ID A0A3B3VM33_9TELE Unreviewed; 2212 AA.
AC A0A3B3VM33;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Thyroglobulin {ECO:0000256|ARBA:ARBA00017326};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000025899.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000025899.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Ensembl; ENSPLAT00000028784.1; ENSPLAP00000025899.1; ENSPLAG00000016323.1.
DR GeneTree; ENSGT00940000168460; -.
DR Proteomes; UP000261500; Unplaced.
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; 5.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 6.
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; 5.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00211; TY; 7.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 6.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 3.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 6.
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 Sulfation {ECO:0000256|ARBA:ARBA00022641};
KW Thyroid hormone {ECO:0000256|ARBA:ARBA00022920};
KW Thyroid hormones biosynthesis {ECO:0000256|ARBA:ARBA00022534}.
FT DOMAIN 37..87
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 88..186
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 227..287
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 482..538
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 539..604
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 795..846
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT REGION 302..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1992..2018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 67..87
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 267..287
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
FT DISULFID 518..538
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 2212 AA; 242273 MW; 76F3B77B03702B8F CRC64;
EALSRCEILR SVAVGTKQEE VPHCLEDGSF SCPVPGPTPC QLQSLLQCAP SGLFEPVQCD
SRGRCWCVDQ DGMELYGTRQ ASIPRRCPSS CEVRSRRLLH SSASSPPQCA ADGSFLPVQC
KFINTTDRTE LDLVKCSALC SSSPEAFETF RNFRKFFPLV SSYCFCSDSR GRELQGTGVE
LLMSEVYDSA FSGPRSAHSF AQTNIYRVLQ RRMLGVRLAL SGHFRCPSPC EEERRAALES
SSVFVPSCEA DGRFSAKQCQ QGALCWCVDP TGRELTGTRR PGDGLVCGED ELHHLVGCCS
RSKRRTDSPL TPPPGSGPAD CPAQRRLALS QLFSGLVRPP QASSGSATLC LSLLRPLRVL
GYSDPTSFLS RLVEVLQGLF PSVGGALEAL TRSPAQRLQE NLFGGKFLQN VAAFNYTGVL
GPRGAVGVDQ LSAQSLQENR DLVRAVSRAL EDPAFLSALR QTLMVLSGAP SGSLQQVLAG
VLRSCSEEED DSSSLFVPRC SLSGGYQPVQ CRDAECWCVN LQGQEAPGSR TAGWPPRCPT
SCEMARANAM KVKSNMAAGA EIHIPACSED GDFLPLQCVG DRCFCVDAEG RKMAAGPTGG
AVTCEFLLHQ NVSDISFTFD LSGRCSKALA EVTAFRQEVD SLVFLSNSTH LPVGYGFLLA
KGLSLSQSEE ELQLSQSEEL KVSERLLSRS RSALRLAASS SELQRHKLQE FNLKYQMYLQ
ITLQKCWCVD EEGEFIPGSL RRSLRLPRCR SRCQRAEAHS LLSDWMKASD ITTASPYHPQ
CEQGGSVNSV LPSGPSWCEL QRLRCRPDGS FDPLQCDVTS CWCVSEDGQE MAGTRSLRQT
GRTPSCDRPL CPAPNITHGA LVCHPAADGR QSCDLVCHHG YQNSLPVSSF LCSIKSRQWD
EGDKPLSGAC QSESVRFYFV LFIFLLPSGR SVALCGDSAV GLWCDAGDSV RLTLRWTADL
SDLTTSDLPH LHHMGEYSLN RDSNFMRRFV PAGLRPAQAH GSIVSFPVVC PAGSFYQQGV
CLLCPQGTYQ ELEGRDFCTR CPRGSSPAGA SAANQCETDC ERRGLRCSQS GDFLLAQPNF
LSGGWRCVSN EGVELEWTSR EERLTDEECS GEDQFGPGSG LGCERPVFVS ACAVEPSCHH
VALFDRRTRC DLYSSLNAVC SASQQVSRLR VKGQPFRARI LLQLCVFLQA TGFLGNPRAE
RFHQLRCSLR VRGGASDLFV LRKNGAELQH QSFVRMRMRK AVSGVFRTQV FSSRNTSLSD
VRRFCQDGCS RDACCHGFIL NQNVLDGGSL LCGWLRAPSV LMCEDEDWDV IGQGPANRIC
GAGLSYSKQQ RSFEFDFGGE KFTISKKATQ LGLTSPVQTQ TECSGSVQLT ALCLATAETG
RTTRPPSSTL VLSAATVQLR FQSLSSAEVL VDPQRKQPVL SFWLSKNDYS SQNALLWCLT
RMQLSVLTDS DRFFRCALYP DTRVCGGYDQ PIRRSCRPLL DRATNNTYSK KVDLSGPVQS
FYERVPFQKM VSYSVRNRPS SMFSSRAVSV SRFRECERRC DEDPCCRGFG FVHETKSRGL
LCLPLISLGV LTCSEDDAST WRTQDCSPPE AETSPEPFGW YQKPGTRLTQ TRYSTVSVCV
RPESVSVFMD DWRLLSESSL LIDASLSTYD VIHVSRDIDT DRERTRDWCL HADEPITEQN
RAWQLTDPNV FLERSPQAAS ISVPGHGTLQ GVAMETAVGS DRRTVIRFLG VPYARPPIGV
LRFEAAQLAD WTGTWDATNL NHQNLGVRTI SDPPVPSSED CLYLNIFTPA VQVIPVLVYF
FNPPANQNQN LLDGSALAAL GNIVVVTASY RTAALGFLTA GGLHGNYGLS DQEAALRWVH
AHISLVGGDS GSVTVGAERR GADISSLTLL SSSPPFHRMI LMGGSVFSPS LVQTASAGRR
QAVDLARELG CVTSDLSDDG PMVACLRSTP VHKLNAAQTK VRVLRSRQFC PAGGQRSVPG
LGSGPQVRVR VLPQSGPDAG HIRTRRPDQQ STQDKGQRSL KTAFYEALSR SLGGASGNAL
LKDAAAWFYS LDHDPSAAGY NLFSRALNNA TRDLFIICPT VQMALHWAAS GTNIFQYHQP
ASTDVLVPLD VQFLFGIPLQ PMNSQRFTSS DRRLSLAVMT YASSFIRTGN PNPSHVWAES
VLPRWQPVTA EAPPTYLELS PALQHQQGLR QNACSFWREL GTRLTSKTGR FC
//