THYG_BOVIN
ID THYG_BOVIN Reviewed; 2769 AA.
AC P01267; O18976; Q28196; Q95478;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Thyroglobulin;
DE Short=Tg;
DE Flags: Precursor;
GN Name=TG;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3855243; DOI=10.1038/316647a0;
RA Mercken L., Simons M.-J., Swillens S., Massaer M., Vassart G.;
RT "Primary structure of bovine thyroglobulin deduced from the sequence of its
RT 8,431-base complementary DNA.";
RL Nature 316:647-651(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-930.
RX PubMed=3855750; DOI=10.1111/j.1432-1033.1985.tb08718.x;
RA Mercken L., Simons M.-J., de Martynhoff G., Swillens S., Vassart G.;
RT "Presence of hormonogenic and repetitive domains in the first 930 amino
RT acids of bovine thyroglobulin as deduced from the cDNA sequence.";
RL Eur. J. Biochem. 147:59-64(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=3032624; DOI=10.1111/j.1432-1033.1987.tb11168.x;
RA de Martynhoff G., Pohl V., Mercken L., van Ommen G.-J., Vassart G.;
RT "Structural organization of the bovine thyroglobulin gene and of its 5'-
RT flanking region.";
RL Eur. J. Biochem. 164:591-599(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1002-1209.
RX PubMed=3681978; DOI=10.1016/0022-2836(87)90403-7;
RA Parma J., Christophe D., Pohl V., Vassart G.;
RT "Structural organization of the 5' region of the thyroglobulin gene.
RT Evidence for intron loss and 'exonization' during evolution.";
RL J. Mol. Biol. 196:769-779(1987).
RN [5]
RP TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-110; ASN-483; ASN-495; ASN-853;
RP ASN-947; ASN-1140; ASN-1365; ASN-1776; ASN-1870; ASN-2014; ASN-2123;
RP ASN-2251 AND ASN-2296, LACK OF GLYCOSYLATION AT ASN-198, AND STRUCTURE OF
RP CARBOHYDRATE.
RX PubMed=8424663; DOI=10.1006/abbi.1993.1038;
RA Rawitch A.B., Pollock H.G., Yang S.X.;
RT "Thyroglobulin glycosylation: location and nature of the N-linked
RT oligosaccharide units in bovine thyroglobulin.";
RL Arch. Biochem. Biophys. 300:271-279(1993).
CC -!- FUNCTION: Acts as a substrate for the production of iodinated thyroid
CC hormones thyroxine (T4) and triiodothyronine (T3) (By similarity). The
CC synthesis of T3 and T4 involves iodination of selected tyrosine
CC residues of TG/thyroglobulin followed by their oxidative coupling (By
CC similarity). Following TG re-internalization and lysosomal-mediated
CC proteolysis, T3 and T4 are released from the polypeptide backbone
CC leading to their secretion into the bloodstream (By similarity). One
CC dimer produces 7 thyroid hormone molecules (By similarity).
CC {ECO:0000250|UniProtKB:F1RRV3, ECO:0000250|UniProtKB:O08710,
CC ECO:0000250|UniProtKB:P01266}.
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:0000250|UniProtKB:O08710}.
CC Note=Secreted into the thyroid follicle lumen. Localizes to colloid
CC globules, a structure formed in the thyroid follicle lumen consisting
CC of cross-linked TG arranged in concentric layers.
CC {ECO:0000250|UniProtKB:O08710}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the thyroid gland.
CC {ECO:0000269|PubMed:8424663}.
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 (By similarity). There are 4
CC pairs of iodinated tyrosines used for coupling: acceptor Tyr-24 is
CC coupled to donor Tyr-149 or Tyr-234, acceptor Tyr-2574 is coupled to
CC donor Tyr-2541, acceptor Tyr-2767 in monomer 1 is coupled to donor Tyr-
CC 2767 in monomer 2 and acceptor Tyr-1310 in monomer 1 is coupled to
CC donor Tyr-108 in monomer 2 (By similarity).
CC {ECO:0000250|UniProtKB:F1RRV3, ECO:0000250|UniProtKB:P01266}.
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. In the thyroid
CC follicle lumen, cross-linked TG (storage form) is solubilized by
CC limited proteolysis mediated by cathepsins CTSB and/or CTSL. Partially
CC cleaved TG is further processed by CTSK/cathepsin K and/or CTSL
CC resulting in the release of T4. Following endocytosis, further
CC processing occurs leading to the release of T3 and more T4 hormones.
CC {ECO:0000250|UniProtKB:O08710}.
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; X02815; CAA26584.1; -; mRNA.
DR EMBL; X02155; CAA26090.1; -; mRNA.
DR EMBL; X05380; CAA28971.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X06071; CAA29457.1; -; Genomic_DNA.
DR EMBL; X06072; CAA29457.1; JOINED; Genomic_DNA.
DR EMBL; X06073; CAA29457.1; JOINED; Genomic_DNA.
DR EMBL; X06074; CAA29457.1; JOINED; Genomic_DNA.
DR EMBL; X06075; CAA29457.1; JOINED; Genomic_DNA.
DR PIR; A01533; UIBO.
DR RefSeq; NP_776308.1; NM_173883.2.
DR SASBDB; P01267; -.
DR SMR; P01267; -.
DR IntAct; P01267; 1.
DR STRING; 9913.ENSBTAP00000010295; -.
DR Allergome; 11790; Bos d TG.
DR ESTHER; bovin-thyro; Thyroglobulin.
DR MEROPS; I31.950; -.
DR MEROPS; S09.978; -.
DR GlyConnect; 598; 1 N-Linked glycan.
DR iPTMnet; P01267; -.
DR PaxDb; P01267; -.
DR PRIDE; P01267; -.
DR ABCD; P01267; 3 sequenced antibodies.
DR GeneID; 280706; -.
DR KEGG; bta:280706; -.
DR CTD; 7038; -.
DR eggNOG; KOG1214; Eukaryota.
DR InParanoid; P01267; -.
DR OrthoDB; 754103at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IPI:CAFA.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006590; P:thyroid hormone generation; ISS:UniProtKB.
DR CDD; cd00191; TY; 8.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR016324; Thyroglobulin.
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; 10.
DR PIRSF; PIRSF001831; Thyroglobulin; 1.
DR SMART; SM00211; TY; 10.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57610; SSF57610; 11.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 9.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 11.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hormone; Iodination; Reference proteome;
KW Repeat; Secreted; Signal; Sulfation; Thyroid hormone;
KW Thyroid hormones biosynthesis.
FT SIGNAL 1..19
FT /evidence="ECO:0000250|UniProtKB:F1RRV3"
FT CHAIN 20..2769
FT /note="Thyroglobulin"
FT /id="PRO_0000008635"
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..297
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 604..657
FT /note="Thyroglobulin type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 658..725
FT /note="Thyroglobulin type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 726..921
FT /note="Thyroglobulin type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 922..1073
FT /note="Thyroglobulin type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1074..1145
FT /note="Thyroglobulin type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1146..1210
FT /note="Thyroglobulin type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1458..1471
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1472..1488
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1489..1505
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DOMAIN 1513..1567
FT /note="Thyroglobulin type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1605..1725
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1726..1893
FT /note="Type IIIB"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1894..1996
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1997..2130
FT /note="Type IIIB"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 2131..2188
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REGION 1827..1851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2189..2769
FT /note="Cholinesterase-like (ChEL)"
FT /evidence="ECO:0000250|UniProtKB:O08710"
FT REGION 2730..2769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1830..1845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 198
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:8424663"
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:0000250|UniProtKB:F1RRV3"
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 703
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 703
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 703
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 703
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 784
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 866
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 866
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 883
FT /note="Diiodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 992
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 992
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 1310
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 1310
FT /note="Thyroxine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 1469
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 1469
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2185
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2541
FT /note="Thyroxine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2574
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2574
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2574
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2574
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2588
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2618
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2698
FT /note="Diiodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2767
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2767
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2767
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2767
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 853
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 853
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 947
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 947
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 1140
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 1140
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 1365
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 1776
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 1776
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 1870
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 1870
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 2014
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 2123
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 2251
FT /note="N-linked (GlcNAc...) (complex) asparagine;
FT alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 2251
FT /note="N-linked (GlcNAc...) (hybrid) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:8424663"
FT CARBOHYD 2296
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:8424663"
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..619
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 408..607
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 630..635
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 637..657
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 661..686
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 697..702
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 704..725
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 729..762
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 773..898
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 900..921
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 925..1031
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1042..1049
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1051..1073
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1077..1108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1126..1145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1149..1169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1181..1188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1190..1210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1215..1264
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1231..1245
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1306..1356
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1331..1347
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1441..1461
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1464..1475
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1478..1492
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1495..1512
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1516..1525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1545..1567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1605..1629
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1609..1615
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1641..1664
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1726..1751
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1730..1736
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1735..1836
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1762..1779
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1894..1920
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1898..1905
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1929..1940
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1997..2025
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2001..2007
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2006..2077
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2036..2049
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2131..2155
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2135..2141
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2164..2173
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2443..2454
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2592..2716
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT CONFLICT 1206
FT /note="S -> R (in Ref. 4; CAA29457)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2769 AA; 303222 MW; 1C7F227E9101DE2A CRC64;
MALALWVFGL LDLICLASAN IFEYQVDAQP LRPCELQRER AFLKREDYVP QCAEDGSFQT
VQCGKDGASC WCVDADGREV PGSRQPGRPA ACLSFCQLQK QQILLSSYIN STATSYLPQC
QDSGDYSPVQ CDLRRRQCWC VDAEGMEVYG TRQQGRPARC PRSCEIRNRR LLHGVGDRSP
PQCSPDGAFR PVQCKLVNTT DMMIFDLVHS YSRFPDAFVT FSSFRSRFPE VSGYCYCADS
QGRELAETGL ELLLDEIYDT IFAGLDLAST FAETTLYRIL QRRFLAVQLV ISGRFRCPTK
CEVERFAATS FRHPYVPSCH PDGEYQAAQC QQGGPCWCVD SRGQEIPGTR QRGEPPSCAE
DQSCPSERRR AFSRLRFGPS GYFSRRSLLL APEEGPVSQR FARFTASCPP SIKELFLDSG
IFQPMLQGRD TRFVAPESLK EAIRGLFPSR ELARLALQFT TNAKRLQQNL FGGRFLVKVG
QFNLSGALGT RGTFNFSHFF QQLGLPGFQD GRALADLAKP LSVGLNSNPA SEAPKASKID
VALRKPVVGS FGFEVNLQEN QNALQFLSSF LELPEFLLFL QHAISVPEDI ARDLGDVMEM
VFSSQGCGQA PGSLFVPACT AEGSYEEVQC FAGDCWCVDA QGRELAGSRV RGGRPRCPTE
CEKQRARMQS LLGSQPAGSS LFVPACTSKG NFLPVQCFNS ECYCVDTEGQ PIPGTRSALG
EPKKCPSPCQ LQAERAFLGT VRTLVSNPST LPALSSIYIP QCSASGQWSP VQCDGPPEQA
FEWYERWEAQ NSAGQALTPA ELLMKIMSYR EAASRNFRLF IQNLYEAGQQ GIFPGLARYS
SFQDVPVSVL EGNQTQPGGN VFLEPYLFWQ ILNGQLDRYP GPYSDFSAPL AHFDLRSCWC
VDEAGQKLEG TRNEPNKVPA CPGSCEEVKL RVLQFIREAE EIVTYSNSSR FPLGESFLAA
KGIRLTDEEL AFPPLSPSRE TFLEKFLSGS DYAIRLAAQS TFDFYQRRLV TLAESPRAPS
PVWSSAYLPQ CDAFGGWEPV QCHAATGHCW CVDGKGEYVP TSLTARSRQI PQCPTSCERL
RASGLLSSWK QAGVQAEPSP KDLFIPTCLE TGEFARLQAS EAGTWCVDPA SGEGVPPGTN
SSAQCPSLCE VLQSGVPSRR TSPGYSPACR AEDGGFSPVQ CDPAQGSCWC VLGSGEEVPG
TRVAGSQPAC ESPQCPLPFS VADVAGGAIL CERASGLGAA AGQRCQLRCS QGYRSAFPPE
PLLCSVQRRR WESRPPQPRA CQRPQFWQTL QTQAQFQLLL PLGKVCSADY SGLLLAFQVF
LLDELTARGF CQIQVKTAGT PVSIPVCDDS SVKVECLSRE RLGVNITWKL QLVDAPPASL
PDLQDVEEAL AGKYLAGRFA DLIQSGTFQL HLDSKTFSAD TSIRFLQGDR FGTSPRTQFG
CLEGFGRVVA ASDASQDALG CVKCPEGSYF QDEQCIPCPA GFYQEQAGSL ACVPCPEGRT
TVYAGAFSQT HCVTDCQKNE VGLQCDQDSQ YRASQRDRTS GKAFCVDGEG RRLPWTEAEA
PLVDAQCLVM RKFEKLPESK VIFSADVAVM VRSEVPGSES SLMQCLADCA LDEACGFLTV
STAGSEVSCD FYAWASDSIA CTTSGRSEDA LGTSQATSFG SLQCQVKVRS REGDPLAVYL
KKGQEFTITG QKRFEQTGFQ SALSGMYSPV TFSASGASLA EVHLFCLLAC DHDSCCDGFI
LVQVQGGPLL CGLLSSPDVL LCHVRDWRDP AEAQANASCP GVTYDQDSRQ VTLRLGGQEI
RGLTPLEGTQ DTLTSFQQVY LWKDSDMGSR SESMGCRRDT EPRPASPSET DLTTGLFSPV
DLIQVIVDGN VSLPSQQHWL FKHLFSLQQA NLWCLSRCAG EPSFCQLAEV TDSEPLYFTC
TLYPEAQVCD DILESSPKGC RLILPRRPSA LYRKKVVLQD RVKNFYNRLP FQKLTGISIR
NKVPMSDKSI SSGFFECERL CDMDPCCTGF GFLNVSQLKG GEVTCLTLNS LGLQTCSEEY
GGVWRILDCG SPDTEVRTYP FGWYQKPVSP SDAPSFCPSV ALPALTENVA LDSWQSLALS
SVIVDPSIRN FDVAHISTAA VGNFSAARDR CLWECSRHQD CLVTTLQTQP GAVRCMFYAD
TQSCTHSLQA QNCRLLLHEE ATYIYRKPNI PLPGFGTSSP SVPIATHGQL LGRSQAIQVG
TSWKPVDQFL GVPYAAPPLG EKRFRAPEHL NWTGSWEATK PRARCWQPGI RTPTPPGVSE
DCLYLNVFVP QNMAPNASVL VFFHNAAEGK GSGDRPAVDG SFLAAVGNLI VVTASYRTGI
FGFLSSGSSE LSGNWGLLDQ VVALTWVQTH IQAFGGDPRR VTLAADRGGA DIASIHLVTT
RAANSRLFRR AVLMGGSALS PAAVIRPERA RQQAAALAKE VGCPSSSVQE MVSCLRQEPA
RILNDAQTKL LAVSGPFHYW GPVVDGQYLR ETPARVLQRA PRVKVDLLIG SSQDDGLINR
AKAVKQFEES QGRTSSKTAF YQALQNSLGG EAADAGVQAA ATWYYSLEHD SDDYASFSRA
LEQATRDYFI ICPVIDMASH WARTVRGNVF MYHAPESYSH SSLELLTDVL YAFGLPFYPA
YEGQFTLEEK SLSLKIMQYF SNFIRSGNPN YPHEFSRRAP EFAAPWPDFV PRDGAESYKE
LSVLLPNRQG LKKADCSFWS KYIQSLKASA DETKDGPSAD SEEEDQPAGS GLTEDLLGLP
ELASKTYSK
