POSTN_HUMAN
ID POSTN_HUMAN Reviewed; 836 AA.
AC Q15063; B1ALD8; C0IMJ1; C0IMJ2; C0IMJ4; D2KRH7; F5H628; Q15064; Q29XZ0;
AC Q3KPJ5; Q5VSY5; Q8IZF9;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Periostin;
DE Short=PN;
DE AltName: Full=Osteoblast-specific factor 2;
DE Short=OSF-2;
DE Flags: Precursor;
GN Name=POSTN; Synonyms=OSF2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Osteosarcoma {ECO:0000269|PubMed:8363580}, and
RC Placenta {ECO:0000269|PubMed:8363580};
RX PubMed=8363580; DOI=10.1042/bj2940271;
RA Takeshita S., Kikuno R., Tezuka K., Amann E.;
RT "Osteoblast-specific factor 2: cloning of a putative bone adhesion protein
RT with homology with the insect protein fasciclin I.";
RL Biochem. J. 294:271-278(1993).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=12235007;
RA Gillan L., Matei D., Fishman D.A., Gerbin C.S., Karlan B.Y., Chang D.D.;
RT "Periostin secreted by epithelial ovarian carcinoma is a ligand for
RT alpha(V)beta(3) and alpha(V)beta(5) integrins and promotes cell motility.";
RL Cancer Res. 62:5358-5364(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5; 6; 7), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RX PubMed=23946676; DOI=10.4137/jcm.s5899;
RA Bai Y., Nakamura M., Zhou G., Li Y., Liu Z., Ozaki T., Mori I., Kakudo K.;
RT "Novel isoforms of periostin expressed in the human thyroid.";
RL Jpn. Clin. Med. 1:13-20(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC TISSUE=Periodontal ligament;
RA Yamada S., Maeda K., Matsubara K., Murakami S.;
RT "Identification and characterization of a novel periodontal ligament-
RT specific periostin isoform.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-798 (ISOFORM 5).
RA Habtemichael N., Schweitzer A., Knauer S., Stauber R.H.;
RT "OSF-2 expression in head and neck squamous cell carcinomas.";
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=11550156;
RX DOI=10.1002/1097-0142(20010815)92:4<843::aid-cncr1391>3.0.co;2-p;
RA Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y.,
RA Fujii Y., Chen L.B.;
RT "Serum level of the periostin, a homologue of an insect cell adhesion
RT molecule, as a prognostic marker in nonsmall cell lung carcinomas.";
RL Cancer 92:843-848(2001).
RN [10]
RP ERRATUM OF PUBMED:11550156.
RA Sasaki H., Dai M., Auclair D., Fukai I., Kiriyama M., Yamakawa Y.,
RA Fujii Y., Chen L.B.;
RL Cancer 95:2580-2580(2002).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=15082792; DOI=10.1128/mcb.24.9.3992-4003.2004;
RA Shao R., Bao S., Bai X., Blanchette C., Anderson R.M., Dang T.,
RA Gishizky M.L., Marks J.R., Wang X.-F.;
RT "Acquired expression of periostin by human breast cancers promotes tumor
RT angiogenesis through up-regulation of vascular endothelial growth factor
RT receptor 2 expression.";
RL Mol. Cell. Biol. 24:3992-4003(2004).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [13]
RP SUBCELLULAR LOCATION, AND GAMMA-CARBOXYGLUTAMATION.
RX PubMed=18450759; DOI=10.1074/jbc.m708029200;
RA Coutu D.L., Wu J.H., Monette A., Rivard G.-E., Blostein M.D., Galipeau J.;
RT "Periostin, a member of a novel family of vitamin K-dependent proteins, is
RT expressed by mesenchymal stromal cells.";
RL J. Biol. Chem. 283:17991-18001(2008).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-599.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP SUBCELLULAR LOCATION, AND LACK OF GAMMA-CARBOXYGLUTAMATION.
RX PubMed=26273833; DOI=10.1371/journal.pone.0135374;
RA Annis D.S., Ma H., Balas D.M., Kumfer K.T., Sandbo N., Potts G.K.,
RA Coon J.J., Mosher D.F.;
RT "Absence of vitamin K-dependent gamma-carboxylation in human periostin
RT extracted from fibrotic lung or secreted from a cell line engineered to
RT optimize gamma-carboxylation.";
RL PLoS ONE 10:E0135374-E0135374(2015).
RN [17] {ECO:0007744|PDB:5WT7}
RP STRUCTURE BY NMR OF 496-632.
RX PubMed=29086898; DOI=10.1007/s12104-017-9786-z;
RA Yun H., Kim E.H., Lee C.W.;
RT "1H, 13C, and 15N resonance assignments of FAS1-IV domain of human
RT periostin, a component of extracellular matrix proteins.";
RL Biomol. NMR. Assign. 12:95-98(2018).
RN [18] {ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 22-631, SUBUNIT, DISULFIDE BONDS,
RP CYSTEINYLATION AT CYS-60, AND MUTAGENESIS OF CYS-60 AND 463-ARG--ALA-465.
RX PubMed=29754429; DOI=10.1002/1873-3468.13091;
RA Liu J., Zhang J., Xu F., Lin Z., Li Z., Liu H.;
RT "Structural characterizations of human periostin dimerization and
RT cysteinylation.";
RL FEBS Lett. 592:1789-1803(2018).
CC -!- FUNCTION: Induces cell attachment and spreading and plays a role in
CC cell adhesion (PubMed:12235007). Enhances incorporation of BMP1 in the
CC fibronectin matrix of connective tissues, and subsequent proteolytic
CC activation of lysyl oxidase LOX (By similarity).
CC {ECO:0000250|UniProtKB:Q62009, ECO:0000269|PubMed:12235007}.
CC -!- SUBUNIT: Homodimer (PubMed:29754429). Interacts with BMP1 and
CC fibronectin. {ECO:0000250|UniProtKB:Q62009,
CC ECO:0000269|PubMed:29754429}.
CC -!- INTERACTION:
CC Q15063; Q15582: TGFBI; NbExp=7; IntAct=EBI-7067070, EBI-10236573;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:Q62009}.
CC Secreted {ECO:0000269|PubMed:18450759, ECO:0000269|PubMed:26273833}.
CC Secreted, extracellular space, extracellular matrix
CC {ECO:0000269|PubMed:12235007, ECO:0000269|PubMed:18450759}.
CC Note=Colocalizes with BMP1 in the Golgi.
CC {ECO:0000250|UniProtKB:Q62009}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1 {ECO:0000269|PubMed:8363580}; Synonyms=OSF-2OS
CC {ECO:0000303|PubMed:8363580};
CC IsoId=Q15063-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:8363580}; Synonyms=OSF-2p1;
CC IsoId=Q15063-2; Sequence=VSP_050005;
CC Name=3 {ECO:0000269|PubMed:12235007};
CC IsoId=Q15063-3; Sequence=VSP_050669, VSP_050670;
CC Name=4;
CC IsoId=Q15063-4; Sequence=VSP_050005, VSP_050670;
CC Name=5;
CC IsoId=Q15063-5; Sequence=VSP_050669;
CC Name=6;
CC IsoId=Q15063-6; Sequence=VSP_055183;
CC Name=7;
CC IsoId=Q15063-7; Sequence=VSP_055183, VSP_050670;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in aorta,
CC stomach, lower gastrointestinal tract, placenta, uterus, thyroid tissue
CC and breast. Up-regulated in epithelial ovarian tumors. Not expressed in
CC normal ovaries. Also highly expressed at the tumor periphery of lung
CC carcinoma tissue but not within the tumor. Overexpressed in breast
CC cancers. {ECO:0000269|PubMed:11550156, ECO:0000269|PubMed:12235007,
CC ECO:0000269|PubMed:15082792, ECO:0000269|PubMed:23946676}.
CC -!- PTM: Gamma-carboxylation is controversial. Gamma-carboxyglutamated;
CC gamma-carboxyglutamate residues are formed by vitamin K dependent
CC carboxylation; this may be required for calcium binding
CC (PubMed:18450759). According to a more recent report, does not contain
CC vitamin K-dependent gamma-carboxyglutamate residues (PubMed:26273833).
CC {ECO:0000269|PubMed:18450759, ECO:0000269|PubMed:26273833}.
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DR EMBL; D13665; BAA02836.1; -; mRNA.
DR EMBL; D13666; BAA02837.1; -; mRNA.
DR EMBL; AY140646; AAN17733.1; -; mRNA.
DR EMBL; EU262883; ABY86630.1; -; mRNA.
DR EMBL; EU262884; ABY86631.1; -; mRNA.
DR EMBL; EU262886; ABY86633.1; -; mRNA.
DR EMBL; AY918092; AAY15840.1; -; mRNA.
DR EMBL; AL138679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL646087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08590.1; -; Genomic_DNA.
DR EMBL; BC106709; AAI06710.1; -; mRNA.
DR EMBL; BC106710; AAI06711.1; -; mRNA.
DR EMBL; GU354210; ADA79517.1; -; mRNA.
DR CCDS; CCDS45034.1; -. [Q15063-2]
DR CCDS; CCDS53864.1; -. [Q15063-3]
DR CCDS; CCDS66530.1; -. [Q15063-6]
DR CCDS; CCDS66531.1; -. [Q15063-5]
DR CCDS; CCDS9364.1; -. [Q15063-1]
DR PIR; S36110; S36110.
DR PIR; S36111; S36111.
DR RefSeq; NP_001129406.1; NM_001135934.1. [Q15063-2]
DR RefSeq; NP_001129407.1; NM_001135935.1. [Q15063-3]
DR RefSeq; NP_001129408.1; NM_001135936.1. [Q15063-4]
DR RefSeq; NP_001273594.1; NM_001286665.1. [Q15063-5]
DR RefSeq; NP_001273595.1; NM_001286666.1. [Q15063-6]
DR RefSeq; NP_001273596.1; NM_001286667.1. [Q15063-7]
DR RefSeq; NP_001317446.1; NM_001330517.1.
DR RefSeq; NP_006466.2; NM_006475.2. [Q15063-1]
DR PDB; 5WT7; NMR; -; A=496-632.
DR PDB; 5YJG; X-ray; 2.40 A; A=22-631.
DR PDB; 5YJH; X-ray; 2.96 A; A=17-631.
DR PDBsum; 5WT7; -.
DR PDBsum; 5YJG; -.
DR PDBsum; 5YJH; -.
DR AlphaFoldDB; Q15063; -.
DR SMR; Q15063; -.
DR BioGRID; 115875; 7.
DR IntAct; Q15063; 5.
DR MINT; Q15063; -.
DR STRING; 9606.ENSP00000369071; -.
DR GlyConnect; 1599; 66 N-Linked glycans (1 site).
DR GlyGen; Q15063; 2 sites, 62 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q15063; -.
DR PhosphoSitePlus; Q15063; -.
DR BioMuta; POSTN; -.
DR DMDM; 93138709; -.
DR EPD; Q15063; -.
DR jPOST; Q15063; -.
DR MassIVE; Q15063; -.
DR MaxQB; Q15063; -.
DR PaxDb; Q15063; -.
DR PeptideAtlas; Q15063; -.
DR PRIDE; Q15063; -.
DR ProteomicsDB; 27060; -.
DR ProteomicsDB; 3153; -.
DR ProteomicsDB; 60417; -. [Q15063-1]
DR ProteomicsDB; 60418; -. [Q15063-2]
DR ProteomicsDB; 60419; -. [Q15063-3]
DR ProteomicsDB; 60420; -. [Q15063-4]
DR ABCD; Q15063; 4 sequenced antibodies.
DR Antibodypedia; 2020; 669 antibodies from 47 providers.
DR DNASU; 10631; -.
DR Ensembl; ENST00000379742.4; ENSP00000369066.4; ENSG00000133110.15. [Q15063-2]
DR Ensembl; ENST00000379743.8; ENSP00000369067.4; ENSG00000133110.15. [Q15063-5]
DR Ensembl; ENST00000379747.9; ENSP00000369071.4; ENSG00000133110.15. [Q15063-1]
DR Ensembl; ENST00000541179.5; ENSP00000437959.1; ENSG00000133110.15. [Q15063-3]
DR Ensembl; ENST00000541481.5; ENSP00000437953.1; ENSG00000133110.15. [Q15063-6]
DR GeneID; 10631; -.
DR KEGG; hsa:10631; -.
DR MANE-Select; ENST00000379747.9; ENSP00000369071.4; NM_006475.3; NP_006466.2.
DR UCSC; uc001uwo.5; human. [Q15063-1]
DR CTD; 10631; -.
DR DisGeNET; 10631; -.
DR GeneCards; POSTN; -.
DR HGNC; HGNC:16953; POSTN.
DR HPA; ENSG00000133110; Tissue enhanced (skin, stomach).
DR MIM; 608777; gene.
DR neXtProt; NX_Q15063; -.
DR OpenTargets; ENSG00000133110; -.
DR PharmGKB; PA134900304; -.
DR VEuPathDB; HostDB:ENSG00000133110; -.
DR eggNOG; KOG1437; Eukaryota.
DR GeneTree; ENSGT00530000063860; -.
DR HOGENOM; CLU_017611_0_0_1; -.
DR InParanoid; Q15063; -.
DR OMA; VFVYRTX; -.
DR PhylomeDB; Q15063; -.
DR TreeFam; TF316269; -.
DR PathwayCommons; Q15063; -.
DR SignaLink; Q15063; -.
DR SIGNOR; Q15063; -.
DR BioGRID-ORCS; 10631; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; POSTN; human.
DR GeneWiki; Periostin; -.
DR GeneWiki; POSTN; -.
DR GenomeRNAi; 10631; -.
DR Pharos; Q15063; Tbio.
DR PRO; PR:Q15063; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q15063; protein.
DR Bgee; ENSG00000133110; Expressed in periodontal ligament and 175 other tissues.
DR ExpressionAtlas; Q15063; baseline and differential.
DR Genevisible; Q15063; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:BHF-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0071307; P:cellular response to vitamin K; IDA:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0009888; P:tissue development; IEA:Ensembl.
DR Gene3D; 2.30.180.10; -; 4.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR036378; FAS1_dom_sf.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR016666; TGFBI/POSTN.
DR Pfam; PF02469; Fasciclin; 4.
DR PIRSF; PIRSF016553; BIGH3_OSF2; 1.
DR SMART; SM00554; FAS1; 4.
DR SUPFAM; SSF82153; SSF82153; 4.
DR PROSITE; PS51041; EMI; 1.
DR PROSITE; PS50213; FAS1; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Disulfide bond;
KW Extracellular matrix; Gamma-carboxyglutamic acid; Glycoprotein;
KW Golgi apparatus; Heparin-binding; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..836
FT /note="Periostin"
FT /id="PRO_0000008789"
FT DOMAIN 40..94
FT /note="EMI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00384"
FT DOMAIN 97..230
FT /note="FAS1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 234..365
FT /note="FAS1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 368..492
FT /note="FAS1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT DOMAIN 496..628
FT /note="FAS1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082"
FT MOD_RES 60
FT /note="S-cysteinyl cysteine"
FT /evidence="ECO:0000269|PubMed:29754429"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT DISULFID 44..80
FT /evidence="ECO:0000269|PubMed:29754429,
FT ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH"
FT DISULFID 69..333
FT /evidence="ECO:0000269|PubMed:29754429,
FT ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH"
FT DISULFID 79..92
FT /evidence="ECO:0000269|PubMed:29754429,
FT ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH"
FT DISULFID 208..311
FT /evidence="ECO:0000269|PubMed:29754429,
FT ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH"
FT DISULFID 467..472
FT /evidence="ECO:0000269|PubMed:29754429,
FT ECO:0007744|PDB:5YJG, ECO:0007744|PDB:5YJH"
FT VAR_SEQ 670..757
FT /note="TTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPEFRLIKEGETIT
FT EVIHGEPIIKKYTKIIDGVPVEITEKETREERIITG -> S (in isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:23946676"
FT /id="VSP_055183"
FT VAR_SEQ 670..727
FT /note="TTKIITKVVEPKIKVIEGSLQPIIKTEGPTLTKVKIEGEPEFRLIKEGETIT
FT EVIHGE -> K (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8363580, ECO:0000303|Ref.4"
FT /id="VSP_050005"
FT VAR_SEQ 670..697
FT /note="TTKIITKVVEPKIKVIEGSLQPIIKTEG -> R (in isoform 3 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:12235007,
FT ECO:0000303|PubMed:23946676, ECO:0000303|Ref.8"
FT /id="VSP_050669"
FT VAR_SEQ 783..810
FT /note="Missing (in isoform 3, isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:12235007,
FT ECO:0000303|PubMed:23946676, ECO:0000303|Ref.4"
FT /id="VSP_050670"
FT VARIANT 339
FT /note="T -> I (in dbSNP:rs9594223)"
FT /id="VAR_049115"
FT VARIANT 814
FT /note="V -> M (in dbSNP:rs9547952)"
FT /id="VAR_049116"
FT MUTAGEN 60
FT /note="C->A: No effect on homodimerization."
FT /evidence="ECO:0000269|PubMed:29754429"
FT MUTAGEN 463..465
FT /note="RTA->NTS: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:29754429"
FT CONFLICT 290
FT /note="I -> F (in Ref. 1; BAA02836/BAA02837, 3; ABY86630/
FT ABY86631/ABY86633 and 4; AAY15840)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="D -> V (in Ref. 1; BAA02836/BAA02837, 3; ABY86630/
FT ABY86631/ABY86633 and 4; AAY15840)"
FT /evidence="ECO:0000305"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 55..62
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:5YJG"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 269..274
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 276..281
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 294..302
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 326..334
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 346..353
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 382..390
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 422..430
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 456..461
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 481..490
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 499..505
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 510..518
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 522..526
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:5WT7"
FT STRAND 531..536
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 538..542
FT /evidence="ECO:0007829|PDB:5YJG"
FT TURN 543..546
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 547..553
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 558..564
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 567..570
FT /evidence="ECO:0007829|PDB:5YJG"
FT HELIX 574..576
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 582..586
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 590..598
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 601..606
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:5YJG"
FT STRAND 619..626
FT /evidence="ECO:0007829|PDB:5YJG"
SQ SEQUENCE 836 AA; 93314 MW; 55E7B82D094824FD CRC64;
MIPFLPMFSL LLLLIVNPIN ANNHYDKILA HSRIRGRDQG PNVCALQQIL GTKKKYFSTC
KNWYKKSICG QKTTVLYECC PGYMRMEGMK GCPAVLPIDH VYGTLGIVGA TTTQRYSDAS
KLREEIEGKG SFTYFAPSNE AWDNLDSDIR RGLESNVNVE LLNALHSHMI NKRMLTKDLK
NGMIIPSMYN NLGLFINHYP NGVVTVNCAR IIHGNQIATN GVVHVIDRVL TQIGTSIQDF
IEAEDDLSSF RAAAITSDIL EALGRDGHFT LFAPTNEAFE KLPRGVLERI MGDKVASEAL
MKYHILNTLQ CSESIMGGAV FETLEGNTIE IGCDGDSITV NGIKMVNKKD IVTNNGVIHL
IDQVLIPDSA KQVIELAGKQ QTTFTDLVAQ LGLASALRPD GEYTLLAPVN NAFSDDTLSM
DQRLLKLILQ NHILKVKVGL NELYNGQILE TIGGKQLRVF VYRTAVCIEN SCMEKGSKQG
RNGAIHIFRE IIKPAEKSLH EKLKQDKRFS TFLSLLEAAD LKELLTQPGD WTLFVPTNDA
FKGMTSEEKE ILIRDKNALQ NIILYHLTPG VFIGKGFEPG VTNILKTTQG SKIFLKEVND
TLLVNELKSK ESDIMTTNGV IHVVDKLLYP ADTPVGNDQL LEILNKLIKY IQIKFVRGST
FKEIPVTVYT TKIITKVVEP KIKVIEGSLQ PIIKTEGPTL TKVKIEGEPE FRLIKEGETI
TEVIHGEPII KKYTKIIDGV PVEITEKETR EERIITGPEI KYTRISTGGG ETEETLKKLL
QEEVTKVTKF IEGGDGHLFE DEEIKRLLQG DTPVRKLQAN KKVQGSRRRL REGRSQ
