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 27-MAR-2024, entry version 185. 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, RC and 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSMUSP00000099524; -. DR GlyCosmos; Q61554; 36 sites, No reported glycans. DR GlyGen; Q61554; 37 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q61554; -. DR PhosphoSitePlus; Q61554; -. DR jPOST; Q61554; -. DR MaxQB; Q61554; -. DR PaxDb; 10090-ENSMUSP00000028633; -. DR PeptideAtlas; Q61554; -. DR ProteomicsDB; 267344; -. DR Pumba; Q61554; -. DR Antibodypedia; 2908; 559 antibodies from 37 providers. DR DNASU; 14118; -. DR Ensembl; ENSMUST00000028633.13; ENSMUSP00000028633.7; ENSMUSG00000027204.14. DR Ensembl; ENSMUST00000103234.2; ENSMUSP00000099524.2; ENSMUSG00000027204.14. DR GeneID; 14118; -. DR KEGG; mmu:14118; -. DR UCSC; uc008mco.1; mouse. DR AGR; MGI:95489; -. DR CTD; 2200; -. DR MGI; MGI:95489; Fbn1. DR VEuPathDB; HostDB:ENSMUSG00000027204; -. DR eggNOG; KOG1217; Eukaryota. DR GeneTree; ENSGT00950000183158; -. DR InParanoid; Q61554; -. DR OMA; DRLDCVD; -. DR OrthoDB; 354414at2759; -. 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 79 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 261 other cell types or 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; ISO:MGI. 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: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; ISO:MGI. DR GO; GO:0006006; P:glucose metabolic process; ISO:MGI. 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:2001205; P:negative regulation of osteoclast development; IDA:UniProtKB. DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IDA:UniProtKB. DR GO; GO:0048050; P:post-embryonic eye morphogenesis; IEA:Ensembl. DR GO; GO:0010737; P:protein kinase A signaling; ISO:MGI. 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 CDD; cd00054; EGF_CA; 29. DR Gene3D; 2.10.25.10; Laminin; 46. DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 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; IPR049388; FBN_EGF_N. 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; PTHR47333:SF2; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR47333; VON WILLEBRAND FACTOR C AND EGF DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF12662; cEGF; 3. DR Pfam; PF12947; EGF_3; 1. DR Pfam; PF07645; EGF_CA; 36. DR Pfam; PF21364; FBN_EGF_st1; 1. DR Pfam; PF18193; Fibrillin_U_N; 1. DR Pfam; PF14670; FXa_inhibition; 1. DR Pfam; PF00683; TB; 9. DR PIRSF; PIRSF036312; Fibrillin; 1. DR SMART; SM00181; EGF; 46. DR SMART; SM00179; EGF_CA; 44. DR SUPFAM; SSF57196; EGF/Laminin; 12. DR SUPFAM; SSF57184; Growth factor receptor domain; 11. DR SUPFAM; SSF57581; TB module/8-cys domain; 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 //