Search by BoMiProt ID - Bomi9832


Primary Information

BoMiProt ID Bomi9832
Protein Name Thyroglobulin
Organism Bos taurus
Uniprot IDP01267
Milk FractionWhey
Ref Sequence ID https://www.ncbi.nlm.nih.gov/gene/280706
Aminoacid Length 2769
Molecular Weight 303222
FASTA Sequence Download
Gene Name TG
Gene ID 280706
Protein Existence Status reviewed

Secondary Information

Protein Function Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3)
Biochemical Properties A 660 kDa (2 × 330 kDa) homodimeric protein.Contain Th1 domain-Tg1 repeat contains a characteristic CWCV (Cys–Trp–Cys–Val) sequence motif.The Tg1 cluster is followed by a hinge domain that connects the Tg1 domain to two Tg type 2 (Tg2) repeats spanning from Cys1442 to Cys1513. After the Tg2 region, the Tg type 3 (Tg3) repeat domain forms the arm region of the Tg molecule at one end of a Tg monomer.After the Tg3 domain, the ChEL domain in the C-terminus provides Tg with structural stability and integrity. In our Tg structure, the ChEL domain contains a thyroxinated tyrosine at Tyr2575 and an apparent dehydroalanine at Tyr2542 in close proximity (∼7 Å apart), which suggests that the two form an acceptor–donor pair that couple to synthesize T4 at Tyr2575 .
Significance in milk Genetic variation in TG has been associated with back fat thickness and marbling in beef cattle as well as milk traits in dairy cattle.Associated with milk and meat quality.Thyroglobulin acts as a carrier for both T3 and T4,stored in thyroid gland.T3 and T4 play an important role in regulating the metabolism and can affect adipocyte growth, differentiation, and homeostasis of fat depots.
PTMs Disulfide bond formation, Glycosylation, Iodination, Sulfation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|P01267|THYG_BOVIN Thyroglobulin OS=Bos taurus OX=9913 GN=TG PE=1 SV=1 MALALWVFGLLDLICLASANIFEYQVDAQPLRPCELQRERAFLKREDYVPQCAEDGSFQT VQCGKDGASCWCVDADGREVPGSRQPGRPAACLSFCQLQKQQILLSSYIN*110STATSYLPQC QDSGDYSPVQCDLRRRQCWCVDAEGMEVYGTRQQGRPARCPRSCEIRNRRLLHGVGDRSP PQCSPDGAFRPVQCKLVNTTDMMIFDLVHSYSRFPDAFVTFSSFRSRFPEVSGYCYCADS QGRELAETGLELLLDEIYDTIFAGLDLASTFAETTLYRILQRRFLAVQLVISGRFRCPTK CEVERFAATSFRHPYVPSCHPDGEYQAAQCQQGGPCWCVDSRGQEIPGTRQRGEPPSCAE DQSCPSERRRAFSRLRFGPSGYFSRRSLLLAPEEGPVSQRFARFTASCPPSIKELFLDSG IFQPMLQGRDTRFVAPESLKEAIRGLFPSRELARLALQFTTNAKRLQQNLFGGRFLVKVG QFN*483LSGALGTRGTFNFSHFFQQLGLPGFQDGRALADLAKPLSVGLNSNPASEAPKASKID VALRKPVVGSFGFEVNLQENQNALQFLSSFLELPEFLLFLQHAISVPEDIARDLGDVMEM VFSSQGCGQAPGSLFVPACTAEGSYEEVQCFAGDCWCVDAQGRELAGSRVRGGRPRCPTE CEKQRARMQSLLGSQPAGSSLFVPACTSKGNFLPVQCFNSECYCVDTEGQPIPGTRSALG EPKKCPSPCQLQAERAFLGTVRTLVSNPSTLPALSSIYIPQCSASGQWSPVQCDGPPEQA FEWYERWEAQNSAGQALTPAELLMKIMSYREAASRNFRLFIQNLYEAGQQGIFPGLARYS SFQDVPVSVLEGN*853QTQPGGNVFLEPYLFWQILNGQLDRYPGPYSDFSAPLAHFDLRSCWC VDEAGQKLEGTRNEPNKVPACPGSCEEVKLRVLQFIREAEEIVTYSN*947SSRFPLGESFLAA KGIRLTDEELAFPPLSPSRETFLEKFLSGSDYAIRLAAQSTFDFYQRRLVTLAESPRAPS PVWSSAYLPQCDAFGGWEPVQCHAATGHCWCVDGKGEYVPTSLTARSRQIPQCPTSCERL RASGLLSSWKQAGVQAEPSPKDLFIPTCLETGEFARLQASEAGTWCVDPASGEGVPPGTN*1140 SSAQCPSLCEVLQSGVPSRRTSPGYSPACRAEDGGFSPVQCDPAQGSCWCVLGSGEEVPG TRVAGSQPACESPQCPLPFSVADVAGGAILCERASGLGAAAGQRCQLRCSQGYRSAFPPE PLLCSVQRRRWESRPPQPRACQRPQFWQTLQTQAQFQLLLPLGKVCSADYSGLLLAFQVF LLDELTARGFCQIQVKTAGTPVSIPVCDDSSVKVECLSRERLGVN*1365ITWKLQLVDAPPASL PDLQDVEEALAGKYLAGRFADLIQSGTFQLHLDSKTFSADTSIRFLQGDRFGTSPRTQFG CLEGFGRVVAASDASQDALGCVKCPEGSYFQDEQCIPCPAGFYQEQAGSLACVPCPEGRT TVYAGAFSQTHCVTDCQKNEVGLQCDQDSQYRASQRDRTSGKAFCVDGEGRRLPWTEAEA PLVDAQCLVMRKFEKLPESKVIFSADVAVMVRSEVPGSESSLMQCLADCALDEACGFLTV STAGSEVSCDFYAWASDSIACTTSGRSEDALGTSQATSFGSLQCQVKVRSREGDPLAVYL KKGQEFTITGQKRFEQTGFQSALSGMYSPVTFSASGASLAEVHLFCLLACDHDSCCDGFI LVQVQGGPLLCGLLSSPDVLLCHVRDWRDPAEAQAN*1776ASCPGVTYDQDSRQVTLRLGGQEI RGLTPLEGTQDTLTSFQQVYLWKDSDMGSRSESMGCRRDTEPRPASPSETDLTTGLFSPV DLIQVIVDGN*1870VSLPSQQHWLFKHLFSLQQANLWCLSRCAGEPSFCQLAEVTDSEPLYFTC TLYPEAQVCDDILESSPKGCRLILPRRPSALYRKKVVLQDRVKNFYNRLPFQKLTGISIR NKVPMSDKSISSGFFECERLCDMDPCCTGFGFLN*2014VSQLKGGEVTCLTLNSLGLQTCSEEY GGVWRILDCGSPDTEVRTYPFGWYQKPVSPSDAPSFCPSVALPALTENVALDSWQSLALS SVIVDPSIRNFDVAHISTAAVGN*2123FSAARDRCLWECSRHQDCLVTTLQTQPGAVRCMFYAD TQSCTHSLQAQNCRLLLHEEATYIYRKPNIPLPGFGTSSPSVPIATHGQLLGRSQAIQVG TSWKPVDQFLGVPYAAPPLGEKRFRAPEHLN*2251WTGSWEATKPRARCWQPGIRTPTPPGVSE DCLYLNVFVPQNMAPNASVLVFFHNAAEGKGSGDRPAVDGSFLAAVGNLIVVTASYRTGI FGFLSSGSSELSGNWGLLDQVVALTWVQTHIQAFGGDPRRVTLAADRGGADIASIHLVTT RAANSRLFRRAVLMGGSALSPAAVIRPERARQQAAALAKEVGCPSSSVQEMVSCLRQEPA RILNDAQTKLLAVSGPFHYWGPVVDGQYLRETPARVLQRAPRVKVDLLIGSSQDDGLINR AKAVKQFEESQGRTSSKTAFYQALQNSLGGEAADAGVQAAATWYYSLEHDSDDYASFSRA LEQATRDYFIICPVIDMASHWARTVRGNVFMYHAPESYSHSSLELLTDVLYAFGLPFYPA YEGQFTLEEKSLSLKIMQYFSNFIRSGNPNYPHEFSRRAPEFAAPWPDFVPRDGAESYKE LSVLLPNRQGLKKADCSFWSKYIQSLKASADETKDGPSADSEEEDQPAGSGLTEDLLGLP ELASKTYSK
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Undergoes sequential proteolysis by cathepsins to release thyroxine (T4) and triiodothyronine (T3) hormones.Iodinated on tyrosine residues by TPO.Iodinated on tyrosine residues by TPO (By similarity). There are 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-24 is coupled to donor Tyr-149 or Tyr-234, acceptor Tyr-2574 is coupled to donor Tyr-2541, acceptor Tyr-2767 in monomer 1 is coupled to donor Tyr-2767 in monomer 2 and acceptor Tyr-1310 in monomer 1 is coupled to donor Tyr-108 in monomer 2 .
Bibliography Kim, K., Kopylov, M., Bobe, D., Kelley, K., Eng, E. T., Arvan, P., & Clarke, O. B. (2021). The structure of natively iodinated bovine thyroglobulin. Acta crystallographica. Section D, Structural biology, 77(Pt 11), 1451–1459. https://doi.org/10.1107/S2059798321010056