ID THYG_MOUSE Reviewed; 2766 AA.
AC O08710; O88590; Q2NKY1; Q9QWY7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 27-MAR-2024, entry version 189.
DE RecName: Full=Thyroglobulin;
DE Short=Tg;
DE Flags: Precursor;
GN Name=Tg; Synonyms=Tgn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9344706; DOI=10.1006/clin.1997.4428;
RA Caturegli P., Vidalain P.O., Vali M., Aguilera-Galaviz L.A., Rose N.R.;
RT "Cloning and characterization of murine thyroglobulin cDNA.";
RL Clin. Immunol. Immunopathol. 85:221-226(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT COG PRO-2283.
RC STRAIN=COG; TISSUE=Thyroid;
RX PubMed=9707574; DOI=10.1073/pnas.95.17.9909;
RA Kim P.S., Hossain S.A., Park Y.-N., Lee I., Yoo S.-E., Arvan P.;
RT "A single amino acid change in the acetylcholinesterase-like domain of
RT thyroglobulin causes congenital goiter with hypothyroidism in the cog/cog
RT mouse: a model of human endoplasmic reticulum storage diseases.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9909-9913(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AKR/J; TISSUE=Thyroid;
RA Hossain S.A., Yoo S.-E., Kim P.S.;
RT "Cloning, characterization, site-directed mutagenesis, and transient
RT expression of 8301-nucleotide AKR/J mouse thyroglobulin cDNA: defective
RT secretion of mutant thyroglobulins.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thyroid;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=12782676; DOI=10.1172/jci15990;
RA Friedrichs B., Tepel C., Reinheckel T., Deussing J., von Figura K.,
RA Herzog V., Peters C., Saftig P., Brix K.;
RT "Thyroid functions of mouse cathepsins B, K, and L.";
RL J. Clin. Invest. 111:1733-1745(2003).
RN [7]
RP SUBUNIT, SUBCELLULAR LOCATION, CHOLINESTERASE-LIKE REGION, DISULFIDE BOND,
RP AND MUTAGENESIS OF GLY-2318.
RX PubMed=19276074; DOI=10.1074/jbc.m806898200;
RA Lee J., Wang X., Di Jeso B., Arvan P.;
RT "The cholinesterase-like domain, essential in thyroglobulin trafficking for
RT thyroid hormone synthesis, is required for protein dimerization.";
RL J. Biol. Chem. 284:12752-12761(2009).
RN [8]
RP INVOLVEMENT IN COG DISEASE.
RX PubMed=3803305; DOI=10.1210/endo-120-2-838;
RA Beamer W.G., Maltais L.J., DeBaets M.H., Eicher E.M.;
RT "Inherited congenital goiter in mice.";
RL Endocrinology 120:838-840(1987).
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 (Probable). One dimer
CC produces 7 thyroid hormone molecules (By similarity).
CC {ECO:0000250|UniProtKB:F1RRV3, ECO:0000250|UniProtKB:P01266,
CC ECO:0000305|PubMed:12782676}.
CC -!- SUBUNIT: Monomer (PubMed:12782676). Homodimer (via ChEL region); occurs
CC in the endoplasmic reticulum and is required for export to the Golgi
CC apparatus (PubMed:19276074, PubMed:12782676). Homooligomer; disulfide-
CC linked; stored in this form in the thyroid follicle lumen (By
CC similarity). {ECO:0000250|UniProtKB:P01266,
CC ECO:0000269|PubMed:12782676, ECO:0000269|PubMed:19276074}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12782676,
CC ECO:0000269|PubMed:19276074}. Note=Secreted into the thyroid follicle
CC lumen (PubMed:12782676). Localizes to colloid globules, a structure
CC formed in the thyroid follicle lumen consisting of cross-linked TG
CC arranged in concentric layers (PubMed:12782676).
CC {ECO:0000269|PubMed:12782676}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in the thyroid gland.
CC {ECO:0000269|PubMed:12782676}.
CC -!- DOMAIN: The cholinesterase-like (ChEL) region is required for
CC dimerization and export from the endoplasmic reticulum.
CC {ECO:0000269|PubMed:19276074}.
CC -!- PTM: Iodinated on tyrosine residues by TPO (By similarity). There are 4
CC pairs of iodinated tyrosines used for coupling: acceptor Tyr-25 is
CC coupled to donor Tyr-150 or Tyr-235, acceptor Tyr-2572 is coupled to
CC donor Tyr-2539, acceptor Tyr-2764 in monomer 1 is coupled to donor Tyr-
CC 2764 in monomer 2 and acceptor Tyr-1310 in monomer 1 is coupled to
CC donor Tyr-109 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 (PubMed:12782676). 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 (PubMed:12782676). Partially cleaved TG is further processed by
CC CTSK/cathepsin K and/or CTSL resulting in the release of T4
CC (PubMed:12782676). Following endocytosis, further processing occurs
CC leading to the release of T3 and more T4 hormones (Probable).
CC {ECO:0000269|PubMed:12782676, ECO:0000305|PubMed:12782676}.
CC -!- DISEASE: Note=Congenital goiter (cog) is caused by a hypertrophy of the
CC thyroid gland (goiter). Mice have reduced growth rate, hypothyroidism
CC due to reduced production of the thyroid hormones thyroxine (T4) and
CC triiodothyronine (T3), and lack colloid globules, a structure in the
CC thyroid follicle lumen that is enriched in Tg/thyroglobulin.
CC {ECO:0000269|PubMed:3803305}.
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; U76389; AAB53204.1; -; mRNA.
DR EMBL; AF076186; AAC32268.1; -; mRNA.
DR EMBL; AF076187; AAC32269.1; -; mRNA.
DR EMBL; CH466545; EDL29374.1; -; Genomic_DNA.
DR EMBL; BC111467; AAI11468.1; -; mRNA.
DR CCDS; CCDS37091.1; -.
DR RefSeq; NP_033401.2; NM_009375.2.
DR SMR; O08710; -.
DR BioGRID; 204170; 3.
DR IntAct; O08710; 1.
DR STRING; 10090.ENSMUSP00000070239; -.
DR ESTHER; mouse-thyro; Thyroglobulin.
DR MEROPS; I31.950; -.
DR MEROPS; S09.978; -.
DR GlyCosmos; O08710; 20 sites, No reported glycans.
DR GlyGen; O08710; 20 sites.
DR iPTMnet; O08710; -.
DR PhosphoSitePlus; O08710; -.
DR CPTAC; non-CPTAC-3953; -.
DR EPD; O08710; -.
DR MaxQB; O08710; -.
DR PaxDb; 10090-ENSMUSP00000070239; -.
DR ProteomicsDB; 262987; -.
DR ABCD; O08710; 5 sequenced antibodies.
DR Antibodypedia; 860; 2134 antibodies from 44 providers.
DR DNASU; 21819; -.
DR Ensembl; ENSMUST00000065916.14; ENSMUSP00000070239.8; ENSMUSG00000053469.15.
DR GeneID; 21819; -.
DR KEGG; mmu:21819; -.
DR UCSC; uc007wap.1; mouse.
DR AGR; MGI:98733; -.
DR CTD; 7038; -.
DR MGI; MGI:98733; Tg.
DR VEuPathDB; HostDB:ENSMUSG00000053469; -.
DR eggNOG; KOG1214; Eukaryota.
DR GeneTree; ENSGT00940000159300; -.
DR HOGENOM; CLU_000943_0_0_1; -.
DR InParanoid; O08710; -.
DR OMA; IQCDGPP; -.
DR OrthoDB; 5314395at2759; -.
DR TreeFam; TF351833; -.
DR BioGRID-ORCS; 21819; 1 hit in 79 CRISPR screens.
DR ChiTaRS; Tg; mouse.
DR PRO; PR:O08710; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O08710; Protein.
DR Bgee; ENSMUSG00000053469; Expressed in trachea and 37 other cell types or tissues.
DR ExpressionAtlas; O08710; baseline and differential.
DR Genevisible; O08710; MM.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0043168; F:anion binding; ISO:MGI.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0051087; F:protein-folding chaperone binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0042446; P:hormone biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0015705; P:iodide transport; IMP:MGI.
DR GO; GO:0031641; P:regulation of myelination; IMP:MGI.
DR GO; GO:0009268; P:response to pH; ISO:MGI.
DR GO; GO:0030878; P:thyroid gland development; IEA:Ensembl.
DR GO; GO:0006590; P:thyroid hormone generation; IDA:UniProtKB.
DR GO; GO:0042403; P:thyroid hormone metabolic process; IMP:MGI.
DR GO; GO:0045056; P:transcytosis; ISO:MGI.
DR CDD; cd00191; TY; 7.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 10.
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; IPR016324; Thyroglobulin.
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; 11.
DR PIRSF; PIRSF001831; Thyroglobulin; 1.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00211; TY; 10.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 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 Disease variant; Disulfide bond; Glycoprotein; Hormone; Iodination;
KW Reference proteome; Repeat; Secreted; Signal; Sulfation; Thyroid hormone;
KW Thyroid hormones biosynthesis.
FT SIGNAL 1..20
FT /evidence="ECO:0000250|UniProtKB:F1RRV3"
FT CHAIN 21..2766
FT /note="Thyroglobulin"
FT /id="PRO_0000008637"
FT DOMAIN 32..93
FT /note="Thyroglobulin type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 94..161
FT /note="Thyroglobulin type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 162..298
FT /note="Thyroglobulin type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 299..359
FT /note="Thyroglobulin type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 605..658
FT /note="Thyroglobulin type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 659..726
FT /note="Thyroglobulin type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 727..922
FT /note="Thyroglobulin type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 923..1074
FT /note="Thyroglobulin type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1075..1146
FT /note="Thyroglobulin type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DOMAIN 1147..1211
FT /note="Thyroglobulin type-1 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1455..1468
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1469..1485
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1486..1502
FT /note="Type II"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DOMAIN 1510..1564
FT /note="Thyroglobulin type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 1602..1722
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1723..1889
FT /note="Type IIIB"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1890..1992
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 1993..2125
FT /note="Type IIIB"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REPEAT 2126..2183
FT /note="Type IIIA"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT REGION 2186..2766
FT /note="Cholinesterase-like (ChEL)"
FT /evidence="ECO:0000305|PubMed:19276074"
FT REGION 2729..2766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 25
FT /note="Sulfotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:F1RRV3"
FT MOD_RES 25
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 25
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 109
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 150
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 150
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 235
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 259
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 704
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 704
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 704
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 704
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 785
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 867
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 867
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 884
FT /note="Diiodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 993
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 993
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 2182
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2539
FT /note="Thyroxine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2572
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2572
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2572
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2572
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2586
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2616
FT /note="Iodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2696
FT /note="Diiodotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2764
FT /note="Diiodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2764
FT /note="Iodotyrosine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2764
FT /note="Thyroxine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT MOD_RES 2764
FT /note="Triiodothyronine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 748
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1864
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1935
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 64..71
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 73..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 97..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 132..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 141..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 165..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 195..236
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 302..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 331..337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 339..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 365..620
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 408..608
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 631..636
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 638..658
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 662..687
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 698..703
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 705..726
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 730..763
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 774..899
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 901..922
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 926..1032
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1043..1050
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1052..1074
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1078..1109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1127..1146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1150..1170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1182..1189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1191..1211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1216..1265
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1232..1246
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..1458
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1461..1472
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1475..1489
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1492..1509
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1513..1522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1542..1564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 1602..1626
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1606..1612
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1638..1661
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1723..1748
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1727..1733
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1732..1834
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1759..1776
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1890..1916
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1894..1901
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1925..1936
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1993..2021
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 1997..2003
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2002..2073
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2032..2045
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2128..2152
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2132..2138
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2161..2170
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2263..2280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT DISULFID 2441..2452
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT DISULFID 2590..2714
FT /evidence="ECO:0000250|UniProtKB:P01266"
FT VARIANT 2283
FT /note="L -> P (in cog; impairs secretion due to ER
FT retention)"
FT /evidence="ECO:0000269|PubMed:9707574"
FT MUTAGEN 2318
FT /note="G->R: Impairs secretion."
FT /evidence="ECO:0000269|PubMed:19276074"
FT CONFLICT 80
FT /note="E -> K (in Ref. 2; AAC32268 and 3; AAC32269)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="V -> I (in Ref. 2; AAC32268 and 3; AAC32269)"
FT /evidence="ECO:0000305"
FT CONFLICT 1327
FT /note="A -> T (in Ref. 1; AAB53204)"
FT /evidence="ECO:0000305"
FT CONFLICT 1427
FT /note="N -> S (in Ref. 1; AAB53204)"
FT /evidence="ECO:0000305"
FT CONFLICT 1436..1442
FT /note="RTQLGCM -> GLSLDVL (in Ref. 1; AAB53204)"
FT /evidence="ECO:0000305"
FT CONFLICT 1721
FT /note="T -> I (in Ref. 1; AAB53204)"
FT /evidence="ECO:0000305"
FT CONFLICT 1813
FT /note="S -> T (in Ref. 1; AAB53204)"
FT /evidence="ECO:0000305"
FT CONFLICT 1957..1959
FT /note="RVK -> KVN (in Ref. 2; AAC32268 and 3; AAC32269)"
FT /evidence="ECO:0000305"
FT CONFLICT 2090
FT /note="S -> SS (in Ref. 1; AAB53204)"
FT /evidence="ECO:0000305"
FT CONFLICT 2407
FT /note="R -> K (in Ref. 2; AAC32268 and 3; AAC32269)"
FT /evidence="ECO:0000305"
FT CONFLICT 2414
FT /note="G -> S (in Ref. 2; AAC32268 and 3; AAC32269)"
FT /evidence="ECO:0000305"
FT CONFLICT 2427
FT /note="R -> K (in Ref. 2; AAC32268 and 3; AAC32269)"
FT /evidence="ECO:0000305"
FT CONFLICT 2434
FT /note="A -> T (in Ref. 2; AAC32268 and 3; AAC32269)"
FT /evidence="ECO:0000305"
FT CONFLICT 2443..2453
FT /note="TSSIQEVVSCL -> NFIHPGSGIMF (in Ref. 2; AAC32268 and
FT 3; AAC32269)"
FT /evidence="ECO:0000305"
FT CONFLICT 2728
FT /note="D -> GN (in Ref. 1; AAB53204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2766 AA; 304473 MW; 06227D4192AC1902 CRC64;
MTALVLWVST LLSSVCLVAA NIFEYQVDAQ PLRPCELQRE KAFLKQAEYV PQCSEDGSFQ
TVQCQNDGQS CWCVDSDGRE VPGSRQLGRP TVCLSFCQLH KQRILLGSYI NSTDALYLPQ
CQDSGNYAPV QCDLQRVQCW CVDTEGMEVY GTRQQGRPTR CPRSCEIRNR RLLHGVGDRS
PPQCTADGEF MPVQCKFVNT TDMMIFDLIH NYNRFPDAFV TFSSFRGRFP EVSGYCYCAD
SQGRELAETG LELLLDEIYD TIFAGLDQAS TFTQSTMYRI LQRRFLAIQL VISGRFRCPT
KCEVEQFAAT RFGHSYIPRC HRDGHYQTVQ CQTEGMCWCV DAQGREVPGT RQQGQPPSCA
ADQSCALERQ QALSRFYFET PDYFSPQDLL SSEDRLAPVS GVRSDTSCPP RIKELFVDSG
LLRSIAVEHY QRLSESRSLL REAIRAVFPS RELAGLALQF TTNPKRLQQN LFGGTFLANA
AQFNLSGALG TRSTFNFSQF FQQFGLPGFL NRDRVTTLAK LLPVRLDSSS TPETLRVSEK
TVAMNKRVVG NFGFKVNLQE NQDALKFLVS LLELPEFLVF LQRAVSVPED IARDLGDVME
MVFSAQACKQ MPGKFFVPSC TAGGSYEDIQ CYAGECWCVD SRGKELDGSR VRGGRPRCPT
KCEKQRAQMQ SLASAQPAGS SFFVPTCTRE GYFLPVQCFN SECYCVDTEG QVIPGTQSTV
GEAKQCPSVC QLQAEQAFLG VVGVLLSNSS MVPSISNVYI PQCSASGQWR HVQCDGPHEQ
VFEWYERWKT QNGDGQELTP AALLMKIVSY REVASRNFSL FLQSLYDAGQ QRIFPVLAQY
PSLQDVPQVV LEGATTPPGE NIFLDPYIFW QILNGQLSQY PGPYSDFNMP LEHFNLRSCW
CVDEAGQKLD GTQTKPGEIP ACPGPCEEVK LRVLKFIKET EEIVSASNAS SFPLGESFLV
AKGIQLTSEE LDLPPQFPSR DAFSEKFLRG GEYAIRLAAQ STLTFYQSLR ASLGKSDGAA
SLLWSGPYMP QCNMIGGWEP VQCHAGTGQC WCVDGRGEFI PGSLMSRSSQ MPQCPTNCEL
SRASGLISAW KQAGPQRNPG PGDLFIPVCL QTGEYVRKQT SGTGTWCVDP ASGEGMPVNT
NGSAQCPGLC DVLKSRALSR KVGLGYSPVC EALDGAFSPV QCDLAQGSCW CVLGSGEEVP
GTRVVGTQPA CESPQCPLPF SGSDVADGVI FCETASSSGV TTVQQCQLLC RQGLRSAFSP
GPLICSLESQ HWVTLPPPRA CQRPQLWQTM QTQAHFQLLL PPGKMCSVDY SGLLQAFQVF
ILDELIARGF CQIQVKTFGT LVSSTVCDNS SIQVGCLTAE RLGVNVTWKL QLEDISVGSL
PDLYSIERAV TGQDLLGRFA DLIQSGRFQL HLDSKTFSAD TTLYFLNGDS FVTSPRTQLG
CMEGFYRVPT TRQDALGCVK CPEGSFSQDG RCTPCPAGTY QEQAGSSACI PCPRGRTTIT
TGAFSKTHCV TDCQKNEAGL QCDQNGQYQA SQKNRDSGEV FCVDSEGRKL QWLQTEAGLS
ESQCLMIRKF DKAPESKVIF DANSPVIVKS SVPSADSPLV QCLTDCANDE ACSFLTVSTM
ESEVSCDFYS WTRDNFACVT SDQEQDAMGS LKATSFGSLR CQVKVRNSGK DSLAVYVKKG
YESTAAGQKS FEPTGFQNVL SGLYSPVVFS ASGANLTDTH TYCLLACDND SCCDGFIITQ
VKGGPTICGL LSSPDILLCH INDWRDTSAT QANATCAGVT YDQGSRQMTL SLGGQEFLQG
LALLEGTQDS FTSFQQVYLW KDSDMGSRPE SMGCERGMVP RSDFPGDMAT ELFSPVDITQ
VIVNTSHSLP SQQYWLFTHL FSAEQANLWC LSRCAQEPIF CQLADITKSS SLYFTCFLYP
EAQVCDNVME SNAKNCSQIL PHQPTALFRR KVVLNDRVKN FYTRLPFQKL TGISIRDKVP
MSGKLISNGF FECERLCDRD PCCTGFGFLN VSQLQGGEVT CLTLNSMGIQ TCNEESGATW
RILDCGSEDT EVHTYPFGWY QKPAVWSDTP SFCPSAALQS LTEEKVTSDS WQTLALSSVI
VDPSIKHFDV AHISTAATSN FSMAQDFCLQ QCSRHQDCLV TTLQIQPGVV RCVFYPDIQN
CIHSLRSHTC WLLLHEEATY IYRKSGIPLV QSDVTSTPSV RIDSFGQLQG GSQVIKVGTA
WKQVYRFLGV PYAAPPLADN RFRAPEVLNW TGSWDATKPR ASCWQPGTRT PTPPQINEDC
LYLNVFVPEN LVSNASVLVF FHNTMEMEGS GGQLTIDGSI LAAVGNFIVV TANYRLGVFG
FLSSGSDEVA GNWGLLDQVA ALTWVQSHIG AFGGDPQRVT LAADRSGADV ASIHLLISRP
TRLQLFRKAL LMGGSALSPA AIISPERAQQ QAAALAKEVG CPTSSIQEVV SCLRQKPANI
LNDAQTKLLA VSGPFHYWGP VVDGQYLREL PSRRLKRPLP VKVDLLIGGS QDDGLINRAK
AVKQFEESQG RTNSKTAFYQ ALQNSLGGED SDARILAAAV WYYSLEHSTD DYASFSRALE
NATRDYFIIC PMVNMASLWA RRTRGNVFMY HVPESYGHGS LELLADVQYA FGLPFYSAYQ
GQFSTEEQSL SLKVMQYFSN FIRSGNPNYP HEFSRKAAEF ATPWPDFIPG AGGESYKELS
AQLPNRQGLK QADCSFWSKY IQTLKDADGA KDAQLTKSEE EDLEVGPGLE EDLSGSLEPV
PKSYSK
//
