QSOX1_MOUSE
ID QSOX1_MOUSE Reviewed; 748 AA.
AC Q8BND5; Q3TDY9; Q3TE19; Q3TR29; Q3UEL4; Q8K041; Q9DBL6;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Sulfhydryl oxidase 1;
DE Short=mSOx;
DE EC=1.8.3.2 {ECO:0000269|PubMed:26819240};
DE AltName: Full=Quiescin Q6;
DE AltName: Full=Skin sulfhydryl oxidase;
DE Flags: Precursor;
GN Name=Qsox1; Synonyms=Qscn6, Sox;
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] (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM 3),
RP AND TISSUE SPECIFICITY.
RX PubMed=12354420; DOI=10.1016/s0923-1811(02)00061-0;
RA Matsuba S., Suga Y., Ishidoh K., Hashimoto Y., Takamori K., Kominami E.,
RA Wilhelm B., Seitz J., Ogawa H.;
RT "Sulfhydryl oxidase (SOx) from mouse epidermis: molecular cloning,
RT nucleotide sequence, and expression of recombinant protein in the cultured
RT cells.";
RL J. Dermatol. Sci. 30:50-62(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Liver, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 137-538 (ISOFORM 3).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, and Salivary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5] {ECO:0007744|PDB:3T58, ECO:0007744|PDB:3T59}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 36-550 IN COMPLEX WITH FAD,
RP COFACTOR, AND DISULFIDE BONDS.
RX PubMed=22801504; DOI=10.1038/nature11267;
RA Alon A., Grossman I., Gat Y., Kodali V.K., DiMaio F., Mehlman T., Haran G.,
RA Baker D., Thorpe C., Fass D.;
RT "The dynamic disulphide relay of quiescin sulphydryl oxidase.";
RL Nature 488:414-418(2012).
RN [6] {ECO:0007744|PDB:5D8I, ECO:0007744|PDB:5D93, ECO:0007744|PDB:5D96}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 36-275, FUNCTION, CATALYTIC
RP ACTIVITY, SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX PubMed=26819240; DOI=10.1093/protein/gzv067;
RA Grossman I., Ilani T., Fleishman S.J., Fass D.;
RT "Overcoming a species-specificity barrier in development of an inhibitory
RT antibody targeting a modulator of tumor stroma.";
RL Protein Eng. Des. Sel. 29:135-147(2016).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 36-550 OF MUTANT ALA-75/THR-122,
RP AND MUTAGENESIS OF HIS-75 AND PRO-122.
RX PubMed=30367560; DOI=10.1002/pro.3537;
RA Javitt G., Grossman-Haham I., Alon A., Resnick E., Mutsafi Y., Ilani T.,
RA Fass D.;
RT "cis-Proline mutants of quiescin sulfhydryl oxidase 1 with altered redox
RT properties undermine extracellular matrix integrity and cell adhesion in
RT fibroblast cultures.";
RL Protein Sci. 28:228-238(2019).
CC -!- FUNCTION: Catalyzes the oxidation of sulfhydryl groups in peptide and
CC protein thiols to disulfides with the reduction of oxygen to hydrogen
CC peroxide (PubMed:26819240). Plays a role in disulfide bond formation in
CC a variety of extracellular proteins (PubMed:26819240). In fibroblasts,
CC required for normal incorporation of laminin into the extracellular
CC matrix, and thereby for normal cell-cell adhesion and cell migration
CC (PubMed:26819240). {ECO:0000269|PubMed:26819240}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR';
CC Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2;
CC Evidence={ECO:0000269|PubMed:26819240};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:22801504};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:22801504};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6IUU3}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O00391}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O00391}. Secreted {ECO:0000269|PubMed:26819240}.
CC Note=A small proportion is secreted, probably via a proteolytic
CC cleavage that removes the membrane anchor.
CC {ECO:0000250|UniProtKB:O00391}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted
CC {ECO:0000269|PubMed:12354420}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BND5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BND5-2; Sequence=VSP_020495, VSP_020496;
CC Name=3;
CC IsoId=Q8BND5-3; Sequence=VSP_020493, VSP_020494;
CC Name=4;
CC IsoId=Q8BND5-4; Sequence=VSP_020491, VSP_020492;
CC -!- TISSUE SPECIFICITY: Detected in skin (at protein level)
CC (PubMed:12354420). Expressed in the seminal vesicles and skin.
CC {ECO:0000269|PubMed:12354420}.
CC -!- PTM: N-glycosylated. O-glycosylated on Thr and Ser residues.
CC {ECO:0000250|UniProtKB:O00391}.
CC -!- SIMILARITY: Belongs to the quiescin-sulfhydryl oxidase (QSOX) family.
CC {ECO:0000305}.
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DR EMBL; AB044284; BAB21936.1; -; mRNA.
DR EMBL; AK004880; BAB23638.1; -; mRNA.
DR EMBL; AK083938; BAC39073.1; -; mRNA.
DR EMBL; AK149465; BAE28897.1; -; mRNA.
DR EMBL; AK163119; BAE37202.1; -; mRNA.
DR EMBL; AK166839; BAE39061.1; -; mRNA.
DR EMBL; AK169877; BAE41429.1; -; mRNA.
DR EMBL; AK169920; BAE41459.1; -; mRNA.
DR EMBL; AK170449; BAE41807.1; -; mRNA.
DR EMBL; BC034131; AAH34131.1; -; mRNA.
DR EMBL; BC076590; AAH76590.1; -; mRNA.
DR CCDS; CCDS15386.1; -. [Q8BND5-1]
DR CCDS; CCDS78713.1; -. [Q8BND5-3]
DR RefSeq; NP_001020116.1; NM_001024945.1. [Q8BND5-1]
DR RefSeq; NP_075757.1; NM_023268.2. [Q8BND5-3]
DR PDB; 3T58; X-ray; 2.40 A; A/B/C/D=36-550.
DR PDB; 3T59; X-ray; 2.80 A; A/B/C/D=36-550.
DR PDB; 5D8I; X-ray; 2.05 A; A/B=36-275.
DR PDB; 5D93; X-ray; 2.20 A; A/D=36-275.
DR PDB; 5D96; X-ray; 2.30 A; A/D=36-275.
DR PDB; 6HF1; X-ray; 1.94 A; A/D=37-274.
DR PDBsum; 3T58; -.
DR PDBsum; 3T59; -.
DR PDBsum; 5D8I; -.
DR PDBsum; 5D93; -.
DR PDBsum; 5D96; -.
DR PDBsum; 6HF1; -.
DR AlphaFoldDB; Q8BND5; -.
DR SMR; Q8BND5; -.
DR BioGRID; 222277; 1.
DR STRING; 10090.ENSMUSP00000035658; -.
DR GlyGen; Q8BND5; 2 sites.
DR iPTMnet; Q8BND5; -.
DR PhosphoSitePlus; Q8BND5; -.
DR CPTAC; non-CPTAC-3297; -.
DR EPD; Q8BND5; -.
DR MaxQB; Q8BND5; -.
DR PaxDb; Q8BND5; -.
DR PeptideAtlas; Q8BND5; -.
DR PRIDE; Q8BND5; -.
DR ProteomicsDB; 300336; -. [Q8BND5-1]
DR ProteomicsDB; 300337; -. [Q8BND5-2]
DR ProteomicsDB; 300338; -. [Q8BND5-3]
DR ProteomicsDB; 300339; -. [Q8BND5-4]
DR ABCD; Q8BND5; 2 sequenced antibodies.
DR Antibodypedia; 47086; 186 antibodies from 33 providers.
DR DNASU; 104009; -.
DR Ensembl; ENSMUST00000035325; ENSMUSP00000035658; ENSMUSG00000033684. [Q8BND5-1]
DR Ensembl; ENSMUST00000111764; ENSMUSP00000107394; ENSMUSG00000033684. [Q8BND5-2]
DR Ensembl; ENSMUST00000194632; ENSMUSP00000142301; ENSMUSG00000033684. [Q8BND5-3]
DR GeneID; 104009; -.
DR KEGG; mmu:104009; -.
DR UCSC; uc007dbo.1; mouse. [Q8BND5-3]
DR UCSC; uc007dbp.1; mouse. [Q8BND5-1]
DR UCSC; uc007dbq.1; mouse. [Q8BND5-4]
DR UCSC; uc011wtx.1; mouse. [Q8BND5-2]
DR CTD; 5768; -.
DR MGI; MGI:1330818; Qsox1.
DR VEuPathDB; HostDB:ENSMUSG00000033684; -.
DR eggNOG; KOG1731; Eukaryota.
DR GeneTree; ENSGT00940000159504; -.
DR HOGENOM; CLU_020182_1_0_1; -.
DR InParanoid; Q8BND5; -.
DR OMA; YLWKAHN; -.
DR OrthoDB; 498515at2759; -.
DR PhylomeDB; Q8BND5; -.
DR TreeFam; TF316749; -.
DR BRENDA; 1.8.3.2; 3474.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 104009; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Qsox1; mouse.
DR PRO; PR:Q8BND5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BND5; protein.
DR Bgee; ENSMUSG00000033684; Expressed in seminal vesicle and 201 other tissues.
DR Genevisible; Q8BND5; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0071949; F:FAD binding; ISO:MGI.
DR GO; GO:0016971; F:flavin-linked sulfhydryl oxidase activity; ISS:UniProtKB.
DR GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB.
DR GO; GO:0085029; P:extracellular matrix assembly; ISO:MGI.
DR GO; GO:0016242; P:negative regulation of macroautophagy; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR Gene3D; 1.20.120.1960; -; 1.
DR Gene3D; 1.20.120.310; -; 1.
DR InterPro; IPR036774; ERV/ALR_sulphydryl_oxid_sf.
DR InterPro; IPR017905; ERV/ALR_sulphydryl_oxidase.
DR InterPro; IPR040986; QSOX_FAD-bd_dom.
DR InterPro; IPR042568; QSOX_FAD-bd_sf.
DR InterPro; IPR041269; QSOX_Trx1.
DR InterPro; IPR039798; Sulfhydryl_oxidase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR22897; PTHR22897; 1.
DR Pfam; PF04777; Evr1_Alr; 1.
DR Pfam; PF18371; FAD_SOX; 1.
DR Pfam; PF18108; QSOX_Trx1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF69000; SSF69000; 1.
DR PROSITE; PS51324; ERV_ALR; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; FAD; Flavoprotein;
KW Glycoprotein; Golgi apparatus; Membrane; Oxidoreductase;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..748
FT /note="Sulfhydryl oxidase 1"
FT /id="PRO_0000249534"
FT TRANSMEM 711..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 33..159
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 399..506
FT /note="ERV/ALR sulfhydryl oxidase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT REGION 581..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 76
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22801504,
FT ECO:0007744|PDB:3T58, ECO:0007744|PDB:3T59"
FT BINDING 411
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22801504,
FT ECO:0007744|PDB:3T58, ECO:0007744|PDB:3T59"
FT BINDING 415
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22801504,
FT ECO:0007744|PDB:3T58, ECO:0007744|PDB:3T59"
FT BINDING 454
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 458
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:O00391"
FT BINDING 481..488
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22801504,
FT ECO:0007744|PDB:3T58, ECO:0007744|PDB:3T59"
FT BINDING 503
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22801504,
FT ECO:0007744|PDB:3T58, ECO:0007744|PDB:3T59"
FT BINDING 506
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:22801504,
FT ECO:0007744|PDB:3T58, ECO:0007744|PDB:3T59"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..76
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:22801504, ECO:0007744|PDB:5D8I,
FT ECO:0007744|PDB:5D93, ECO:0007744|PDB:5D96"
FT DISULFID 104..113
FT /evidence="ECO:0000269|PubMed:22801504,
FT ECO:0000269|PubMed:26819240, ECO:0007744|PDB:3T58,
FT ECO:0007744|PDB:3T59, ECO:0007744|PDB:5D8I,
FT ECO:0007744|PDB:5D93, ECO:0007744|PDB:5D96"
FT DISULFID 396..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000269|PubMed:22801504, ECO:0007744|PDB:3T58,
FT ECO:0007744|PDB:3T59"
FT DISULFID 452..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654"
FT DISULFID 512..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00654,
FT ECO:0000269|PubMed:22801504, ECO:0007744|PDB:3T58,
FT ECO:0007744|PDB:3T59"
FT VAR_SEQ 126..154
FT /note="FFQAFTKNGSGATLPGAGANVQTLRMRLI -> VCEGGATVEWFWPSTQSSV
FT PHFPGTFLGC (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020491"
FT VAR_SEQ 155..748
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020492"
FT VAR_SEQ 567..568
FT /note="VM -> LL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12354420,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_020493"
FT VAR_SEQ 569..748
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12354420,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_020494"
FT VAR_SEQ 660..661
FT /note="VN -> LL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020495"
FT VAR_SEQ 662..748
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020496"
FT MUTAGEN 75
FT /note="H->A: Causes local perturbations of protein folding;
FT when associated with T-122."
FT /evidence="ECO:0000269|PubMed:30367560"
FT MUTAGEN 122
FT /note="P->T: Causes local perturbations of protein folding;
FT when associated with T-122."
FT /evidence="ECO:0000269|PubMed:30367560"
FT CONFLICT 637
FT /note="M -> I (in Ref. 2; BAE41429)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="F -> L (in Ref. 2; BAE41429)"
FT /evidence="ECO:0000305"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:6HF1"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6HF1"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:6HF1"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:6HF1"
FT HELIX 74..89
FT /evidence="ECO:0007829|PDB:6HF1"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:6HF1"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:6HF1"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:6HF1"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:6HF1"
FT HELIX 110..115
FT /evidence="ECO:0007829|PDB:6HF1"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:6HF1"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5D8I"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:6HF1"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:6HF1"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:5D8I"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:6HF1"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:6HF1"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:6HF1"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:6HF1"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:6HF1"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:6HF1"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:6HF1"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:6HF1"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:6HF1"
FT HELIX 259..267
FT /evidence="ECO:0007829|PDB:6HF1"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6HF1"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:3T58"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:3T59"
FT HELIX 304..316
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:3T58"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 327..343
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 348..363
FT /evidence="ECO:0007829|PDB:3T58"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 371..380
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:3T58"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 406..426
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 437..449
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 453..466
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 473..491
FT /evidence="ECO:0007829|PDB:3T58"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:3T58"
FT TURN 509..511
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:3T59"
FT HELIX 528..538
FT /evidence="ECO:0007829|PDB:3T58"
FT HELIX 541..543
FT /evidence="ECO:0007829|PDB:3T58"
FT CONFLICT Q8BND5-4:127
FT /note="C -> Y (in Ref. 2; BAE37202)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 748 AA; 82785 MW; 0499F6B8DAB5A8D1 CRC64;
MRRCGRLSGP PSLLLLLLLL SPLLFSGPGA YAARLSVLYS SSDPLTLLDA DSVRPTVLGS
SSAWAVEFFA SWCGHCIAFA PTWKELANDV KDWRPALNLA VLDCAEETNS AVCREFNIAG
FPTVRFFQAF TKNGSGATLP GAGANVQTLR MRLIDALESH RDTWPPACPP LEPAKLNDID
GFFTRNKADY LALVFEREDS YLGREVTLDL SQYHAVAVRR VLNTESDLVN KFGVTDFPSC
YLLLRNGSVS RVPVLVESRS FYTSYLRGLP GLTRDAPPTT ATPVTADKIA PTVWKFADRS
KIYMADLESA LHYILRVEVG KFSVLEGQRL VALKKFVAVL AKYFPGQPLV QNFLHSINDW
LQKQQKKRIP YSFFKAALDS RKEDAVLTEK VNWVGCQGSE PHFRGFPCSL WVLFHFLTVQ
ANRYSEAHPQ EPADGQEVLQ AMRSYVQFFF GCRDCADHFE QMAAASMHQV RSPSNAILWL
WTSHNRVNAR LSGALSEDPH FPKVQWPPRE LCSACHNELN GQVPLWDLGA TLNFLKAHFS
PANIVIDSSA SRHTGRRGSP EATPELVMDT LKLESRNSVL GHEQAASAES PGATALDVPA
EKPEASGPQE LYTGLRMGGA SPGQGPPERM EDHQRDMQEN APGQQHLSKR DTEALFLPEV
NHLQGPLELR RGGRSPKQLA PILEEEPEAL AIQGQGQWLQ VLGGGISHLD ISLCVGLYSV
SFMGLLAMYT YFRARLRTPK GHASYPTA
