FBN1_MOUSE
ID FBN1_MOUSE Reviewed; 2873 AA.
AC Q61554; A2AQ53; Q60826;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Fibrillin-1 {ECO:0000250|UniProtKB:P35555};
DE Contains:
DE RecName: Full=Asprosin {ECO:0000250|UniProtKB:P35555};
DE Flags: Precursor;
GN Name=Fbn1 {ECO:0000312|MGI:MGI:95489};
GN Synonyms=Fbn-1 {ECO:0000303|PubMed:7829516};
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=7829516; DOI=10.1074/jbc.270.4.1798;
RA Yin W., Germiller J., Sanguineti C., Smiley E., Pangilinan T., Pereira L.,
RA Ramirez F., Bonadio J.;
RT "Primary structure and developmental expression of Fbn-1, the mouse
RT fibrillin gene.";
RL J. Biol. Chem. 270:1798-1806(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Kidney;
RA Ota K., Kumar A., Wada J., Liu Z., Kanwar Y.S.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=16407178; DOI=10.1074/jbc.m511599200;
RA Carta L., Pereira L., Arteaga-Solis E., Lee-Arteaga S.Y., Lenart B.,
RA Starcher B., Merkel C.A., Sukoyan M., Kerkis A., Hazeki N., Keene D.R.,
RA Sakai L.Y., Ramirez F.;
RT "Fibrillins 1 and 2 perform partially overlapping functions during aortic
RT development.";
RL J. Biol. Chem. 281:8016-8023(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2705 AND SER-2711, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, 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 [6]
RP INTERACTION WITH THSD4.
RX PubMed=19940141; DOI=10.1074/jbc.m109.076919;
RA Tsutsui K., Manabe R., Yamada T., Nakano I., Oguri Y., Keene D.R.,
RA Sengle G., Sakai L.Y., Sekiguchi K.;
RT "ADAMTSL-6 is a novel extracellular matrix protein that binds to fibrillin-
RT 1 and promotes fibrillin-1 fibril formation.";
RL J. Biol. Chem. 285:4870-4882(2010).
RN [7]
RP FUNCTION.
RX PubMed=20855508; DOI=10.1083/jcb.201003089;
RA Nistala H., Lee-Arteaga S., Smaldone S., Siciliano G., Carta L., Ono R.N.,
RA Sengle G., Arteaga-Solis E., Levasseur R., Ducy P., Sakai L.Y.,
RA Karsenty G., Ramirez F.;
RT "Fibrillin-1 and -2 differentially modulate endogenous TGF-{beta} and BMP
RT bioavailability during bone formation.";
RL J. Cell Biol. 190:1107-1121(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24039232; DOI=10.1242/jcs.127571;
RA Tiedemann K., Boraschi-Diaz I., Rajakumar I., Kaur J., Roughley P.,
RA Reinhardt D.P., Komarova S.V.;
RT "Fibrillin-1 directly regulates osteoclast formation and function by a dual
RT mechanism.";
RL J. Cell Sci. 126:4187-4194(2013).
RN [9]
RP DEVELOPMENTAL STAGE (ASPROSIN), AND TISSUE SPECIFICITY (ASPROSIN).
RX PubMed=27087445; DOI=10.1016/j.cell.2016.02.063;
RA Romere C., Duerrschmid C., Bournat J., Constable P., Jain M., Xia F.,
RA Saha P.K., Del Solar M., Zhu B., York B., Sarkar P., Rendon D.A.,
RA Gaber M.W., LeMaire S.A., Coselli J.S., Milewicz D.M., Sutton V.R.,
RA Butte N.F., Moore D.D., Chopra A.R.;
RT "Asprosin, a fasting-induced glucogenic protein hormone.";
RL Cell 165:566-579(2016).
RN [10]
RP FUNCTION (ASPROSIN), AND DISRUPTION PHENOTYPE (ASPROSIN).
RX PubMed=29106398; DOI=10.1038/nm.4432;
RA Duerrschmid C., He Y., Wang C., Li C., Bournat J.C., Romere C., Saha P.K.,
RA Lee M.E., Phillips K.J., Jain M., Jia P., Zhao Z., Farias M., Wu Q.,
RA Milewicz D.M., Sutton V.R., Moore D.D., Butte N.F., Krashes M.J., Xu Y.,
RA Chopra A.R.;
RT "Asprosin is a centrally acting orexigenic hormone.";
RL Nat. Med. 23:1444-1453(2017).
RN [11]
RP FUNCTION (ASPROSIN).
RX PubMed=31798959; DOI=10.1038/s41421-019-0122-x;
RA Wei F., Long A., Wang Y.;
RT "The Asprosin-OLFR734 hormonal signaling axis modulates male fertility.";
RL Cell Discov. 5:55-55(2019).
RN [12]
RP FUNCTION (ASPROSIN).
RX PubMed=31230984; DOI=10.1016/j.cmet.2019.05.022;
RA Li E., Shan H., Chen L., Long A., Zhang Y., Liu Y., Jia L., Wei F., Han J.,
RA Li T., Liu X., Deng H., Wang Y.;
RT "OLFR734 mediates glucose metabolism as a receptor of asprosin.";
RL Cell Metab. 30:319-328(2019).
RN [13]
RP FUNCTION (ASPROSIN).
RX PubMed=30997682; DOI=10.1002/jcp.28694;
RA Jung T.W., Kim H.C., Kim H.U., Park T., Park J., Kim U., Kim M.K.,
RA Jeong J.H.;
RT "Asprosin attenuates insulin signaling pathway through PKCdelta-activated
RT ER stress and inflammation in skeletal muscle.";
RL J. Cell. Physiol. 234:20888-20899(2019).
RN [14]
RP FUNCTION (ASPROSIN).
RX PubMed=32337066; DOI=10.1038/s41421-020-0152-4;
RA Liu Y., Long A., Chen L., Jia L., Wang Y.;
RT "The Asprosin-OLFR734 module regulates appetitive behaviors.";
RL Cell Discov. 6:19-19(2020).
RN [15]
RP BIOTECHNOLOGY (ASPROSIN).
RX PubMed=33904407; DOI=10.7554/elife.63784;
RA Mishra I., Duerrschmid C., Ku Z., He Y., Xie W., Silva E.S., Hoffman J.,
RA Xin W., Zhang N., Xu Y., An Z., Chopra A.R.;
RT "Asprosin-neutralizing antibodies as a treatment for metabolic syndrome.";
RL Elife 10:0-0(2021).
RN [16]
RP FUNCTION (ASPROSIN).
RX PubMed=33705351; DOI=10.1530/joe-20-0503;
RA Miao Y., Qin H., Zhong Y., Huang K., Rao C.;
RT "Novel adipokine asprosin modulates browning and adipogenesis in white
RT adipose tissue.";
RL J. Endocrinol. 249:83-93(2021).
CC -!- FUNCTION: [Fibrillin-1]: Structural component of the 10-12 nm diameter
CC microfibrils of the extracellular matrix, which conveys both structural
CC and regulatory properties to load-bearing connective tissues.
CC Fibrillin-1-containing microfibrils provide long-term force bearing
CC structural support. In tissues such as the lung, blood vessels and
CC skin, microfibrils form the periphery of the elastic fiber, acting as a
CC scaffold for the deposition of elastin. In addition, microfibrils can
CC occur as elastin-independent networks in tissues such as the ciliary
CC zonule, tendon, cornea and glomerulus where they provide tensile
CC strength and have anchoring roles. Fibrillin-1 also plays a key role in
CC tissue homeostasis through specific interactions with growth factors,
CC such as the bone morphogenetic proteins (BMPs), growth and
CC differentiation factors (GDFs) and latent transforming growth factor-
CC beta-binding proteins (LTBPs), cell-surface integrins and other
CC extracellular matrix protein and proteoglycan components (By
CC similarity). Regulates osteoblast maturation by controlling TGF-beta
CC bioavailability and calibrating TGF-beta and BMP levels, respectively
CC (PubMed:20855508). Negatively regulates osteoclastogenesis by binding
CC and sequestering an osteoclast differentiation and activation factor
CC TNFSF11. This leads to disruption of TNFSF11-induced Ca(2+) signaling
CC and impairment of TNFSF11-mediated nuclear translocation and activation
CC of transcription factor NFATC1 which regulates genes important for
CC osteoclast differentiation and function (PubMed:24039232). Mediates
CC cell adhesion via its binding to cell surface receptors integrins
CC ITGAV:ITGB3 and ITGA5:ITGB1. Binds heparin and this interaction plays
CC an important role in the assembly of microfibrils (By similarity).
CC {ECO:0000250|UniProtKB:P35555, ECO:0000269|PubMed:20855508,
CC ECO:0000269|PubMed:24039232}.
CC -!- FUNCTION: [Asprosin]: Adipokine secreted by white adipose tissue that
CC plays an important regulatory role in the glucose metabolism of liver,
CC muscle and pancreas (PubMed:31230984, PubMed:30997682). Hormone that
CC targets the liver in response to fasting to increase plasma glucose
CC levels (PubMed:31230984). Binds the olfactory receptor Olfr734 at the
CC surface of hepatocytes and promotes hepatocyte glucose release by
CC activating the protein kinase A activity in the liver, resulting in
CC rapid glucose release into the circulation (PubMed:31230984). May act
CC as a regulator of adaptive thermogenesis by inhibiting browning and
CC energy consumption, while increasing lipid deposition in white adipose
CC tissue (PubMed:33705351). Also acts as an orexigenic hormone that
CC increases appetite: crosses the blood brain barrier and exerts effects
CC on the hypothalamus (PubMed:29106398). In the arcuate nucleus of the
CC hypothalamus, asprosin directly activates orexigenic AgRP neurons and
CC indirectly inhibits anorexigenic POMC neurons, resulting in appetite
CC stimulation (PubMed:29106398, PubMed:32337066). Activates orexigenic
CC AgRP neurons via binding to the olfactory receptor Olfr734
CC (PubMed:32337066). May also play a role in sperm motility in testis via
CC interaction with Olfr734 receptor (PubMed:31798959).
CC {ECO:0000269|PubMed:29106398, ECO:0000269|PubMed:30997682,
CC ECO:0000269|PubMed:31230984, ECO:0000269|PubMed:31798959,
CC ECO:0000269|PubMed:32337066, ECO:0000269|PubMed:33705351}.
CC -!- SUBUNIT: [Fibrillin-1]: Interacts with COL16A1. Interacts with integrin
CC alpha-V/beta-3. Interacts with ADAMTS10; this interaction promotes
CC microfibril assembly (By similarity). Interacts with THSD4; this
CC interaction promotes fibril formation (PubMed:19940141). Interacts (via
CC N-terminal domain) with FBLN2 and FBLN5. Interacts with ELN. Forms a
CC ternary complex with ELN and FBLN2 or FBLN5 and a significant
CC interaction with ELN seen only in the presence of FBLN2 or FBLN5.
CC Interacts (via N-terminal domain) with LTBP2 (via C-terminal domain) in
CC a Ca(+2)-dependent manner. Interacts (via N-terminal domain) with LTBP1
CC (via C-terminal domain). Interacts with integrins ITGA5:ITGB1,
CC ITGAV:ITGB3 and ITGAV:ITGB6. Interacts (via N-terminal domain) with
CC BMP2, BMP4, BMP7, BMP10 and GDF5. Interacts (via N-terminal domain)
CC with MFAP2 and MFAP5. Interacts with ADAMTSL5. Interacts with MFAP4.
CC Interacts (via N-terminal domain) with TNFSF11 in a Ca(+2)-dependent
CC manner (By similarity). Interacts (via N-terminal domain) with EFEMP2;
CC this interaction inhibits EFEMP2 binding to LOX and ELN (By
CC similarity). {ECO:0000250|UniProtKB:P35555,
CC ECO:0000269|PubMed:19940141}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P35555}.
CC Note=Fibrillin-1 and Asprosin chains are still linked together during
CC the secretion from cells, but are subsequently separated by furin.
CC {ECO:0000250|UniProtKB:P35555}.
CC -!- SUBCELLULAR LOCATION: [Fibrillin-1]: Secreted, extracellular space,
CC extracellular matrix {ECO:0000269|PubMed:24039232}.
CC -!- SUBCELLULAR LOCATION: [Asprosin]: Secreted
CC {ECO:0000250|UniProtKB:P35555}. Note=Secreted by white adipose tissue
CC and circulates in the plasma. {ECO:0000250|UniProtKB:P35555}.
CC -!- TISSUE SPECIFICITY: [Fibrillin-1]: Strongly expressed during the first
CC week of osteoblast differentiation. {ECO:0000269|PubMed:24039232}.
CC -!- TISSUE SPECIFICITY: [Asprosin]: Secreted by white adipose tissue (at
CC protein level). {ECO:0000269|PubMed:27087445}.
CC -!- DEVELOPMENTAL STAGE: [Asprosin]: Displays circadian oscillation with an
CC acute decrease in levels coinciding with the onset of feeding (at
CC protein level) (PubMed:27087445). {ECO:0000269|PubMed:27087445}.
CC -!- PTM: Cleavage of N- and C-terminus by furin is required for
CC incorporation into the extracellular matrix and assembly into
CC microfibrils. The C-terminus, which corresponds to the Asprosin chain,
CC was initially thought to constitute a propeptide. Fibrillin-1 and
CC Asprosin chains are still linked together during the secretion from
CC cells, but are subsequently separated by furin, an essential step for
CC incorporation of Fibrillin-1 into the nascent microfibrils.
CC {ECO:0000250|UniProtKB:P35555}.
CC -!- PTM: [Fibrillin-1]: Forms intermolecular disulfide bonds either with
CC other fibrillin-1 molecules or with other components of the
CC microfibrils. {ECO:0000250|UniProtKB:P35555}.
CC -!- PTM: O-glycosylated on serine residues by POGLUT2 and POGLUT3 which is
CC necessary for efficient protein secretion.
CC {ECO:0000250|UniProtKB:P35555}.
CC -!- DISRUPTION PHENOTYPE: Neonatal lethality due to ruptured aortic
CC aneurysm, impaired pulmonary function and/or diaphragmatic collapse.
CC Neonatal aorta show a disorganized and poorly developed medial layer
CC but normal levels of elastin cross-links.
CC {ECO:0000269|PubMed:16407178}.
CC -!- DISRUPTION PHENOTYPE: [Asprosin]: Mice lacking Asprosin show low
CC appetite, reduced adiposity and protection from diet-induced obesity.
CC {ECO:0000269|PubMed:29106398}.
CC -!- BIOTECHNOLOGY: [Asprosin]: Attractive therapeutic target for type II
CC diabetes and metabolic syndrome (PubMed:33904407). Inactivation by
CC monoclonal antibodies that recognize unique Asprosin epitopes reduces
CC appetite, body weight and blood glucose levels in mice with metabolic
CC syndrome, leading to mitigate metabolic syndrome (PubMed:33904407).
CC {ECO:0000269|PubMed:33904407}.
CC -!- SIMILARITY: Belongs to the fibrillin family. {ECO:0000305}.
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DR EMBL; L29454; AAA56840.1; -; mRNA.
DR EMBL; U22493; AAA64217.1; -; mRNA.
DR EMBL; AL844547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS16676.1; -.
DR PIR; A55624; A55624.
DR RefSeq; NP_032019.2; NM_007993.2.
DR RefSeq; XP_006498810.1; XM_006498747.1.
DR BMRB; Q61554; -.
DR SMR; Q61554; -.
DR IntAct; Q61554; 1.
DR STRING; 10090.ENSMUSP00000028633; -.
DR GlyGen; Q61554; 15 sites.
DR iPTMnet; Q61554; -.
DR PhosphoSitePlus; Q61554; -.
DR jPOST; Q61554; -.
DR MaxQB; Q61554; -.
DR PaxDb; Q61554; -.
DR PeptideAtlas; Q61554; -.
DR PRIDE; Q61554; -.
DR ProteomicsDB; 267344; -.
DR Antibodypedia; 2908; 513 antibodies from 37 providers.
DR DNASU; 14118; -.
DR Ensembl; ENSMUST00000028633; ENSMUSP00000028633; ENSMUSG00000027204.
DR Ensembl; ENSMUST00000103234; ENSMUSP00000099524; ENSMUSG00000027204.
DR GeneID; 14118; -.
DR KEGG; mmu:14118; -.
DR UCSC; uc008mco.1; mouse.
DR CTD; 2200; -.
DR MGI; MGI:95489; Fbn1.
DR VEuPathDB; HostDB:ENSMUSG00000027204; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00950000183158; -.
DR InParanoid; Q61554; -.
DR OMA; YLQGSAC; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q61554; -.
DR TreeFam; TF316849; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-1566948; Elastic fibre formation.
DR Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
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-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 14118; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Fbn1; mouse.
DR PRO; PR:Q61554; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q61554; protein.
DR Bgee; ENSMUSG00000027204; Expressed in external carotid artery and 259 other tissues.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0001527; C:microfibril; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0034199; P:activation of protein kinase A activity; ISS:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISO:MGI.
DR GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0048048; P:embryonic eye morphogenesis; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISO:MGI.
DR GO; GO:0001822; P:kidney development; ISO:MGI.
DR GO; GO:0001656; P:metanephros development; ISO:MGI.
DR GO; GO:1903444; P:negative regulation of brown fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IDA:UniProtKB.
DR GO; GO:2001205; P:negative regulation of osteoclast development; IDA:UniProtKB.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:UniProtKB.
DR GO; GO:0032100; P:positive regulation of appetite; IDA:UniProtKB.
DR GO; GO:0048050; P:post-embryonic eye morphogenesis; IEA:Ensembl.
DR GO; GO:0010737; P:protein kinase A signaling; ISS:UniProtKB.
DR GO; GO:0035582; P:sequestering of BMP in extracellular matrix; IMP:BHF-UCL.
DR GO; GO:0035583; P:sequestering of TGFbeta in extracellular matrix; IMP:BHF-UCL.
DR GO; GO:0001501; P:skeletal system development; ISO:MGI.
DR Gene3D; 3.90.290.10; -; 9.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR011398; FBN.
DR InterPro; IPR040872; Fibrillin_U_N.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR PANTHER; PTHR24039:SF22; PTHR24039:SF22; 7.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 40.
DR Pfam; PF18193; Fibrillin_U_N; 1.
DR Pfam; PF00683; TB; 9.
DR SMART; SM00181; EGF; 46.
DR SMART; SM00179; EGF_CA; 44.
DR SUPFAM; SSF57184; SSF57184; 11.
DR SUPFAM; SSF57581; SSF57581; 9.
DR PROSITE; PS00010; ASX_HYDROXYL; 43.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 38.
DR PROSITE; PS50026; EGF_3; 45.
DR PROSITE; PS01187; EGF_CA; 43.
DR PROSITE; PS51364; TB; 9.
PE 1: Evidence at protein level;
KW Calcium; Disulfide bond; EGF-like domain; Extracellular matrix;
KW Glycoprotein; Hormone; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT PROPEP 25..44
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT /id="PRO_0000436883"
FT CHAIN 45..2733
FT /note="Fibrillin-1"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT /id="PRO_0000007582"
FT CHAIN 2734..2873
FT /note="Asprosin"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT /id="PRO_0000436884"
FT DOMAIN 81..112
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 115..146
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 147..178
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 184..236
FT /note="TB 1"
FT DOMAIN 246..287
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 288..329
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 334..389
FT /note="TB 2"
FT DOMAIN 451..491
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 492..531
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 532..573
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 574..614
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 615..655
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 661..713
FT /note="TB 3"
FT DOMAIN 725..766
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 767..808
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 809..848
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 853..904
FT /note="TB 4"
FT DOMAIN 912..953
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 958..1010
FT /note="TB 5"
FT DOMAIN 1030..1071
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1072..1114
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1115..1156
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1157..1198
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1199..1239
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1240..1281
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1282..1323
FT /note="EGF-like 21; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1324..1364
FT /note="EGF-like 22; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1365..1405
FT /note="EGF-like 23; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1406..1447
FT /note="EGF-like 24; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1448..1488
FT /note="EGF-like 25; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1489..1529
FT /note="EGF-like 26; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1534..1591
FT /note="TB 6"
FT DOMAIN 1608..1649
FT /note="EGF-like 27; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1650..1690
FT /note="EGF-like 28; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1695..1750
FT /note="TB 7"
FT DOMAIN 1768..1809
FT /note="EGF-like 29; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1810..1850
FT /note="EGF-like 30; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1851..1892
FT /note="EGF-like 31; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1893..1931
FT /note="EGF-like 32; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1932..1974
FT /note="EGF-like 33; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1975..2014
FT /note="EGF-like 34; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2015..2056
FT /note="EGF-like 35; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2061..2113
FT /note="TB 8"
FT DOMAIN 2129..2167
FT /note="EGF-like 36; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2168..2207
FT /note="EGF-like 37; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2208..2248
FT /note="EGF-like 38; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2249..2292
FT /note="EGF-like 39; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2293..2334
FT /note="EGF-like 40; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2339..2392
FT /note="TB 9"
FT DOMAIN 2404..2445
FT /note="EGF-like 41; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2446..2486
FT /note="EGF-like 42; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2487..2525
FT /note="EGF-like 43; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2526..2568
FT /note="EGF-like 44; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2569..2608
FT /note="EGF-like 45; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2609..2649
FT /note="EGF-like 46; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2650..2689
FT /note="EGF-like 47; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 45..452
FT /note="N-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT REGION 45..81
FT /note="Fibrillin unique N-terminal (FUN) domain"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT REGION 119..329
FT /note="Interaction with MFAP4"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT REGION 195..221
FT /note="Hybrid domain 1"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT REGION 862..887
FT /note="Hybrid domain 2"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT REGION 1530..2733
FT /note="C-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT REGION 2728..2747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1543..1545
FT /note="Cell attachment site"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT SITE 44..45
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT SITE 2733..2734
FT /note="Cleavage; by furin"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT MOD_RES 2704
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT MOD_RES 2705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2711
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 268
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 512
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1069
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1137
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1220
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1304
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1347
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1388
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1486
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1510
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1630
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1705
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 1832
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1873
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1904
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1913
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 1955
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2037
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2079
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2150
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2229
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2315
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2467
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2549
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2630
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT CARBOHYD 2736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2769
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..68
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT DISULFID 67..80
FT /evidence="ECO:0000250|UniProtKB:P35555"
FT DISULFID 85..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 89..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 102..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 119..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 123..134
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 136..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 150..160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 154..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 168..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 250..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 257..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 273..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 292..304
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 299..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 315..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 455..467
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 462..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 478..490
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 496..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 501..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 517..530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 536..548
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 543..557
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 559..572
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 578..589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 584..598
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 600..613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 619..630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 625..639
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 641..654
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 729..741
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 736..750
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 752..765
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 771..783
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 778..792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 794..807
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 813..823
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 818..832
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 834..847
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 855..877
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 864..889
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 878..892
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 898..910
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 916..928
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 923..937
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 939..952
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1034..1046
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1041..1055
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1057..1070
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1076..1088
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1083..1097
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1099..1113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1119..1131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1126..1140
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1142..1155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1161..1173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1168..1182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1184..1197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1203..1214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1210..1223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1225..1238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1244..1256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1251..1265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1267..1280
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1286..1298
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1293..1307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1309..1322
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1328..1341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1335..1350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1352..1363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1369..1382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1376..1391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1393..1404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1410..1422
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1417..1431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1433..1446
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1452..1463
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1458..1472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1474..1487
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1493..1504
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1499..1513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1515..1528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1536..1564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1551..1576
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1565..1579
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1566..1591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1612..1624
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1619..1633
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1635..1648
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1654..1665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1660..1674
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1676..1689
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1772..1784
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1779..1793
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1795..1808
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1814..1826
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1820..1835
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1837..1849
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1855..1867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1862..1876
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1878..1891
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1897..1907
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1902..1916
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1918..1930
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1936..1949
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1944..1958
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1960..1973
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1979..1991
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1986..2000
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2002..2013
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2019..2031
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2026..2040
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2042..2055
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2063..2085
FT /evidence="ECO:0000250|UniProtKB:P35555,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2072..2098
FT /evidence="ECO:0000250|UniProtKB:P35555,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2086..2101
FT /evidence="ECO:0000250|UniProtKB:P35555,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2087..2113
FT /evidence="ECO:0000250|UniProtKB:P35555,
FT ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2133..2144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2139..2153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2155..2166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2172..2183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2178..2192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2194..2206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2212..2223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2219..2232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2234..2247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2253..2267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2260..2276
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2278..2291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2297..2309
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2304..2318
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2320..2333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2408..2420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2415..2429
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2431..2444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2450..2461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2457..2470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2472..2485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2491..2502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2498..2511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2513..2524
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2530..2543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2537..2552
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2554..2567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2573..2583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2579..2592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2594..2607
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2613..2624
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2619..2633
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2635..2648
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2654..2665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2661..2674
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2676..2688
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CONFLICT 120
FT /note="S -> N (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="A -> V (in Ref. 1; AAA56840 and 2; AAA64217)"
FT /evidence="ECO:0000305"
FT CONFLICT 435..438
FT /note="PYPS -> LY (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="F -> V (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 566..568
FT /note="TRD -> SSE (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 579..585
FT /note="SIRNMCL -> RTPNMCP (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="S -> R (in Ref. 2; AAA64217)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="V -> W (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="T -> S (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 1137
FT /note="S -> T (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 1243
FT /note="E -> Q (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 1427
FT /note="G -> A (in Ref. 2; AAA64217)"
FT /evidence="ECO:0000305"
FT CONFLICT 1516
FT /note="P -> S (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 1539
FT /note="D -> N (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 1696
FT /note="L -> I (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 1728
FT /note="G -> R (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 1821
FT /note="Q -> L (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 1886
FT /note="V -> E (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2048..2051
FT /note="LSST -> WSSS (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2346..2347
FT /note="LQ -> FE (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2368
FT /note="D -> V (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2375
FT /note="P -> L (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2405
FT /note="I -> V (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2443
FT /note="A -> S (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2474
FT /note="K -> N (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2542
FT /note="V -> I (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2637
FT /note="T -> A (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2689
FT /note="V -> L (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2698
FT /note="G -> A (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2774
FT /note="N -> S (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
FT CONFLICT 2823..2824
FT /note="KP -> NA (in Ref. 1; AAA56840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2873 AA; 312298 MW; 11C09D2C1ADE7292 CRC64;
MRRGGLLEVA LAFALLLESY TSHGADANLE AGSLKETRAN RAKRRGGGGH DALKGPNVCG
SRYNAYCCPG WKTLPGGNQC IVPICRHSCG DGFCSRPNMC TCPSGQISPS CGSRSIQHCS
IRCMNGGSCS DDHCLCQKGY IGTHCGQPVC ESGCLNGGRC VAPNRCACTY GFTGPQCERD
YRTGPCFTVV SNQMCQGQLS GIVCTKTLCC ATVGRAWGHP CEMCPAQPHP CRRGFIPNIR
TGACQDVDEC QAIPGMCQGG NCINTVGSFE CKCPAGHKFN EVSQKCEDID ECSTIPGVCD
GGECTNTVSS YFCKCPPGFY TSPDGTRCVD VRPGYCYTAL ANGRCSNQLP QSITKMQCCC
DLGRCWSPGV TVAPEMCPIR STEDFNKLCS VPLVIPGRPE YPPPPIGPLP PVQPVPPGYP
PGPVIPAPRP PPEYPYPSPS REPPRVLPFN VTDYCQLVRY LCQNGRCIPT PGSYRCECNK
GFQLDIRGEC IDVDECEKNP CTGGECINNQ GSYTCHCRAG YQSTLTRTEC RDIDECLQNG
RICNNGRCIN TDGSFHCVCN AGFHVTRDGK NCEDMDECSI RNMCLNGMCI NEDGSFKCIC
KPGFQLASDG RYCKDINECE TPGICMNGRC VNTDGSYRCE CFPGLAVGLD GRVCVDTHMR
STCYGGYRRG QCVKPLFGAV TKSECCCAST EYAFGEPCQP CPAQNSAEYQ ALCSSGPGMT
SAGTDINECA LDPDICPNGI CENLRGTYKC ICNSGYEVDI TGKNCVDINE CVLNSLLCDN
GQCRNTPGSF VCTCPKGFVY KPDLKTCEDI DECESSPCIN GVCKNSPGSF ICECSPESTL
DPTKTICIET IKGTCWQTVI DGRCEINING ATLKSECCSS LGAAWGSPCT ICQLDPICGK
GFSRIKGTQC EDINECEVFP GVCKNGLCVN SRGSFKCECP NGMTLDATGR ICLDIRLETC
FLKYDDEECT LPIAGRHRMD ACCCSVGAAW GTEECEECPL RNSREYEELC PRGPGFATKD
ITNGKPFFKD INECKMIPSL CTHGKCRNTI GSFKCRCDSG FALDSEERNC TDIDECRISP
DLCGRGQCVN TPGDFECKCD EGYESGFMMM KNCMDIDECQ RDPLLCRGGI CHNTEGSYRC
ECPPGHQLSP NISACIDINE CELSANLCPH GRCVNLIGKY QCACNPGYHP THDRLFCVDI
DECSIMNGGC ETFCTNSDGS YECSCQPGFA LMPDQRSCTD IDECEDNPNI CDGGQCTNIP
GEYRCLCYDG FMASEDMKTC VDVNECDLNP NICLSGTCEN TKGSFICHCD MGYSGKKGKT
GCTDINECEI GAHNCGRHAV CTNTAGSFKC SCSPGWIGDG IKCTDLDECS NGTHMCSQHA
DCKNTMGSYR CLCKDGYTGD GFTCTDLDEC SENLNLCGNG QCLNAPGGYR CECDMGFVPS
ADGKACEDID ECSLPNICVF GTCHNLPGLF RCECEIGYEL DRSGGNCTDV NECLDPTTCI
SGNCVNTPGS YTCDCPPDFE LNPTRVGCVD TRSGNCYLDI RPRGDNGDTA CSNEIGVGVS
KASCCCSLGK AWGTPCELCP SVNTSEYKIL CPGGEGFRPN PITVILEDID ECQELPGLCQ
GGKCINTFGS FQCRCPTGYY LNEDTRVCDD VNECETPGIC GPGTCYNTVG NYTCICPPDY
MQVNGGNNCM DMRRSLCYRN YYADNQTCDG ELLFNMTKKM CCCSYNIGRA WNKPCEQCPI
PSTDEFATLC GSQRPGFVID IYTGLPVDID ECREIPGVCE NGVCINMVGS FRCECPVGFF
YNDKLLVCED IDECQNGPVC QRNAECINTA GSYRCDCKPG YRLTSTGQCN DRNECQEIPN
ICSHGQCIDT VGSFYCLCHT GFKTNVDQTM CLDINECERD ACGNGTCRNT IGSFNCRCNH
GFILSHNNDC IDVDECATGN GNLCRNGQCV NTVGSFQCRC NEGYEVAPDG RTCVDINECV
LDPGKCAPGT CQNLDGSYRC ICPPGYSLQN DKCEDIDECV EEPEICALGT CSNTEGSFKC
LCPEGFSLSS TGRRCQDLRM SYCYAKFEGG KCSSPKSRNH SKQECCCALK GEGWGDPCEL
CPTEPDEAFR QICPFGSGII VGPDDSAVDM DECKEPDVCR HGQCINTDGS YRCECPFGYI
LEGNECVDTD ECSVGNPCGN GTCKNVIGGF ECTCEEGFEP GPMMTCEDIN ECAQNPLLCA
FRCVNTYGSY ECKCPVGYVL REDRRMCKDE DECAEGKHDC TEKQMECKNL IGTYMCICGP
GYQRRPDGEG CIDENECQTK PGICENGRCL NTLGSYTCEC NDGFTASPTQ DECLDNREGY
CFSEVLQNMC QIGSSNRNPV TKSECCCDGG RGWGPHCEIC PFEGTVAYKK LCPHGRGFMT
NGADIDECKV IHDVCRNGEC VNDRGSYHCI CKTGYTPDIT GTACVDLNEC NQAPKPCNFI
CKNTEGSYQC SCPKGYILQE DGRSCKDLDE CATKQHNCQF LCVNTIGGFT CKCPPGFTQH
HTACIDNNEC TSDINLCGSK GVCQNTPGSF TCECQRGFSL DQSGASCEDV DECEGNHRCQ
HGCQNIIGGY RCSCPQGYLQ HYQWNQCVDE NECLSAHVCG GASCHNTLGS YKCMCPTGFQ
YEQFSGGCQD INECGSSQAP CSYGCSNTEG GYLCGCPPGY FRIGQGHCVS GMGMGRGGPE
PPASSEMDDN SLSPEACYEC KINGYPKRGR KRRSTNETDA SDIQDGSEME ANVSLASWDV
EKPASFAFNI SHVNNKVRIL ELLPALTTLM NHNRYLIESG NEDGFFKINQ KEGVSYLHFT
KKKPVAGTYS LQISSTPLYK KKELNQLEDR YDKDYLSGEL GDNLKMKIQI LLH
