2730       2740       2750       2760 
LSAQLPNRQG LKKADCSFWS KYIQTLKDAD GAKDAQLTKS GEEDLEVGPG SEEDFSGSLE 


PVPKSYSK 

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References

[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]"The complete structure of the rat thyroglobulin gene."
Musti A.M., Avvedimento V.E., Polistina C., Ursini V.M., Obici S., Nitsch L., Cocozza S., di Lauro R.
Proc. Natl. Acad. Sci. U.S.A. 83:323-327(1986) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRUIRT. A22016.
UniGeneRn.10429.

3D structure databases

ProteinModelPortalP06882.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246946. 4 interactions.
IntActP06882. 3 interactions.

Protein family/group databases

MEROPSS09.978.

Proteomic databases

PaxDbP06882.
PRIDEP06882.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:3848. rat.

Organism-specific databases

RGD3848. Tg.

Phylogenomic databases

eggNOGCOG2272.
HOGENOMHOG000128427.
HOVERGENHBG017929.
InParanoidP06882.
PhylomeDBP06882.

Gene expression databases

GenevestigatorP06882.

Family and domain databases

Gene3D4.10.800.10. 12 hits.
InterProIPR002018. CarbesteraseB.
IPR019819. Carboxylesterase_B_CS.
IPR016324. Thyroglobulin.
IPR000716. Thyroglobulin_1.
IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
[Graphical view]
PfamPF00135. COesterase. 1 hit.
PF07699. GCC2_GCC3. 1 hit.
PF00086. Thyroglobulin_1. 8 hits.
[Graphical view]
PIRSFPIRSF001831. Thyroglobulin. 1 hit.
SMARTSM00211. TY. 10 hits.
[Graphical view]
SUPFAMSSF57610. SSF57610. 13 hits.
PROSITEPS00941. CARBOXYLESTERASE_B_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 9 hits.
PS51162. THYROGLOBULIN_1_2. 11 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio604540.
PROP06882.

Entry information

Entry nameTHYG_RAT
AccessionPrimary (citable) accession number: P06882
Secondary accession number(s): Q9JKY6, Q9JM94
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 11, 2001
Last modified: April 16, 2014
This is version 127 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families