FBN2_HUMAN
ID FBN2_HUMAN Reviewed; 2912 AA.
AC P35556; B4DU01; Q59ES6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Fibrillin-2 {ECO:0000303|PubMed:32329225};
DE Contains:
DE RecName: Full=Placensin {ECO:0000303|PubMed:32329225};
DE Flags: Precursor;
GN Name=FBN2 {ECO:0000303|PubMed:32329225, ECO:0000312|HGNC:HGNC:3604};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND VARIANTS
RP SER-594; GLY-1772; LEU-2266; LEU-2580 AND PRO-2771.
RX PubMed=8120105; DOI=10.1083/jcb.124.5.855;
RA Zhang H., Apfelroth S.D., Hu W., Davis E.C., Sanguineti C., Bonadio J.,
RA Mecham R.P., Ramirez F.;
RT "Structure and expression of fibrillin-2, a novel microfibrillar component
RT preferentially located in elastic matrices.";
RL J. Cell Biol. 124:855-863(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 752-2912 (ISOFORM 2).
RX PubMed=1852206; DOI=10.1038/352330a0;
RA Lee B., Godfrey M., Vitale E., Hori H., Mattei M.-G., Sarfarazi M.,
RA Tsipouras P., Ramirez F., Hollister D.W.;
RT "Linkage of Marfan syndrome and a phenotypically related disorder to two
RT different fibrillin genes.";
RL Nature 352:330-334(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 937-2912 (ISOFORM 1).
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH MFAP2 AND MFAP5.
RX PubMed=15131124; DOI=10.1074/jbc.m313672200;
RA Hanssen E., Hew F.H., Moore E., Gibson M.A.;
RT "MAGP-2 has multiple binding regions on fibrillins and has covalent
RT periodic association with fibrillin-containing microfibrils.";
RL J. Biol. Chem. 279:29185-29194(2004).
RN [7]
RP INTERACTION WITH BMP2; BMP4; BMP7; BMP10 AND GDF5.
RX PubMed=18339631; DOI=10.1074/jbc.m707820200;
RA Sengle G., Charbonneau N.L., Ono R.N., Sasaki T., Alvarez J., Keene D.R.,
RA Baechinger H.P., Sakai L.Y.;
RT "Targeting of bone morphogenetic protein growth factor complexes to
RT fibrillin.";
RL J. Biol. Chem. 283:13874-13888(2008).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1112.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP INTERACTION WITH ADAMTSL5.
RX PubMed=23010571; DOI=10.1016/j.matbio.2012.09.003;
RA Bader H.L., Wang L.W., Ho J.C., Tran T., Holden P., Fitzgerald J.,
RA Atit R.P., Reinhardt D.P., Apte S.S.;
RT "A disintegrin-like and metalloprotease domain containing thrombospondin
RT type 1 motif-like 5 (ADAMTSL5) is a novel fibrillin-1-, fibrillin-2-, and
RT heparin-binding member of the ADAMTS superfamily containing a netrin-like
RT module.";
RL Matrix Biol. 31:398-411(2012).
RN [10]
RP TISSUE SPECIFICITY, INVOLVEMENT IN EOMD, VARIANTS EOMD LYS-1144 AND
RP THR-1247, AND VARIANTS ILE-965; ASN-1381; ALA-1416 AND LYS-1438.
RX PubMed=24899048; DOI=10.1093/hmg/ddu276;
RA Ratnapriya R., Zhan X., Fariss R.N., Branham K.E., Zipprer D.,
RA Chakarova C.F., Sergeev Y.V., Campos M.M., Othman M., Friedman J.S.,
RA Maminishkis A., Waseem N.H., Brooks M., Rajasimha H.K., Edwards A.O.,
RA Lotery A., Klein B.E., Truitt B.J., Li B., Schaumberg D.A., Morgan D.J.,
RA Morrison M.A., Souied E., Tsironi E.E., Grassmann F., Fishman G.A.,
RA Silvestri G., Scholl H.P., Kim I.K., Ramke J., Tuo J., Merriam J.E.,
RA Merriam J.C., Park K.H., Olson L.M., Farrer L.A., Johnson M.P.,
RA Peachey N.S., Lathrop M., Baron R.V., Igo R.P. Jr., Klein R.,
RA Hagstrom S.A., Kamatani Y., Martin T.M., Jiang Y., Conley Y., Sahel J.A.,
RA Zack D.J., Chan C.C., Pericak-Vance M.A., Jacobson S.G., Gorin M.B.,
RA Klein M.L., Allikmets R., Iyengar S.K., Weber B.H., Haines J.L.,
RA Leveillard T., Deangelis M.M., Stambolian D., Weeks D.E.,
RA Bhattacharya S.S., Chew E.Y., Heckenlively J.R., Abecasis G.R., Swaroop A.;
RT "Rare and common variants in extracellular matrix gene Fibrillin 2 (FBN2)
RT are associated with macular degeneration.";
RL Hum. Mol. Genet. 23:5827-5837(2014).
RN [11]
RP INTERACTION WITH MFAP4.
RX PubMed=26601954; DOI=10.1074/jbc.m115.681775;
RA Pilecki B., Holm A.T., Schlosser A., Moeller J.B., Wohl A.P., Zuk A.V.,
RA Heumueller S.E., Wallis R., Moestrup S.K., Sengle G., Holmskov U.,
RA Sorensen G.L.;
RT "Characterization of microfibrillar-associated protein 4 (MFAP4) as a
RT tropoelastin- and fibrillin-binding protein involved in elastic fiber
RT formation.";
RL J. Biol. Chem. 291:1103-1114(2016).
RN [12]
RP FUNCTION (PLACENSIN), SUBCELLULAR LOCATION (PLACENSIN), GLYCOSYLATION
RP (PLACENSIN), TISSUE SPECIFICITY, AND TISSUE SPECIFICITY (PLACENSIN).
RX PubMed=32329225; DOI=10.15252/embr.201949530;
RA Yu Y., He J.H., Hu L.L., Jiang L.L., Fang L., Yao G.D., Wang S.J., Yang Q.,
RA Guo Y., Liu L., Shang T., Sato Y., Kawamura K., Hsueh A.J., Sun Y.P.;
RT "Placensin is a glucogenic hormone secreted by human placenta.";
RL EMBO Rep. 21:e49530-e49530(2020).
RN [13]
RP GLYCOSYLATION AT SER-298; SER-340; SER-516; SER-555; SER-597; SER-638;
RP SER-679; SER-832; SER-872; SER-977; SER-1095; SER-1180; THR-1222; SER-1263;
RP SER-1347; SER-1390; SER-1672; SER-1873; SER-1954; SER-1996; SER-2193;
RP SER-2274; SER-2360; SER-2471; SER-2512; SER-2594 AND SER-2675.
RX PubMed=34411563; DOI=10.1016/j.jbc.2021.101055;
RA Williamson D.B., Sohn C.J., Ito A., Haltiwanger R.S.;
RT "POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2,
RT and LTBP1 and promote secretion of fibrillin-1.";
RL J. Biol. Chem. 297:101055-101055(2021).
RN [14]
RP VARIANTS CCA TYR-1253 AND SER-1434, AND VARIANT ILE-965.
RX PubMed=7493032; DOI=10.1038/ng1295-456;
RA Putnam E.A., Zhang H., Ramirez F., Milewicz D.M.;
RT "Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder,
RT congenital contractural arachnodactyly.";
RL Nat. Genet. 11:456-458(1995).
RN [15]
RP VARIANTS CCA ASP-1057 AND THR-1093, AND VARIANTS SER-594; HIS-681; ILE-965;
RP GLY-1772; LEU-2266; THR-2428 AND PRO-2771.
RX PubMed=9714438;
RX DOI=10.1002/(sici)1096-8628(19980724)78:4<350::aid-ajmg9>3.0.co;2-p;
RA Park E.-S., Putnam E.A., Chitayat D., Child A., Milewicz D.M.;
RT "Clustering of FBN2 mutations in patients with congenital contractural
RT arachnodactyly indicates an important role of the domains encoded by exons
RT 24 through 34 during human development.";
RL Am. J. Med. Genet. 78:350-355(1998).
RN [16]
RP VARIANT CCA HIS-1115.
RX PubMed=9737771; DOI=10.1007/s004390050777;
RA Babcock D., Gasner C., Francke U., Maslen C.;
RT "A single mutation that results in an Asp-to-His substitution and partial
RT exon skipping in a family with congenital contractural arachnodactyly.";
RL Hum. Genet. 103:22-28(1998).
RN [17]
RP VARIANTS CCA PHE-1142 AND TRP-1253.
RX PubMed=10797416;
RX DOI=10.1002/(sici)1096-8628(20000501)92:1<7::aid-ajmg2>3.0.co;2-8;
RA Belleh S., Zhou G., Wang M., Der Kaloustian V.M., Pagon R.A., Godfrey M.;
RT "Two novel fibrillin-2 mutations in congenital contractural
RT arachnodactyly.";
RL Am. J. Med. Genet. 92:7-12(2000).
RN [18]
RP VARIANTS CCA ASP-1057; THR-1093; PHE-1142; CYS-1179; TYR-1198; ARG-1240;
RP TRP-1253; TYR-1253; TRP-1257; ARG-1268 AND SER-1434, AND VARIANT ILE-965.
RX PubMed=11754102; DOI=10.1002/humu.10017;
RA Gupta P.A., Putnam E.A., Carmical S.G., Kaitila I., Steinmann B., Child A.,
RA Danesino C., Metcalfe K., Berry S.A., Chen E., Delorme C.V., Thong M.-K.,
RA Ades L.C., Milewicz D.M.;
RT "Ten novel FBN2 mutations in congenital contractural arachnodactyly:
RT delineation of the molecular pathogenesis and clinical phenotype.";
RL Hum. Mutat. 19:39-48(2002).
RN [19]
RP VARIANTS CCA SER-754; SER-1091; HIS-1115; PRO-1122; ARG-1142; CYS-1146;
RP PHE-1156; LYS-1161; PHE-1246; PHE-1384; TYR-1384; ASN-1408 AND ARG-1425.
RX PubMed=19006240; DOI=10.1002/humu.20854;
RA Callewaert B.L., Loeys B.L., Ficcadenti A., Vermeer S., Landgren M.,
RA Kroes H.Y., Yaron Y., Pope M., Foulds N., Boute O., Galan F., Kingston H.,
RA Van der Aa N., Salcedo I., Swinkels M.E., Wallgren-Pettersson C.,
RA Gabrielli O., De Backer J., Coucke P.J., De Paepe A.M.;
RT "Comprehensive clinical and molecular assessment of 32 probands with
RT congenital contractural arachnodactyly: report of 14 novel mutations and
RT review of the literature.";
RL Hum. Mutat. 30:334-341(2009).
RN [20]
RP VARIANT CCA LYS-1259.
RX PubMed=20799338; DOI=10.1002/ajmg.a.33628;
RA Sampson M.G., Coughlin C.R. II, Kaplan P., Conlin L.K., Meyers K.E.,
RA Zackai E.H., Spinner N.B., Copelovitch L.;
RT "Evidence for a recurrent microdeletion at chromosome 16p11.2 associated
RT with congenital anomalies of the kidney and urinary tract (CAKUT) and
RT Hirschsprung disease.";
RL Am. J. Med. Genet. A 152A:2618-2622(2010).
RN [21]
RP VARIANT VAL-2062.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
RN [22]
RP VARIANT CCA ARG-1406.
RX PubMed=25834781; DOI=10.1016/j.fob.2015.02.005;
RA Liu W., Zhao N., Li X.F., Wang H., Sui Y., Lu Y.P., Feng W.H., Ma C.,
RA Han W.T., Jiang M.;
RT "A novel FBN2 mutation in a Chinese family with congenital contractural
RT arachnodactyly.";
RL FEBS Open Bio 5:163-166(2015).
RN [23]
RP VARIANT CCA ARG-1257.
RX PubMed=27196565; DOI=10.1371/journal.pone.0155908;
RA Deng H., Lu Q., Xu H., Deng X., Yuan L., Yang Z., Guo Y., Lin Q., Xiao J.,
RA Guan L., Song Z.;
RT "Identification of a Novel Missense FBN2 Mutation in a Chinese Family with
RT Congenital Contractural Arachnodactyly Using Exome Sequencing.";
RL PLoS ONE 11:E0155908-E0155908(2016).
CC -!- FUNCTION: [Fibrillin-2]: Fibrillins are structural components of 10-12
CC nm extracellular calcium-binding microfibrils, which occur either in
CC association with elastin or in elastin-free bundles. Fibrillin-2-
CC containing microfibrils regulate the early process of elastic fiber
CC assembly. Regulates osteoblast maturation by controlling TGF-beta
CC bioavailability and calibrating TGF-beta and BMP levels, respectively.
CC {ECO:0000250|UniProtKB:Q61555}.
CC -!- FUNCTION: [Placensin]: Hormone secreted by trophoblasts that promotes
CC trophoblast invasiveness (PubMed:32329225). Has glucogenic activity: is
CC able to increase plasma glucose levels (By similarity).
CC {ECO:0000250|UniProtKB:Q61555, ECO:0000269|PubMed:32329225}.
CC -!- SUBUNIT: Interacts with BMP2, BMP4, BMP7, BMP10 and GDF5
CC (PubMed:18339631). Interacts with MFAP2 and MFAP5 (PubMed:15131124).
CC Interacts with ADAMTSL5 (PubMed:23010571). Interacts with MFAP4
CC (PubMed:26601954). {ECO:0000269|PubMed:15131124,
CC ECO:0000269|PubMed:18339631, ECO:0000269|PubMed:23010571,
CC ECO:0000269|PubMed:26601954}.
CC -!- INTERACTION:
CC P35556; P35555: FBN1; NbExp=2; IntAct=EBI-6164392, EBI-2505934;
CC P35556; P02751: FN1; NbExp=2; IntAct=EBI-6164392, EBI-1220319;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32329225}.
CC Note=Fibrillin-2 and Placensin chains are still linked together during
CC the secretion from cells, but are subsequently separated by furin.
CC {ECO:0000269|PubMed:32329225}.
CC -!- SUBCELLULAR LOCATION: [Fibrillin-2]: Secreted, extracellular space,
CC extracellular matrix {ECO:0000269|PubMed:8120105}.
CC -!- SUBCELLULAR LOCATION: [Placensin]: Secreted
CC {ECO:0000269|PubMed:32329225}. Note=Secreted by placental cells.
CC {ECO:0000269|PubMed:32329225}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35556-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35556-2; Sequence=VSP_037369, VSP_037370, VSP_037371;
CC -!- TISSUE SPECIFICITY: Almost exclusively expressed in placenta
CC (PubMed:32329225). Expressed at much lower level in other tissues
CC (PubMed:32329225). Expressed in fetal eye (18 weeks)in the retinal
CC pigment epithelium (RPE), the choroid, Bruch's membrane and in the
CC sclera (PubMed:24899048). Not expressed in the neural retina
CC (PubMed:24899048). {ECO:0000269|PubMed:24899048,
CC ECO:0000269|PubMed:32329225}.
CC -!- TISSUE SPECIFICITY: [Placensin]: Present at high level in
CC cytotrophoblasts as compared with syncytiotrophoblasts at 8-9 weeks of
CC pregnancy (at protein level) (PubMed:32329225). Levels in the serum
CC increase during pregnancy (at protein level) (PubMed:32329225).
CC {ECO:0000269|PubMed:32329225}.
CC -!- PTM: [Placensin]: N-glycosylated. {ECO:0000269|PubMed:32329225}.
CC -!- PTM: O-glycosylated on serine residues by POGLUT2 and POGLUT3.
CC {ECO:0000269|PubMed:34411563}.
CC -!- DISEASE: Contractural arachnodactyly, congenital (CCA) [MIM:121050]: An
CC autosomal dominant connective tissue disorder characterized by
CC contractures, arachnodactyly, scoliosis, and crumpled ears.
CC {ECO:0000269|PubMed:10797416, ECO:0000269|PubMed:11754102,
CC ECO:0000269|PubMed:19006240, ECO:0000269|PubMed:20799338,
CC ECO:0000269|PubMed:25834781, ECO:0000269|PubMed:27196565,
CC ECO:0000269|PubMed:7493032, ECO:0000269|PubMed:9714438,
CC ECO:0000269|PubMed:9737771}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Macular degeneration, early-onset (EOMD) [MIM:616118]: An
CC ocular disorder characterized by macular changes resulting in
CC progressive loss of visual acuity. {ECO:0000269|PubMed:24899048}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the fibrillin family. {ECO:0000305}.
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DR EMBL; U03272; AAA18950.1; -; mRNA.
DR EMBL; AK300440; BAG62163.1; -; mRNA.
DR EMBL; AC025169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC034235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X62009; CAB56757.1; -; mRNA.
DR EMBL; AB209735; BAD92972.1; -; mRNA.
DR CCDS; CCDS34222.1; -. [P35556-1]
DR PIR; A54105; A54105.
DR RefSeq; NP_001990.2; NM_001999.3. [P35556-1]
DR SMR; P35556; -.
DR BioGRID; 108495; 52.
DR IntAct; P35556; 26.
DR MINT; P35556; -.
DR STRING; 9606.ENSP00000424571; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR GlyConnect; 1236; 13 N-Linked glycans (2 sites).
DR GlyGen; P35556; 12 sites, 14 N-linked glycans (3 sites).
DR iPTMnet; P35556; -.
DR PhosphoSitePlus; P35556; -.
DR BioMuta; FBN2; -.
DR DMDM; 238054385; -.
DR EPD; P35556; -.
DR jPOST; P35556; -.
DR MassIVE; P35556; -.
DR MaxQB; P35556; -.
DR PaxDb; P35556; -.
DR PeptideAtlas; P35556; -.
DR PRIDE; P35556; -.
DR ProteomicsDB; 55082; -. [P35556-1]
DR ProteomicsDB; 55083; -. [P35556-2]
DR Antibodypedia; 2482; 168 antibodies from 28 providers.
DR DNASU; 2201; -.
DR Ensembl; ENST00000262464.9; ENSP00000262464.4; ENSG00000138829.12. [P35556-1]
DR Ensembl; ENST00000508053.5; ENSP00000424571.1; ENSG00000138829.12. [P35556-1]
DR GeneID; 2201; -.
DR KEGG; hsa:2201; -.
DR MANE-Select; ENST00000262464.9; ENSP00000262464.4; NM_001999.4; NP_001990.2.
DR UCSC; uc003kuu.3; human. [P35556-1]
DR CTD; 2201; -.
DR DisGeNET; 2201; -.
DR GeneCards; FBN2; -.
DR GeneReviews; FBN2; -.
DR HGNC; HGNC:3604; FBN2.
DR HPA; ENSG00000138829; Tissue enriched (placenta).
DR MalaCards; FBN2; -.
DR MIM; 121050; phenotype.
DR MIM; 612570; gene.
DR MIM; 616118; phenotype.
DR neXtProt; NX_P35556; -.
DR OpenTargets; ENSG00000138829; -.
DR Orphanet; 115; Congenital contractural arachnodactyly.
DR Orphanet; 279; NON RARE IN EUROPE: Age-related macular degeneration.
DR PharmGKB; PA28017; -.
DR VEuPathDB; HostDB:ENSG00000138829; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00950000183158; -.
DR HOGENOM; CLU_000233_0_0_1; -.
DR InParanoid; P35556; -.
DR OMA; HQCVACP; -.
DR OrthoDB; 430975at2759; -.
DR PhylomeDB; P35556; -.
DR TreeFam; TF316849; -.
DR PathwayCommons; P35556; -.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-1566948; Elastic fibre formation.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR SignaLink; P35556; -.
DR BioGRID-ORCS; 2201; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; FBN2; human.
DR GenomeRNAi; 2201; -.
DR Pharos; P35556; Tbio.
DR PRO; PR:P35556; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P35556; protein.
DR Bgee; ENSG00000138829; Expressed in cartilage tissue and 126 other tissues.
DR ExpressionAtlas; P35556; baseline and differential.
DR Genevisible; P35556; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0001527; C:microfibril; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030023; F:extracellular matrix constituent conferring elasticity; IC:UniProtKB.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IDA:UniProtKB.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0060346; P:bone trabecula formation; ISS:BHF-UCL.
DR GO; GO:0043010; P:camera-type eye development; IEP:UniProtKB.
DR GO; GO:0048048; P:embryonic eye morphogenesis; IEP:UniProtKB.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0001890; P:placenta development; IDA:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:BHF-UCL.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:BHF-UCL.
DR GO; GO:1901163; P:regulation of trophoblast cell migration; IDA:UniProtKB.
DR GO; GO:0035583; P:sequestering of TGFbeta in extracellular matrix; ISS:BHF-UCL.
DR Gene3D; 3.90.290.10; -; 9.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
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:SF26; PTHR24039:SF26; 5.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 38.
DR Pfam; PF18193; Fibrillin_U_N; 1.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF00683; TB; 9.
DR SMART; SM00181; EGF; 46.
DR SMART; SM00179; EGF_CA; 44.
DR SUPFAM; SSF57184; SSF57184; 13.
DR SUPFAM; SSF57581; SSF57581; 9.
DR PROSITE; PS00010; ASX_HYDROXYL; 43.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 37.
DR PROSITE; PS50026; EGF_3; 45.
DR PROSITE; PS01187; EGF_CA; 43.
DR PROSITE; PS51364; TB; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disease variant; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..77
FT /evidence="ECO:0000305"
FT /id="PRO_0000436887"
FT CHAIN 78..2779
FT /note="Fibrillin-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000007584"
FT CHAIN 2780..2912
FT /note="Placensin"
FT /evidence="ECO:0000305|PubMed:32329225"
FT /id="PRO_0000436888"
FT DOMAIN 111..142
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 145..176
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 176..208
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 214..266
FT /note="TB 1"
FT DOMAIN 276..317
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 318..359
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 364..417
FT /note="TB 2"
FT DOMAIN 494..534
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 535..574
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 575..616
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 617..657
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 658..698
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 704..756
FT /note="TB 3"
FT DOMAIN 768..809
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 810..851
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 852..891
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 896..947
FT /note="TB 4"
FT DOMAIN 955..996
FT /note="EGF-like 14; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1001..1052
FT /note="TB 5"
FT DOMAIN 1073..1114
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1115..1157
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1158..1199
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1200..1241
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1242..1282
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1283..1324
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1325..1366
FT /note="EGF-like 21; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1367..1407
FT /note="EGF-like 22; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1408..1448
FT /note="EGF-like 23; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1449..1490
FT /note="EGF-like 24; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1491..1531
FT /note="EGF-like 25; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1532..1572
FT /note="EGF-like 26; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1577..1633
FT /note="TB 6"
FT DOMAIN 1650..1691
FT /note="EGF-like 27; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1692..1733
FT /note="EGF-like 28; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1738..1791
FT /note="TB 7"
FT DOMAIN 1808..1849
FT /note="EGF-like 29; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1850..1891
FT /note="EGF-like 30; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1892..1933
FT /note="EGF-like 31; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1934..1972
FT /note="EGF-like 32; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1973..2015
FT /note="EGF-like 33; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2016..2055
FT /note="EGF-like 34; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2056..2097
FT /note="EGF-like 35; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2102..2155
FT /note="TB 8"
FT DOMAIN 2171..2212
FT /note="EGF-like 36; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2213..2252
FT /note="EGF-like 37; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2253..2293
FT /note="EGF-like 38; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2294..2337
FT /note="EGF-like 39; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2338..2379
FT /note="EGF-like 40; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2384..2437
FT /note="TB 9"
FT DOMAIN 2449..2490
FT /note="EGF-like 41; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2491..2531
FT /note="EGF-like 42; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2532..2570
FT /note="EGF-like 43; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2571..2613
FT /note="EGF-like 44; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2614..2653
FT /note="EGF-like 45; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2654..2694
FT /note="EGF-like 46; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 2695..2734
FT /note="EGF-like 47; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 27..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..359
FT /note="Interaction with MFAP4"
FT /evidence="ECO:0000269|PubMed:26601954"
FT REGION 1735..2171
FT /note="Interaction with MFAP4"
FT /evidence="ECO:0000269|PubMed:26601954"
FT COMPBIAS 28..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 298
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 340
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 555
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 597
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 638
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 679
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 832
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 872
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 977
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1095
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1180
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1222
FT /note="O-linked (Glc) threonine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1263
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1347
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1390
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1672
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1714
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1873
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1954
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 1996
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 2120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2193
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 2225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2274
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 2360
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 2471
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 2512
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 2594
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 2675
FT /note="O-linked (Glc) serine"
FT /evidence="ECO:0000269|PubMed:34411563"
FT CARBOHYD 2808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 115..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 119..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 132..141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 149..159
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 153..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 166..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 180..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 184..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 198..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 280..292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 287..301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 303..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 322..334
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 329..343
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 345..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 498..510
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 505..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 521..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 539..549
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 544..558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 560..573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 579..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 586..600
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 602..615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 621..632
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 627..641
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 643..656
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 662..673
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 668..682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 684..697
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 772..784
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 779..793
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 795..808
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 814..826
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 821..835
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 837..850
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 856..866
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 861..875
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 877..890
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 959..971
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 966..980
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 982..995
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1077..1089
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1084..1098
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1100..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..1156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1162..1174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1169..1183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1185..1198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1204..1216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1211..1225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1227..1240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1246..1257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1253..1266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1268..1281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1287..1299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1294..1308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1310..1323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1329..1341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1336..1350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1352..1365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1371..1384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1378..1393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1395..1406
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1412..1425
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1419..1434
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1436..1447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1453..1465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1460..1474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1476..1489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1495..1506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1501..1515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1517..1530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1536..1547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1542..1556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1558..1571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1654..1666
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1661..1675
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1677..1690
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1696..1708
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1703..1717
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1719..1732
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1812..1824
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1819..1833
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1835..1848
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1854..1867
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1861..1876
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1878..1890
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1896..1908
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1903..1917
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1919..1932
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1938..1948
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1943..1957
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1959..1971
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1977..1990
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1985..1999
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2001..2014
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2020..2032
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2027..2041
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2043..2054
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2060..2072
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2067..2081
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2083..2096
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2175..2187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2182..2196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2198..2211
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2217..2228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2223..2237
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2239..2251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2257..2268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2264..2277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2279..2292
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2298..2312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2305..2321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2323..2336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2342..2354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2349..2363
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2365..2378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2453..2465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2460..2474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2476..2489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2495..2506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2502..2515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2517..2530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2536..2547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2543..2556
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2558..2569
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2575..2588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2582..2597
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2599..2612
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2618..2628
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2624..2637
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2639..2652
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2658..2669
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2664..2678
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2680..2693
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2699..2710
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2706..2719
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2721..2733
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 113..145
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:1852206"
FT /id="VSP_037369"
FT VAR_SEQ 1491..1506
FT /note="DIDECSFQNICVFGTC -> GGSPGFQLIFKLDQPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:1852206"
FT /id="VSP_037370"
FT VAR_SEQ 1507..2912
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:1852206"
FT /id="VSP_037371"
FT VARIANT 391
FT /note="E -> K (in CCA; dbSNP:rs137852826)"
FT /id="VAR_015851"
FT VARIANT 594
FT /note="T -> S"
FT /evidence="ECO:0000269|PubMed:8120105,
FT ECO:0000269|PubMed:9714438"
FT /id="VAR_054979"
FT VARIANT 681
FT /note="R -> H (in dbSNP:rs548605398)"
FT /evidence="ECO:0000269|PubMed:9714438"
FT /id="VAR_054980"
FT VARIANT 754
FT /note="G -> S (in CCA; dbSNP:rs145259927)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058364"
FT VARIANT 965
FT /note="V -> I (in dbSNP:rs154001)"
FT /evidence="ECO:0000269|PubMed:11754102,
FT ECO:0000269|PubMed:24899048, ECO:0000269|PubMed:7493032,
FT ECO:0000269|PubMed:9714438"
FT /id="VAR_002349"
FT VARIANT 1057
FT /note="G -> D (in CCA)"
FT /evidence="ECO:0000269|PubMed:11754102,
FT ECO:0000269|PubMed:9714438"
FT /id="VAR_054981"
FT VARIANT 1091
FT /note="N -> S (in CCA)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058365"
FT VARIANT 1093
FT /note="I -> T (in CCA)"
FT /evidence="ECO:0000269|PubMed:11754102,
FT ECO:0000269|PubMed:9714438"
FT /id="VAR_054982"
FT VARIANT 1115
FT /note="D -> H (in CCA; the underlying nucleotide
FT substitution also causes low level in-frame mis-splicing of
FT exon 25; dbSNP:rs137852827)"
FT /evidence="ECO:0000269|PubMed:19006240,
FT ECO:0000269|PubMed:9737771"
FT /id="VAR_010739"
FT VARIANT 1122
FT /note="S -> P (in CCA)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058366"
FT VARIANT 1142
FT /note="C -> F (in CCA; dbSNP:rs137852828)"
FT /evidence="ECO:0000269|PubMed:10797416,
FT ECO:0000269|PubMed:11754102"
FT /id="VAR_010740"
FT VARIANT 1142
FT /note="C -> R (in CCA)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058367"
FT VARIANT 1144
FT /note="E -> K (in EOMD; dbSNP:rs200060005)"
FT /evidence="ECO:0000269|PubMed:24899048"
FT /id="VAR_072651"
FT VARIANT 1146
FT /note="Y -> C (in CCA)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058368"
FT VARIANT 1156
FT /note="C -> F (in CCA; dbSNP:rs1206843725)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058369"
FT VARIANT 1161
FT /note="E -> K (in CCA; dbSNP:rs1554123065)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058370"
FT VARIANT 1179
FT /note="G -> C (in CCA)"
FT /evidence="ECO:0000269|PubMed:11754102"
FT /id="VAR_054983"
FT VARIANT 1198
FT /note="C -> Y (in CCA; dbSNP:rs863223567)"
FT /evidence="ECO:0000269|PubMed:11754102"
FT /id="VAR_054984"
FT VARIANT 1240
FT /note="C -> R (in CCA)"
FT /evidence="ECO:0000269|PubMed:11754102"
FT /id="VAR_054985"
FT VARIANT 1246
FT /note="C -> F (in CCA)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058371"
FT VARIANT 1247
FT /note="M -> T (in EOMD; dbSNP:rs149054177)"
FT /evidence="ECO:0000269|PubMed:24899048"
FT /id="VAR_072652"
FT VARIANT 1253
FT /note="C -> W (in CCA; dbSNP:rs28931602)"
FT /evidence="ECO:0000269|PubMed:10797416,
FT ECO:0000269|PubMed:11754102"
FT /id="VAR_010741"
FT VARIANT 1253
FT /note="C -> Y (in CCA; dbSNP:rs137852825)"
FT /evidence="ECO:0000269|PubMed:11754102,
FT ECO:0000269|PubMed:7493032"
FT /id="VAR_002350"
FT VARIANT 1257
FT /note="C -> R (in CCA)"
FT /evidence="ECO:0000269|PubMed:27196565"
FT /id="VAR_076482"
FT VARIANT 1257
FT /note="C -> W (in CCA)"
FT /evidence="ECO:0000269|PubMed:11754102"
FT /id="VAR_054986"
FT VARIANT 1259
FT /note="N -> K (in CCA; dbSNP:rs267606802)"
FT /evidence="ECO:0000269|PubMed:20799338"
FT /id="VAR_072653"
FT VARIANT 1268
FT /note="C -> R (in CCA)"
FT /evidence="ECO:0000269|PubMed:11754102"
FT /id="VAR_054987"
FT VARIANT 1381
FT /note="H -> N (in dbSNP:rs78727187)"
FT /evidence="ECO:0000269|PubMed:24899048"
FT /id="VAR_072654"
FT VARIANT 1384
FT /note="C -> F (in CCA)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058372"
FT VARIANT 1384
FT /note="C -> Y (in CCA; dbSNP:rs794727560)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058373"
FT VARIANT 1406
FT /note="C -> R (in CCA)"
FT /evidence="ECO:0000269|PubMed:25834781"
FT /id="VAR_074052"
FT VARIANT 1408
FT /note="D -> N (in CCA)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058374"
FT VARIANT 1416
FT /note="T -> A (in dbSNP:rs200837433)"
FT /evidence="ECO:0000269|PubMed:24899048"
FT /id="VAR_072655"
FT VARIANT 1425
FT /note="C -> R (in CCA)"
FT /evidence="ECO:0000269|PubMed:19006240"
FT /id="VAR_058375"
FT VARIANT 1434
FT /note="C -> S (in CCA)"
FT /evidence="ECO:0000269|PubMed:11754102,
FT ECO:0000269|PubMed:7493032"
FT /id="VAR_002351"
FT VARIANT 1438
FT /note="E -> K (in dbSNP:rs56168072)"
FT /evidence="ECO:0000269|PubMed:24899048"
FT /id="VAR_072656"
FT VARIANT 1772
FT /note="W -> G"
FT /evidence="ECO:0000269|PubMed:8120105,
FT ECO:0000269|PubMed:9714438"
FT /id="VAR_054988"
FT VARIANT 2062
FT /note="E -> V (found in a renal cell carcinoma case;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064705"
FT VARIANT 2266
FT /note="F -> L"
FT /evidence="ECO:0000269|PubMed:8120105,
FT ECO:0000269|PubMed:9714438"
FT /id="VAR_054989"
FT VARIANT 2278
FT /note="T -> M (in dbSNP:rs2307109)"
FT /id="VAR_055415"
FT VARIANT 2311
FT /note="M -> V (in dbSNP:rs32209)"
FT /id="VAR_055416"
FT VARIANT 2428
FT /note="P -> T (in dbSNP:rs1801169)"
FT /evidence="ECO:0000269|PubMed:9714438"
FT /id="VAR_016143"
FT VARIANT 2580
FT /note="S -> L (in dbSNP:rs2291628)"
FT /evidence="ECO:0000269|PubMed:8120105"
FT /id="VAR_055417"
FT VARIANT 2581
FT /note="L -> S (in dbSNP:rs2291628)"
FT /id="VAR_054990"
FT VARIANT 2771
FT /note="S -> P (in dbSNP:rs1801170)"
FT /evidence="ECO:0000269|PubMed:8120105,
FT ECO:0000269|PubMed:9714438"
FT /id="VAR_014664"
FT CONFLICT 146
FT /note="I -> L (in Ref. 2; BAG62163)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..195
FT /note="GPNR -> AQP (in Ref. 1; AAA18950)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="I -> T (in Ref. 1; AAA18950 and 2; BAG62163)"
FT /evidence="ECO:0000305"
FT CONFLICT 1161
FT /note="E -> G (in Ref. 1; AAA18950 and 4; CAB56757)"
FT /evidence="ECO:0000305"
FT CONFLICT 1244
FT /note="D -> G (in Ref. 2; BAG62163)"
FT /evidence="ECO:0000305"
FT CONFLICT 1409
FT /note="L -> R (in Ref. 4; CAB56757)"
FT /evidence="ECO:0000305"
FT CONFLICT 1503
FT /note="F -> S (in Ref. 1; AAA18950)"
FT /evidence="ECO:0000305"
FT CONFLICT 2584
FT /note="A -> G (in Ref. 1; AAA18950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2912 AA; 314775 MW; 0F0D78319E9911E6 CRC64;
MGRRRRLCLQ LYFLWLGCVV LWAQGTAGQP QPPPPKPPRP QPPPQQVRSA TAGSEGGFLA
PEYREEGAAV ASRVRRRGQQ DVLRGPNVCG SRFHSYCCPG WKTLPGGNQC IVPICRNSCG
DGFCSRPNMC TCSSGQISST CGSKSIQQCS VRCMNGGTCA DDHCQCQKGY IGTYCGQPVC
ENGCQNGGRC IGPNRCACVY GFTGPQCERD YRTGPCFTQV NNQMCQGQLT GIVCTKTLCC
ATIGRAWGHP CEMCPAQPQP CRRGFIPNIR TGACQDVDEC QAIPGICQGG NCINTVGSFE
CRCPAGHKQS ETTQKCEDID ECSIIPGICE TGECSNTVGS YFCVCPRGYV TSTDGSRCID
QRTGMCFSGL VNGRCAQELP GRMTKMQCCC EPGRCWGIGT IPEACPVRGS EEYRRLCMDG
LPMGGIPGSA GSRPGGTGGN GFAPSGNGNG YGPGGTGFIP IPGGNGFSPG VGGAGVGAGG
QGPIITGLTI LNQTIDICKH HANLCLNGRC IPTVSSYRCE CNMGYKQDAN GDCIDVDECT
SNPCTNGDCV NTPGSYYCKC HAGFQRTPTK QACIDIDECI QNGVLCKNGR CVNTDGSFQC
ICNAGFELTT DGKNCVDHDE CTTTNMCLNG MCINEDGSFK CICKPGFVLA PNGRYCTDVD
ECQTPGICMN GHCINSEGSF RCDCPPGLAV GMDGRVCVDT HMRSTCYGGI KKGVCVRPFP
GAVTKSECCC ANPDYGFGEP CQPCPAKNSA EFHGLCSSGV GITVDGRDIN ECALDPDICA
NGICENLRGS YRCNCNSGYE PDASGRNCID IDECLVNRLL CDNGLCRNTP GSYSCTCPPG
YVFRTETETC EDINECESNP CVNGACRNNL GSFNCECSPG SKLSSTGLIC IDSLKGTCWL
NIQDSRCEVN INGATLKSEC CATLGAAWGS PCERCELDTA CPRGLARIKG VTCEDVNECE
VFPGVCPNGR CVNSKGSFHC ECPEGLTLDG TGRVCLDIRM EQCYLKWDED ECIHPVPGKF
RMDACCCAVG AAWGTECEEC PKPGTKEYET LCPRGAGFAN RGDVLTGRPF YKDINECKAF
PGMCTYGKCR NTIGSFKCRC NSGFALDMEE RNCTDIDECR ISPDLCGSGI CVNTPGSFEC
ECFEGYESGF MMMKNCMDID ECERNPLLCR GGTCVNTEGS FQCDCPLGHE LSPSREDCVD
INECSLSDNL CRNGKCVNMI GTYQCSCNPG YQATPDRQGC TDIDECMIMN GGCDTQCTNS
EGSYECSCSE GYALMPDGRS CADIDECENN PDICDGGQCT NIPGEYRCLC YDGFMASMDM
KTCIDVNECD LNSNICMFGE CENTKGSFIC HCQLGYSVKK GTTGCTDVDE CEIGAHNCDM
HASCLNIPGS FKCSCREGWI GNGIKCIDLD ECSNGTHQCS INAQCVNTPG SYRCACSEGF
TGDGFTCSDV DECAENINLC ENGQCLNVPG AYRCECEMGF TPASDSRSCQ DIDECSFQNI
CVFGTCNNLP GMFHCICDDG YELDRTGGNC TDIDECADPI NCVNGLCVNT PGRYECNCPP
DFQLNPTGVG CVDNRVGNCY LKFGPRGDGS LSCNTEIGVG VSRSSCCCSL GKAWGNPCET
CPPVNSTEYY TLCPGGEGFR PNPITIILED IDECQELPGL CQGGNCINTF GSFQCECPQG
YYLSEDTRIC EDIDECFAHP GVCGPGTCYN TLGNYTCICP PEYMQVNGGH NCMDMRKSFC
YRSYNGTTCE NELPFNVTKR MCCCTYNVGK AWNKPCEPCP TPGTADFKTI CGNIPGFTFD
IHTGKAVDID ECKEIPGICA NGVCINQIGS FRCECPTGFS YNDLLLVCED IDECSNGDNL
CQRNADCINS PGSYRCECAA GFKLSPNGAC VDRNECLEIP NVCSHGLCVD LQGSYQCICH
NGFKASQDQT MCMDVDECER HPCGNGTCKN TVGSYNCLCY PGFELTHNND CLDIDECSSF
FGQVCRNGRC FNEIGSFKCL CNEGYELTPD GKNCIDTNEC VALPGSCSPG TCQNLEGSFR
CICPPGYEVK SENCIDINEC DEDPNICLFG SCTNTPGGFQ CLCPPGFVLS DNGRRCFDTR
QSFCFTNFEN GKCSVPKAFN TTKAKCCCSK MPGEGWGDPC ELCPKDDEVA FQDLCPYGHG
TVPSLHDTRE DVNECLESPG ICSNGQCINT DGSFRCECPM GYNLDYTGVR CVDTDECSIG
NPCGNGTCTN VIGSFECNCN EGFEPGPMMN CEDINECAQN PLLCAFRCMN TFGSYECTCP
IGYALREDQK MCKDLDECAE GLHDCESRGM MCKNLIGTFM CICPPGMARR PDGEGCVDEN
ECRTKPGICE NGRCVNIIGS YRCECNEGFQ SSSSGTECLD NRQGLCFAEV LQTICQMASS
SRNLVTKSEC CCDGGRGWGH QCELCPLPGT AQYKKICPHG PGYTTDGRDI DECKVMPNLC
TNGQCINTMG SFRCFCKVGY TTDISGTSCI DLDECSQSPK PCNYICKNTE GSYQCSCPRG
YVLQEDGKTC KDLDECQTKQ HNCQFLCVNT LGGFTCKCPP GFTQHHTACI DNNECGSQPS
LCGAKGICQN TPGSFSCECQ RGFSLDATGL NCEDVDECDG NHRCQHGCQN ILGGYRCGCP
QGYIQHYQWN QCVDENECSN PNACGSASCY NTLGSYKCAC PSGFSFDQFS SACHDVNECS
SSKNPCNYGC SNTEGGYLCG CPPGYYRVGQ GHCVSGMGFN KGQYLSLDTE VDEENALSPE
ACYECKINGY SKKDSRQKRS IHEPDPTAVE QISLESVDMD SPVNMKFNLS HLGSKEHILE
LRPAIQPLNN HIRYVISQGN DDSVFRIHQR NGLSYLHTAK KKLMPGTYTL EITSIPLYKK
KELKKLEESN EDDYLLGELG EALRMRLQIQ LY
