NID1_MOUSE
ID NID1_MOUSE Reviewed; 1245 AA.
AC P10493; Q3TKX9; Q8BQI3; Q8C3U8; Q8C9P6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Nidogen-1;
DE Short=NID-1;
DE AltName: Full=Entactin;
DE Flags: Precursor;
GN Name=Nid1; Synonyms=Ent;
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], AND PROTEIN SEQUENCE OF 29-40.
RX PubMed=3264556; DOI=10.1083/jcb.107.6.2749;
RA Durkin M.E., Chakravarti S., Bartos B.B., Liu S.H., Friedman R.L.,
RA Chung A.E.;
RT "Amino acid sequence and domain structure of entactin. Homology with
RT epidermal growth factor precursor and low density lipoprotein receptor.";
RL J. Cell Biol. 107:2749-2756(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2496973; DOI=10.1002/j.1460-2075.1989.tb03349.x;
RA Mann K., Deutzmann R., Aumailley M., Timpl R., Raimondi L., Yamamda Y.,
RA Pan T.-C., Conway D., Chu M.-L.;
RT "Amino acid sequence of mouse nidogen, a multidomain basement membrane
RT protein with binding activity for laminin, collagen IV and cells.";
RL EMBO J. 8:65-72(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic lung, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-251.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8224873; DOI=10.1016/0378-1119(93)90205-h;
RA Durkin M.E., Liu S.H., Reing J., Chung A.E.;
RT "Characterization of the 5' end of the mouse Ent gene encoding the basement
RT membrane protein, entactin.";
RL Gene 132:261-266(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1207-1245.
RC STRAIN=C57BL/6J X CBA/J;
RX PubMed=7601446; DOI=10.1016/0888-7543(95)80204-y;
RA Durkin M.E., Wewer U.M., Chung A.E.;
RT "Exon organization of the mouse entactin gene corresponds to the structural
RT domains of the polypeptide and has regional homology to the low-density
RT lipoprotein receptor gene.";
RL Genomics 26:219-228(1995).
RN [7]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=3084254; DOI=10.1111/j.1432-1033.1986.tb09605.x;
RA Paulsson M., Deutzmann R., Dziadek M., Nowack H., Timpl R., Weber S.,
RA Engel J.;
RT "Purification and structural characterization of intact and fragmented
RT nidogen obtained from a tumor basement membrane.";
RL Eur. J. Biochem. 156:467-478(1986).
RN [8]
RP GLYCOSYLATION AT ASN-187; THR-299; SER-331; THR-337; THR-345; THR-348;
RP ASN-415; THR-920 AND THR-933, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8326911; DOI=10.1016/s0934-8832(11)80005-3;
RA Fujiwara S., Shinkai H., Mann K., Timpl R.;
RT "Structure and localization of O- and N-linked oligosaccharide chains on
RT basement membrane protein nidogen.";
RL Matrix 13:215-222(1993).
RN [9]
RP INTERACTION WITH FBLN1.
RX PubMed=9299350; DOI=10.1006/jmbi.1997.1244;
RA Adam S., Goehring W., Wiedemann H., Chu M.-L., Timpl R., Kostka G.;
RT "Binding of fibulin-1 to nidogen depends on its C-terminal globular domain
RT and a specific array of calcium-binding epidermal growth factor-like (EG)
RT modules.";
RL J. Mol. Biol. 272:226-236(1997).
RN [10]
RP INTERACTION WITH LGALS3BP.
RX PubMed=9501082; DOI=10.1093/emboj/17.6.1606;
RA Sasaki T., Brakebusch C., Engel J., Timpl R.;
RT "Mac-2 binding protein is a cell-adhesive protein of the extracellular
RT matrix which self-assembles into ring-like structures and binds beta1
RT integrins, collagens and fibronectin.";
RL EMBO J. 17:1606-1613(1998).
RN [11]
RP INTERACTION WITH FBLN1.
RX PubMed=11589703; DOI=10.1046/j.0014-2956.2001.02437.x;
RA Ries A., Goehring W., Fox J.W., Timpl R., Sasaki T.;
RT "Recombinant domains of mouse nidogen-1 and their binding to basement
RT membrane proteins and monoclonal antibodies.";
RL Eur. J. Biochem. 268:5119-5128(2001).
RN [12]
RP INTERACTION WITH PLXDC1.
RX PubMed=16574105; DOI=10.1016/j.febslet.2006.03.033;
RA Lee H.K., Seo I.A., Park H.K., Park H.T.;
RT "Identification of the basement membrane protein nidogen as a candidate
RT ligand for tumor endothelial marker 7 in vitro and in vivo.";
RL FEBS Lett. 580:2253-2257(2006).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 381-665.
RX PubMed=11427896; DOI=10.1038/89683;
RA Hopf M., Gohring W., Ries A., Timpl R., Hohenester E.;
RT "Crystal structure and mutational analysis of a perlecan-binding fragment
RT of nidogen-1.";
RL Nat. Struct. Biol. 8:634-640(2001).
CC -!- FUNCTION: Sulfated glycoprotein widely distributed in basement
CC membranes and tightly associated with laminin. Also binds to collagen
CC IV and perlecan. It probably has a role in cell-extracellular matrix
CC interactions.
CC -!- SUBUNIT: Interacts with FBLN1 and LGALS3BP. Interacts with PLXDC1.
CC {ECO:0000269|PubMed:11589703, ECO:0000269|PubMed:16574105,
CC ECO:0000269|PubMed:9299350, ECO:0000269|PubMed:9501082}.
CC -!- INTERACTION:
CC P10493; P02468: Lamc1; NbExp=5; IntAct=EBI-1032117, EBI-7059830;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:8326911}.
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DR EMBL; X14194; CAA32408.1; -; mRNA.
DR EMBL; X14480; CAA32642.1; -; mRNA.
DR EMBL; AK041633; BAC31014.1; -; mRNA.
DR EMBL; AK084876; BAC39300.1; -; mRNA.
DR EMBL; AK144878; BAE26114.1; -; mRNA.
DR EMBL; AK166779; BAE39014.1; -; mRNA.
DR EMBL; BC131669; AAI31670.1; -; mRNA.
DR EMBL; AH003206; AAA77652.1; -; Genomic_DNA.
DR EMBL; X83093; CAA58148.1; -; Genomic_DNA.
DR CCDS; CCDS26244.1; -.
DR PIR; S02730; MMMSND.
DR RefSeq; NP_035047.2; NM_010917.2.
DR PDB; 1GL4; X-ray; 2.00 A; A=385-665.
DR PDB; 1H4U; X-ray; 2.20 A; A=395-659.
DR PDB; 1NPE; X-ray; 2.30 A; A=941-1207.
DR PDBsum; 1GL4; -.
DR PDBsum; 1H4U; -.
DR PDBsum; 1NPE; -.
DR AlphaFoldDB; P10493; -.
DR SMR; P10493; -.
DR BioGRID; 201770; 15.
DR ComplexPortal; CPX-1281; Laminin111-nidogen complex.
DR ComplexPortal; CPX-1284; Laminin211-nidogen complex.
DR ComplexPortal; CPX-1286; Laminin221-nidogen complex.
DR IntAct; P10493; 6.
DR MINT; P10493; -.
DR STRING; 10090.ENSMUSP00000005532; -.
DR GlyGen; P10493; 9 sites.
DR iPTMnet; P10493; -.
DR MetOSite; P10493; -.
DR PhosphoSitePlus; P10493; -.
DR CPTAC; non-CPTAC-3848; -.
DR EPD; P10493; -.
DR jPOST; P10493; -.
DR MaxQB; P10493; -.
DR PaxDb; P10493; -.
DR PeptideAtlas; P10493; -.
DR PRIDE; P10493; -.
DR ProteomicsDB; 252964; -.
DR Antibodypedia; 4102; 425 antibodies from 34 providers.
DR DNASU; 18073; -.
DR Ensembl; ENSMUST00000005532; ENSMUSP00000005532; ENSMUSG00000005397.
DR GeneID; 18073; -.
DR KEGG; mmu:18073; -.
DR UCSC; uc007pmf.2; mouse.
DR CTD; 4811; -.
DR MGI; MGI:97342; Nid1.
DR VEuPathDB; HostDB:ENSMUSG00000005397; -.
DR eggNOG; KOG1214; Eukaryota.
DR GeneTree; ENSGT00940000156318; -.
DR HOGENOM; CLU_003163_1_0_1; -.
DR InParanoid; P10493; -.
DR OMA; HVSRLQF; -.
DR OrthoDB; 95286at2759; -.
DR PhylomeDB; P10493; -.
DR TreeFam; TF320666; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR BioGRID-ORCS; 18073; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Nid1; mouse.
DR EvolutionaryTrace; P10493; -.
DR PRO; PR:P10493; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P10493; protein.
DR Bgee; ENSMUSG00000005397; Expressed in endothelial cell of lymphatic vessel and 274 other tissues.
DR Genevisible; P10493; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098637; C:protein complex involved in cell-matrix adhesion; IC:ComplexPortal.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005518; F:collagen binding; IDA:MGI.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0043236; F:laminin binding; ISO:MGI.
DR GO; GO:0043237; F:laminin-1 binding; IDA:MGI.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR GO; GO:0032836; P:glomerular basement membrane development; IMP:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IC:ComplexPortal.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IC:ComplexPortal.
DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; IC:ComplexPortal.
DR GO; GO:0110011; P:regulation of basement membrane organization; IC:ComplexPortal.
DR CDD; cd00255; nidG2; 1.
DR CDD; cd00191; TY; 1.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.40.155.10; -; 1.
DR Gene3D; 4.10.800.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; IPR006605; G2_nidogen/fibulin_G2F.
DR InterPro; IPR009017; GFP.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF12947; EGF_3; 2.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF07474; G2F; 1.
DR Pfam; PF00058; Ldl_recept_b; 3.
DR Pfam; PF06119; NIDO; 1.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00682; G2F; 1.
DR SMART; SM00135; LY; 5.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00211; TY; 1.
DR SUPFAM; SSF54511; SSF54511; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR SUPFAM; SSF57610; SSF57610; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 4.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51120; LDLRB; 4.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50993; NIDOGEN_G2; 1.
DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Basement membrane; Calcium; Cell adhesion;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal; Sulfation.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:3264556"
FT CHAIN 29..1245
FT /note="Nidogen-1"
FT /id="PRO_0000007670"
FT DOMAIN 106..268
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 384..424
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 428..665
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00348"
FT DOMAIN 666..707
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 708..749
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 756..799
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 800..838
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 844..917
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500"
FT REPEAT 988..1030
FT /note="LDL-receptor class B 1"
FT REPEAT 1031..1073
FT /note="LDL-receptor class B 2"
FT REPEAT 1074..1118
FT /note="LDL-receptor class B 3"
FT REPEAT 1119..1160
FT /note="LDL-receptor class B 4"
FT DOMAIN 1206..1242
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 307..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 700..702
FT /note="Cell attachment site"
FT SITE 457
FT /note="Involved in perlecan binding"
FT SITE 459
FT /note="Involved in perlecan binding"
FT SITE 648
FT /note="Involved in perlecan binding"
FT MOD_RES 290
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 295
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8326911"
FT CARBOHYD 299
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8326911"
FT CARBOHYD 331
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:8326911"
FT CARBOHYD 337
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8326911"
FT CARBOHYD 345
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8326911"
FT CARBOHYD 348
FT /note="O-linked (GalNAc...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:8326911"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8326911"
FT CARBOHYD 920
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8326911"
FT CARBOHYD 933
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8326911"
FT DISULFID 388..401
FT DISULFID 395..410
FT DISULFID 409..616
FT DISULFID 412..423
FT DISULFID 670..683
FT /evidence="ECO:0000250"
FT DISULFID 677..693
FT /evidence="ECO:0000250"
FT DISULFID 695..706
FT /evidence="ECO:0000250"
FT DISULFID 712..725
FT /evidence="ECO:0000250"
FT DISULFID 719..734
FT /evidence="ECO:0000250"
FT DISULFID 736..748
FT /evidence="ECO:0000250"
FT DISULFID 760..775
FT /evidence="ECO:0000250"
FT DISULFID 767..785
FT /evidence="ECO:0000250"
FT DISULFID 787..798
FT /evidence="ECO:0000250"
FT DISULFID 804..815
FT /evidence="ECO:0000250"
FT DISULFID 809..824
FT /evidence="ECO:0000250"
FT DISULFID 826..837
FT /evidence="ECO:0000250"
FT DISULFID 847..876
FT /evidence="ECO:0000250"
FT DISULFID 887..894
FT /evidence="ECO:0000250"
FT DISULFID 896..917
FT /evidence="ECO:0000250"
FT DISULFID 1210..1221
FT /evidence="ECO:0000250"
FT DISULFID 1217..1230
FT /evidence="ECO:0000250"
FT DISULFID 1232..1241
FT /evidence="ECO:0000250"
FT CONFLICT 170
FT /note="P -> L (in Ref. 2; CAA32642)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="R -> K (in Ref. 2; CAA32642)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="A -> R (in Ref. 1; CAA32408)"
FT /evidence="ECO:0000305"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:1GL4"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 429..442
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 449..461
FT /evidence="ECO:0007829|PDB:1GL4"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 466..473
FT /evidence="ECO:0007829|PDB:1GL4"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:1GL4"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:1GL4"
FT HELIX 487..495
FT /evidence="ECO:0007829|PDB:1GL4"
FT HELIX 506..510
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 513..522
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 525..527
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 529..536
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 547..554
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 568..575
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 578..590
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 601..612
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 627..641
FT /evidence="ECO:0007829|PDB:1GL4"
FT TURN 642..645
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 646..656
FT /evidence="ECO:0007829|PDB:1GL4"
FT STRAND 942..960
FT /evidence="ECO:0007829|PDB:1NPE"
FT HELIX 964..966
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 968..984
FT /evidence="ECO:0007829|PDB:1NPE"
FT TURN 985..988
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 989..994
FT /evidence="ECO:0007829|PDB:1NPE"
FT TURN 995..998
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 999..1007
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1011..1014
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1021..1027
FT /evidence="ECO:0007829|PDB:1NPE"
FT TURN 1028..1031
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1032..1037
FT /evidence="ECO:0007829|PDB:1NPE"
FT TURN 1038..1041
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1042..1047
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1054..1057
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1062..1070
FT /evidence="ECO:0007829|PDB:1NPE"
FT TURN 1071..1074
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1075..1080
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1083..1085
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1087..1092
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1099..1102
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1109..1115
FT /evidence="ECO:0007829|PDB:1NPE"
FT TURN 1116..1119
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1120..1125
FT /evidence="ECO:0007829|PDB:1NPE"
FT TURN 1126..1129
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1130..1135
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1138..1146
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1150..1157
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1160..1165
FT /evidence="ECO:0007829|PDB:1NPE"
FT TURN 1166..1169
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1170..1175
FT /evidence="ECO:0007829|PDB:1NPE"
FT TURN 1176..1179
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1180..1185
FT /evidence="ECO:0007829|PDB:1NPE"
FT STRAND 1196..1199
FT /evidence="ECO:0007829|PDB:1NPE"
SQ SEQUENCE 1245 AA; 136538 MW; 92D12D128E6EF144 CRC64;
MLDASGCSWA MWTWALLQLL LLVGPGGCLN RQELFPFGPG QGDLELEAGD DVVSPSLELI
GELSFYDRTD ITSVYVTTNG IIAMSEPPAT EYHPGTFPPS FGSVAPFLAD LDTTDGLGNV
YYREDLSPFI IQMAAEYVQR GFPEVSFQPT SVVVVTWESV APYGGPSSSP AEEGKRNTFQ
AVLASSNSSS YAIFLYPEDG LQFFTTFSKK DESQVPAVVG FSKGLVGFLW KSNGAYNIFA
NDRESIENLA KSSNAGHQGV WVFEIGSPAT AKGVVSADVN LDLDDDGADY EDEDYDLVTS
HLGLEDVATP SPSHSPRRGY PDPHNVPRIL SPGYEATERP RGVPTERTRS FQLPAERFPQ
HHPQVIDVDE VEETGVVFSY NTGSQQTCAN NRHQCSVHAE CRDYATGFCC RCVANYTGNG
RQCVAEGSPQ RVNGKVKGRI FVGSSQVPVV FENTDLHSYV VMNHGRSYTA ISTIPETVGY
SLLPLAPIGG IIGWMFAVEQ DGFKNGFSIT GGEFTRQAEV TFLGHPGKLV LKQQFSGIDE
HGHLTISTEL EGRVPQIPYG ASVHIEPYTE LYHYSSSVIT SSSTREYTVM EPDQDGAAPS
HTHIYQWRQT ITFQECAHDD ARPALPSTQQ LSVDSVFVLY NKEERILRYA LSNSIGPVRD
GSPDALQNPC YIGTHGCDSN AACRPGPGTQ FTCECSIGFR GDGQTCYDID ECSEQPSRCG
NHAVCNNLPG TFRCECVEGY HFSDRGTCVA AEDQRPINYC ETGLHNCDIP QRAQCIYMGG
SSYTCSCLPG FSGDGRACRD VDECQHSRCH PDAFCYNTPG SFTCQCKPGY QGDGFRCMPG
EVSKTRCQLE REHILGAAGG ADAQRPTLQG MFVPQCDEYG HYVPTQCHHS TGYCWCVDRD
GRELEGSRTP PGMRPPCLST VAPPIHQGPV VPTAVIPLPP GTHLLFAQTG KIERLPLERN
TMKKTEAKAF LHIPAKVIIG LAFDCVDKVV YWTDISEPSI GRASLHGGEP TTIIRQDLGS
PEGIALDHLG RTIFWTDSQL DRIEVAKMDG TQRRVLFDTG LVNPRGIVTD PVRGNLYWTD
WNRDNPKIET SHMDGTNRRI LAQDNLGLPN GLTFDAFSSQ LCWVDAGTHR AECLNPAQPG
RRKVLEGLQY PFAVTSYGKN LYYTDWKTNS VIAMDLAISK EMDTFHPHKQ TRLYGITIAL
SQCPQGHNYC SVNNGGCTHL CLPTPGSRTC RCPDNTLGVD CIERK
