THYG_PIG
ID THYG_PIG Reviewed; 2692 AA.
AC F1RRV3; D1KKB3;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 5.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Thyroglobulin {ECO:0000305};
DE Flags: Precursor;
GN Name=TG {ECO:0000312|EMBL:AEMK02000022};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000312|Proteomes:UP000008227};
RN [1] {ECO:0000312|EMBL:ACY66900.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang Y., Zhao X., Xu N.;
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000312|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 20-26, SULFATION AT TYR-24, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12387814; DOI=10.1016/s0006-291x(02)02425-7;
RA Venot N., Nlend M.-C., Cauvi D., Chabaud O.;
RT "The hormonogenic tyrosine 5 of porcine thyroglobulin is sulfated.";
RL Biochem. Biophys. Res. Commun. 298:193-197(2002).
RN [4] {ECO:0000305}
RP IODINATION.
RX PubMed=12325367; DOI=10.1016/s0021-9258(18)99388-9;
RA Coval M.L., Taurog A.;
RT "Purification and iodinating activity of hog thyroid peroxidase.";
RL J. Biol. Chem. 242:5510-5523(1967).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=7021557; DOI=10.1016/s0021-9258(19)52523-6;
RA Gavaret J.M., Cahnmann H.J., Nunez J.;
RT "Thyroid hormone synthesis in thyroglobulin. The mechanism of the coupling
RT reaction.";
RL J. Biol. Chem. 256:9167-9173(1981).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY, AND PROTEOLYTIC CLEAVAGE.
RC TISSUE=Thyroid;
RX PubMed=11082042; DOI=10.1242/jcs.113.24.4487;
RA Tepel C., Broemme D., Herzog V., Brix K.;
RT "Cathepsin K in thyroid epithelial cells: sequence, localization and
RT possible function in extracellular proteolysis of thyroglobulin.";
RL J. Cell Sci. 113:4487-4498(2000).
CC -!- FUNCTION: Acts as a substrate for the production of iodinated thyroid
CC hormones thyroxine (T4) and triiodothyronine (T3) (PubMed:7021557). The
CC synthesis of T3 and T4 involves iodination of selected tyrosine
CC residues of TG/thyroglobulin followed by their oxidative coupling
CC (PubMed:7021557). Following TG re-internalization and lysosomal-
CC mediated proteolysis, T3 and T4 are released from the polypeptide
CC backbone leading to their secretion into the bloodstream (By
CC similarity). One dimer produces 7 thyroid hormone molecules (By
CC similarity). {ECO:0000250|UniProtKB:O08710,
CC ECO:0000250|UniProtKB:P01266, ECO:0000269|PubMed:7021557}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer (via ChEL region); occurs
CC in the endoplasmic reticulum and is required for export to the Golgi
CC apparatus (By similarity). Homooligomer; disulfide-linked; stored in
CC this form in the thyroid follicle lumen (By similarity).
CC {ECO:0000250|UniProtKB:O08710, ECO:0000250|UniProtKB:P01266}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12387814}.
CC Note=Secreted into the follicular lumina of the thyroid
CC (PubMed:12387814). Localizes to colloid globules, a structure formed in
CC the thyroid follicle lumen consisting of cross-linked TG arranged in
CC concentric layers (By similarity). {ECO:0000250|UniProtKB:P01266,
CC ECO:0000269|PubMed:12387814}.
CC -!- TISSUE SPECIFICITY: Expressed in thyroid epithelial cells.
CC {ECO:0000269|PubMed:12387814}.
CC -!- DOMAIN: The cholinesterase-like (ChEL) region is required for
CC dimerization and export from the endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:O08710}.
CC -!- PTM: Iodinated on tyrosine residues by TPO (PubMed:12325367). There are
CC 4 pairs of iodinated tyrosines used for coupling: acceptor Tyr-24 is
CC coupled to donor Tyr-149 or Tyr-234, acceptor Tyr-2500 is coupled to
CC donor Tyr-2467, acceptor Tyr-2690 in monomer 1 is coupled to donor Tyr-
CC 2690 in monomer 2 and acceptor Tyr-1241 in monomer 1 is coupled to
CC donor Tyr-108 in monomer 2 (By similarity).
CC {ECO:0000250|UniProtKB:P01266, ECO:0000269|PubMed:12325367}.
CC -!- PTM: Sulfated tyrosines are desulfated during iodination.
CC {ECO:0000250|UniProtKB:P01266}.
CC -!- PTM: Undergoes sequential proteolysis by cathepsins to release
CC thyroxine (T4) and triiodothyronine (T3) hormones (By similarity). In
CC the thyroid follicle lumen, cross-linked TG (storage form) is
CC solubilized by limited proteolysis mediated by cathepsins CTSB and/or
CC CTSL (By similarity). Partially cleaved TG is further processed by
CC CTSK/cathepsin K and/or CTSL resulting in the release of T4
CC (PubMed:11082042). Following endocytosis, further processing occurs
CC leading to the release of T3 and more T4 hormones (By similarity).
CC {ECO:0000250|UniProtKB:O08710, ECO:0000269|PubMed:11082042}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
CC -!- CAUTION: The cholinesterase-like (ChEL) region lacks the Ser residue of
CC the catalytic triad suggesting that it has no esterase activity.
CC {ECO:0000305}.
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DR EMBL; GQ261999; ACY66900.1; -; mRNA.
DR EMBL; AEMK02000022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001161890.1; NM_001168418.1.
DR AlphaFoldDB; F1RRV3; -.
DR SMR; F1RRV3; -.
DR STRING; 9823.ENSSSCP00000006358; -.
DR ESTHER; pig-d1kkb3; Thyroglobulin.
DR MEROPS; S09.978; -.
DR PaxDb; F1RRV3; -.
DR PeptideAtlas; F1RRV3; -.
DR PRIDE; F1RRV3; -.
DR GeneID; 100156471; -.
DR KEGG; ssc:100156471; -.
DR CTD; 7038; -.
DR eggNOG; KOG1214; Eukaryota.
DR InParanoid; F1RRV3; -.
DR OMA; SGPYVPQ; -.
DR OrthoDB; 754103at2759; -.
DR TreeFam; TF351833; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006590; P:thyroid hormone generation; IDA:UniProtKB.
DR CDD; cd00191; TY; 7.
DR Gene3D; 3.40.50.1820; -; 1.
DR Gene3D; 4.10.800.10; -; 10.
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 Pfam; PF00135; COesterase; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00086; Thyroglobulin_1; 12.
DR SMART; SM00211; TY; 10.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF57610; SSF57610; 11.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 6.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 11.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hormone;
KW Iodination; Reference proteome; Repeat; Secreted; Signal; Sulfation;
KW Thyroid hormone; Thyroid hormones biosynthesis.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:12387814"
FT CHAIN 20..2692
FT /note="Thyroglobulin"
FT /evidence="ECO:0000255"
FT /id="PRO_5012700411"
FT DOMAIN 31..92
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 93..160
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 161..248
FT /note="Thyroglobulin type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 298..358
FT /note="Thyroglobulin type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 606..659
FT /note="Thyroglobulin type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 660..727
FT /note="Thyroglobulin type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 728..923
FT /note="Thyroglobulin type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1021..1079
FT /note="Thyroglobulin type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1088..1147
FT /note="Thyroglobulin type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1148..1212
FT /note="Thyroglobulin type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1389..1402
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1403..1419
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1420..1436
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DOMAIN 1444..1498
FT /note="Thyroglobulin type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1535..1655
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1656..1823
FT /note="Type IIIB"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1824..1926
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1927..2060
FT /note="Type IIIB"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 2061..2118
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REGION 2119..2692
FT /note="Cholinesterase-like (ChEL)"
FT /evidence="ECO:0000250|UniProtKB:O08710"
FT REGION 2658..2692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 24
FT /note="Sulfotyrosine; alternate"
FT /evidence="ECO:0000269|PubMed:12387814"
FT MOD_RES 24
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 24
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 108
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 149
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 149
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 234
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 258
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 705
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 705
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 705
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 705
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 786
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 868
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 868
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 885
FT /note="Diiodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 994
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 994
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 1241
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 1241
FT /note="Thyroxine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 1400
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 1400
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2115
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2467
FT /note="Thyroxine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2500
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2500
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2500
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2500
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2514
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2544
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2624
FT /note="Diiodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2690
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2690
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2690
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2690
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 949
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 34..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 63..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 72..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 96..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 131..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 140..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 164..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 194..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 301..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 330..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 338..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 364..621
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 408..609
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 632..637
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 639..659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 663..688
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 699..704
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 706..727
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 731..764
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 775..900
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 902..923
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 927..1033
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1044..1051
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1053..1079
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1128..1147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1151..1171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1183..1190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1192..1212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1237..1287
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1262..1278
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1372..1392
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1395..1406
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1409..1423
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1426..1443
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1447..1456
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1476..1498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1535..1559
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1539..1545
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1571..1594
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1656..1681
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1660..1666
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1665..1766
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1692..1709
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1824..1850
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1828..1835
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1859..1870
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1927..1955
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1931..1937
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1936..2007
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1966..1979
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2061..2085
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2065..2071
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2094..2103
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2518..2642
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT CONFLICT 11
FT /note="L -> P (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="S -> C (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="F -> L (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="G -> E (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="L -> P (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="E -> K (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="S -> L (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 395
FT /note="G -> A (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="R -> Q (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="L -> V (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 861
FT /note="G -> R (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="T -> S (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1137
FT /note="M -> T (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1360
FT /note="N -> D (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1524
FT /note="I -> K (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1541
FT /note="R -> L (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1546
FT /note="S -> G (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1590
FT /note="G -> R (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1605
FT /note="A -> P (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1619..1621
FT /note="IGQ -> VGR (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1657
FT /note="L -> F (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1712
FT /note="V -> M (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 1719
FT /note="R -> H (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 2189
FT /note="T -> S (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 2379
FT /note="Y -> C (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 2384
FT /note="G -> R (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 2390..2395
FT /note="NDAQMQ -> HDAQSK (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 2650
FT /note="L -> S (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 2662
FT /note="G -> E (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
FT CONFLICT 2676
FT /note="T -> A (in Ref. 1; ACY66900)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2692 AA; 293030 MW; 3309B325849A1795 CRC64;
MALALWVFAL LGSACLVSAN IFEYQVDAQP LRPCELQRER AFLKRADYVP QCAEDGSFQT
VQCKKDGGSC WCVDADGREV PGSRQPGRPV ACLSFCQLQK QQILLSSYIN STATSYLPQC
QDSGAYAPVQ CDVRREQCWC VDAEGMEVYG TRRLGRPARC PGSCEIRNRR LLHGVGDKSP
PQCSADGTFL PVQCKFVNTT DMMFFDLVHS YNRFPDAFVT FSSFRSRFPE VSGYCHCADS
QGRELAGTGL ELLLDEIYDT VFAGLDLASS FTETTLYRIL QRRFLAVQLV TSGRFRCPTK
CEVERFAATS FGHPYVPSCG RDGEYQAGQC QQEGLCWCVD AQGQEIPGTR RPSEPLSCAE
GQSCPSERRR ALSRLHLGPS GYSGQRGSFL AAERGPVSQT VPSFAASCPL PLKELFVESG
ILQPVVQGQK KEVTAATESL LKEGLRGIFP SRELARLALQ FTANPKRLQQ NLFGGRFLAN
VGQFNLSGAL GTRGTFNFSH FFQQLGLPGF QKRQALADPA KSLSVGLDSN PATEAPEALK
MGVAMNKTVV GSFGFEVNLQ ENRNALTFLS SLLELPEFLL FLQHAISVPE DIARDLGDVM
EMALSSQGCE QTPGSLFVPS CTAEGSYEDV QCFAGECWCV DARGRELAGS RARGGRPRCP
TACEKQRERM QSLLGRQPAG SSVFVPSCTR EGHFLPVQCF SSDCYCVDAD GQPIPGTRTA
PGEPKQCPTP CQLQAEQAFL GTVRGLISNP SEPPVLSSIY IPQCSASGQW RRVQCDGPPE
QAFEWYERWG AQSRSGQELT PAELLMKIMS YREAASGSFR LFIQNLYEAG QQGIFPGLAR
YSSLQDVPLA VLEGNLTQAT GNILLEPYLF WQILNGQLPR YPGPYSDFSA PLAHLDLRSC
WCVDEAGRKL EGTQTEPSKV PACPGSCEEV KLRVLQFIKE AEEIVMVSNS SQFPLGESFL
AAKGIRLTDE ELALPPLSPS RETFLEKFLS GSDYAIRLAA QSTFSFYQRR RVALSDAPRT
SGPLQPYPYV PQCDALGSWE PVQCHAATGH CWCVDGEGAY LPASLAARSP QVLQCPTPCE
TSRVRGLLSA WKQAGSQVRP SPKDLFIPAC TETGEFARLQ ASEASTWCVD PASGEAMPPG
TNSSAPCPGL CEVLQRGVPS RRASPGTTPA CRAEDGGFAP VQCDPAQGSC WCVLGSGEEV
PGTRVAGSQP ACERPQLWQT IQTRGQFQLQ LPPGKVCSAD YAGLLPTFQV VILDELTARG
FCRIQVTTAR TPVSIPVCDD STVRVGCLSL DRLGVNVTWT LRLEDAPPAS LPDLRDIEEA
LAGKDLVGRF ADLIQSGTFQ LHLDSRTFPA DPSIHFLQGN SLGTSPRTRF GCVEGSRQVP
ATSNTSQDPL GCVRCPEGSY FQEEQCIPCP AGFYQEQTGS LACAPCPAGT TTTSVGAFSQ
THCVTACQRD EAGLQCDQDG QYRASQRDRA SGKAFCVDSE GRRLPWSETQ APLVDAQCLM
MRKFEKLPES KVIFTADVAV LGSIVPDSES SLMQCLADCA RDEACSFLTV SLEGSEGSCD
FYAWTSDNIA CTSSGQEEDA LGTSKATSLG SLTCQVKVRP GDGVAPAVYL KKGQEFATIG
QKRFEQTGFQ NALSGLYSPV VFSASGASLT EAHLFCLLAC DRDSCCDGFI LTQVQGGPII
CGLLSSPDVL LCHVRDWRDP SEAQADATCP GVTYDQDSRQ GTLRLGGQEF KSLTPREGAR
DTFTSFQQVY LWKDSDMGSR SESMGCRRDM QPRPESPEET DLTAELFSPV DLNQVIVSEN
RSLPSQQHRL FKHLFSLQQA HLWCLSRCVQ EPSFCQLAEI TDSSPLYLTC TLYPEAQVCD
DVMEASPRGC RRILPRRPNA LFQRRVVLQD RVKNFYTRLP FQKLTGLSIR HKVPMADKAI
SSGFFECERL CDVDPCCTGF GFLNVSQLKG GEVTCLTLNS LGLQTCSEEN GGSWRLLACG
SPDTEVRTYP FGWYQKPAVQ NDAPSFCPSA ALPPVPEKVA LDSWQPLPPS SVVVDPSIRN
FDVAHISTAA VGDFSAARER CLLECSRHQA CLVTTLQTRP GAVRCMFYAD TQSCTHSLQA
QNCQLLLREE ATHIYRKPDI PLPGLGSSAP TVTIATHGQL LGTSQAIQLG ASWKQVDQFL
GVPYAAPPLA ESRFRAPEPL NWTGTWDATK PRASCWQPGI RPATAPGVSE DCLYLSVFVP
QSLTPNSSVL VFFHNGAEGP LAMAVDGSFL AAVGNLIVVT ASYRTGVFGF LSSGSSEVSG
NWGLLDQVAA LTWVQTHIGV FGGDPRRVAL AADRGGADVA GIHLLTSRAT NSRLFRRAVL
MGGSVLSPAA VIRPDRAQQQ AAALAKEVGC PPRPSQKWYP ASAGACQPPN DAQMQLLAVS
GPFHYWGPVV DGQLLREAPA RALQRPPRAK LDLLIGSSQD DGLIDRAKAV KRFEESQGRT
SSKTAFYQAL QNSLGGEAGD PGVQAAATWY YSLEHDTDDY ASFSRALEAA TRDYFIICPV
IDMASHWART ARGNVFMYHA PESYSHGSLE LLADVRYAFG LPFYPAYEGQ FTQEEKSLSL
KIMQYFSNFV RSGNPNYPHE FSRKAPEFAA PWPDFVPGDG AESYKELSVL LPNRQGLKKA
DCSFWSKYIL SLKASADEAE DGPLAESEEE DRPGLTEDLL GLPELASKSY SK
