SPON1_HUMAN
ID SPON1_HUMAN Reviewed; 807 AA.
AC Q9HCB6; A8K6W5; O94862; Q8NCD7; Q8WUR5;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Spondin-1;
DE AltName: Full=F-spondin;
DE AltName: Full=Vascular smooth muscle cell growth-promoting factor;
DE Flags: Precursor;
GN Name=SPON1; Synonyms=KIAA0762, VSGP;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Ovary;
RX PubMed=11368520; DOI=10.1006/abbi.2001.2367;
RA Miyamoto K., Morishita Y., Yamazaki M., Minamino N., Kangawa K., Matsuo H.,
RA Mizutani T., Yamada K., Minegishi T.;
RT "Isolation and characterization of vascular smooth muscle cell growth
RT promoting factor from bovine ovarian follicular fluid and its cDNA cloning
RT from bovine and human ovary.";
RL Arch. Biochem. Biophys. 390:93-100(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [LARGE SCALE MRNA] OF 84-807, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [6]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [7]
RP GLYCOSYLATION AT TRP-448; TRP-451; TRP-507; TRP-510; TRP-564; TRP-620;
RP TRP-623 AND TRP-674.
RX PubMed=12096136; DOI=10.1074/mcp.m100011-mcp200;
RA Gonzalez de Peredo A., Klein D., Macek B., Hess D., Peter-Katalinic J.,
RA Hofsteenge J.;
RT "C-mannosylation and O-fucosylation of thrombospondin type 1 repeats.";
RL Mol. Cell. Proteomics 1:11-18(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 40-186, AND DISULFIDE BONDS.
RX PubMed=19020352; DOI=10.1107/s0907444908028308;
RA Nagae M., Nishikawa K., Yasui N., Yamasaki M., Nogi T., Takagi J.;
RT "Structure of the F-spondin reeler domain reveals a unique beta-sandwich
RT fold with a deformable disulfide-bonded loop.";
RL Acta Crystallogr. D 64:1138-1145(2008).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-194, AND DISULFIDE BONDS.
RX PubMed=18602404; DOI=10.1016/j.jmb.2008.06.045;
RA Tan K., Duquette M., Liu J.H., Lawler J., Wang J.H.;
RT "The crystal structure of the heparin-binding reelin-N domain of f-
RT spondin.";
RL J. Mol. Biol. 381:1213-1223(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 191-434 IN COMPLEX WITH CALCIUM,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-214.
RX PubMed=21569239; DOI=10.1186/1472-6807-11-22;
RA Tan K., Lawler J.;
RT "The structure of the Ca+-binding, glycosylated F-spondin domain of F-
RT spondin - A C2-domain variant in an extracellular matrix protein.";
RL BMC Struct. Biol. 11:22-22(2011).
CC -!- FUNCTION: Cell adhesion protein that promotes the attachment of spinal
CC cord and sensory neuron cells and the outgrowth of neurites in vitro.
CC May contribute to the growth and guidance of axons in both the spinal
CC cord and the PNS (By similarity). Major factor for vascular smooth
CC muscle cell. {ECO:0000250}.
CC -!- SUBUNIT: Binds to the central extracellular domain of APP and inhibits
CC beta-secretase cleavage of APP. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9HCB6; P05067-4: APP; NbExp=3; IntAct=EBI-2431846, EBI-302641;
CC Q9HCB6; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2431846, EBI-3867333;
CC Q9HCB6; Q99750: MDFI; NbExp=3; IntAct=EBI-2431846, EBI-724076;
CC Q9HCB6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2431846, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highest expression in lung, lower expression in
CC brain, heart, kidney, liver and testis, and lowest expression in
CC pancreas, skeletal muscle and ovary. Not expressed in spleen.
CC {ECO:0000269|PubMed:11368520, ECO:0000269|PubMed:9872452}.
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; AB051390; BAB18461.1; -; mRNA.
DR EMBL; AK074803; BAC11217.1; -; mRNA.
DR EMBL; AK291780; BAF84469.1; -; mRNA.
DR EMBL; CH471064; EAW68488.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68489.1; -; Genomic_DNA.
DR EMBL; BC019825; AAH19825.1; -; mRNA.
DR EMBL; BC136513; AAI36514.1; -; mRNA.
DR EMBL; BC136563; AAI36564.1; -; mRNA.
DR EMBL; AB018305; BAA34482.2; -; mRNA.
DR CCDS; CCDS73262.1; -.
DR RefSeq; NP_006099.2; NM_006108.3.
DR PDB; 2ZOT; X-ray; 2.70 A; A/B/C/D=29-198.
DR PDB; 2ZOU; X-ray; 1.45 A; A/B=40-186.
DR PDB; 3COO; X-ray; 2.00 A; A/B=29-194.
DR PDB; 3Q13; X-ray; 1.95 A; A=191-434.
DR PDBsum; 2ZOT; -.
DR PDBsum; 2ZOU; -.
DR PDBsum; 3COO; -.
DR PDBsum; 3Q13; -.
DR AlphaFoldDB; Q9HCB6; -.
DR SMR; Q9HCB6; -.
DR BioGRID; 115687; 24.
DR IntAct; Q9HCB6; 7.
DR STRING; 9606.ENSP00000460236; -.
DR GlyConnect; 1768; 5 N-Linked glycans (1 site).
DR GlyGen; Q9HCB6; 13 sites, 5 N-linked glycans (1 site), 2 O-linked glycans (3 sites).
DR iPTMnet; Q9HCB6; -.
DR PhosphoSitePlus; Q9HCB6; -.
DR BioMuta; SPON1; -.
DR DMDM; 52783472; -.
DR EPD; Q9HCB6; -.
DR jPOST; Q9HCB6; -.
DR MassIVE; Q9HCB6; -.
DR PeptideAtlas; Q9HCB6; -.
DR PRIDE; Q9HCB6; -.
DR ProteomicsDB; 81664; -.
DR Antibodypedia; 62004; 166 antibodies from 26 providers.
DR DNASU; 10418; -.
DR Ensembl; ENST00000576479.4; ENSP00000460236.1; ENSG00000262655.4.
DR GeneID; 10418; -.
DR KEGG; hsa:10418; -.
DR MANE-Select; ENST00000576479.4; ENSP00000460236.1; NM_006108.4; NP_006099.2.
DR UCSC; uc031xfv.2; human.
DR CTD; 10418; -.
DR DisGeNET; 10418; -.
DR GeneCards; SPON1; -.
DR HGNC; HGNC:11252; SPON1.
DR HPA; ENSG00000262655; Tissue enhanced (gallbladder).
DR MIM; 604989; gene.
DR neXtProt; NX_Q9HCB6; -.
DR OpenTargets; ENSG00000262655; -.
DR PharmGKB; PA36082; -.
DR VEuPathDB; HostDB:ENSG00000262655; -.
DR eggNOG; KOG3539; Eukaryota.
DR GeneTree; ENSGT00940000154910; -.
DR HOGENOM; CLU_014540_1_0_1; -.
DR InParanoid; Q9HCB6; -.
DR OMA; CLRGAGM; -.
DR OrthoDB; 517669at2759; -.
DR PhylomeDB; Q9HCB6; -.
DR PathwayCommons; Q9HCB6; -.
DR Reactome; R-HSA-5083635; Defective B3GALTL causes PpS.
DR Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
DR SignaLink; Q9HCB6; -.
DR SIGNOR; Q9HCB6; -.
DR BioGRID-ORCS; 10418; 8 hits in 199 CRISPR screens.
DR ChiTaRS; SPON1; human.
DR EvolutionaryTrace; Q9HCB6; -.
DR GeneWiki; Spondin_1; -.
DR GenomeRNAi; 10418; -.
DR Pharos; Q9HCB6; Tbio.
DR PRO; PR:Q9HCB6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9HCB6; protein.
DR Bgee; ENSG00000262655; Expressed in gall bladder and 193 other tissues.
DR Genevisible; Q9HCB6; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISS:BHF-UCL.
DR GO; GO:0050693; F:LBD domain binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl.
DR GO; GO:1902993; P:positive regulation of amyloid precursor protein catabolic process; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0010954; P:positive regulation of protein processing; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR CDD; cd08544; Reeler; 1.
DR Gene3D; 2.20.100.10; -; 6.
DR Gene3D; 2.60.40.2130; -; 1.
DR Gene3D; 2.60.40.4060; -; 1.
DR InterPro; IPR002861; Reeler_dom.
DR InterPro; IPR042307; Reeler_sf.
DR InterPro; IPR009465; Spondin_N.
DR InterPro; IPR038678; Spondin_N_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR044004; TSP1_spondin_dom.
DR Pfam; PF02014; Reeler; 1.
DR Pfam; PF06468; Spond_N; 1.
DR Pfam; PF19028; TSP1_spondin; 1.
DR Pfam; PF00090; TSP_1; 5.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF82895; SSF82895; 6.
DR PROSITE; PS51019; REELIN; 1.
DR PROSITE; PS51020; SPONDIN; 1.
DR PROSITE; PS50092; TSP1; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..807
FT /note="Spondin-1"
FT /id="PRO_0000035865"
FT DOMAIN 29..194
FT /note="Reelin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00363"
FT DOMAIN 195..388
FT /note="Spondin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00364"
FT DOMAIN 442..495
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 501..555
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 558..611
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 614..666
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 668..721
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 754..806
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21569239,
FT ECO:0007744|PDB:3Q13"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21569239,
FT ECO:0007744|PDB:3Q13"
FT BINDING 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21569239,
FT ECO:0007744|PDB:3Q13"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21569239,
FT ECO:0007744|PDB:3Q13"
FT CARBOHYD 448
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:12096136"
FT CARBOHYD 451
FT /note="C-linked (Man) tryptophan; partial"
FT /evidence="ECO:0000269|PubMed:12096136"
FT CARBOHYD 507
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:12096136"
FT CARBOHYD 510
FT /note="C-linked (Man) tryptophan; partial"
FT /evidence="ECO:0000269|PubMed:12096136"
FT CARBOHYD 564
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:12096136"
FT CARBOHYD 620
FT /note="C-linked (Man) tryptophan; partial"
FT /evidence="ECO:0000269|PubMed:12096136"
FT CARBOHYD 623
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:12096136"
FT CARBOHYD 674
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:12096136"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..128
FT /evidence="ECO:0000269|PubMed:18602404,
FT ECO:0000269|PubMed:19020352, ECO:0007744|PDB:2ZOT,
FT ECO:0007744|PDB:2ZOU, ECO:0007744|PDB:3COO"
FT DISULFID 156..182
FT /evidence="ECO:0000269|PubMed:18602404,
FT ECO:0000269|PubMed:19020352, ECO:0007744|PDB:2ZOT,
FT ECO:0007744|PDB:2ZOU, ECO:0007744|PDB:3COO"
FT DISULFID 199..336
FT /evidence="ECO:0000269|PubMed:21569239,
FT ECO:0007744|PDB:3Q13"
FT DISULFID 200..340
FT /evidence="ECO:0000269|PubMed:21569239,
FT ECO:0007744|PDB:3Q13"
FT DISULFID 202..415
FT /evidence="ECO:0000269|PubMed:21569239,
FT ECO:0007744|PDB:3Q13"
FT DISULFID 443..480
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 454..489
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 459..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 502..538
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 513..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 548..554
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 559..595
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 570..574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 605..610
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 615..650
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 626..630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 660..665
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CONFLICT 500
FT /note="S -> P (in Ref. 2; BAC11217)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="T -> M (in Ref. 1; BAB18461)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="C -> Y (in Ref. 2; BAC11217)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="C -> R (in Ref. 2; BAC11217)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="I -> T (in Ref. 4; AAH19825)"
FT /evidence="ECO:0000305"
FT CONFLICT 729
FT /note="L -> P (in Ref. 1; BAB18461)"
FT /evidence="ECO:0000305"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:3COO"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3COO"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:2ZOU"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 157..169
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2ZOU"
FT STRAND 203..213
FT /evidence="ECO:0007829|PDB:3Q13"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:3Q13"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:3Q13"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:3Q13"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:3Q13"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:3Q13"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:3Q13"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:3Q13"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:3Q13"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:3Q13"
FT STRAND 302..311
FT /evidence="ECO:0007829|PDB:3Q13"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:3Q13"
FT STRAND 324..334
FT /evidence="ECO:0007829|PDB:3Q13"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:3Q13"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:3Q13"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3Q13"
FT STRAND 401..412
FT /evidence="ECO:0007829|PDB:3Q13"
SQ SEQUENCE 807 AA; 90973 MW; CEA84A83F206A5A5 CRC64;
MRLSPAPLKL SRTPALLALA LPLAAALAFS DETLDKVPKS EGYCSRILRA QGTRREGYTE
FSLRVEGDPD FYKPGTSYRV TLSAAPPSYF RGFTLIALRE NREGDKEEDH AGTFQIIDEE
ETQFMSNCPV AVTESTPRRR TRIQVFWIAP PAGTGCVILK ASIVQKRIIY FQDEGSLTKK
LCEQDSTFDG VTDKPILDCC ACGTAKYRLT FYGNWSEKTH PKDYPRRANH WSAIIGGSHS
KNYVLWEYGG YASEGVKQVA ELGSPVKMEE EIRQQSDEVL TVIKAKAQWP AWQPLNVRAA
PSAEFSVDRT RHLMSFLTMM GPSPDWNVGL SAEDLCTKEC GWVQKVVQDL IPWDAGTDSG
VTYESPNKPT IPQEKIRPLT SLDHPQSPFY DPEGGSITQV ARVVIERIAR KGEQCNIVPD
NVDDIVADLA PEEKDEDDTP ETCIYSNWSP WSACSSSTCD KGKRMRQRML KAQLDLSVPC
PDTQDFQPCM GPGCSDEDGS TCTMSEWITW SPCSISCGMG MRSRERYVKQ FPEDGSVCTL
PTEETEKCTV NEECSPSSCL MTEWGEWDEC SATCGMGMKK RHRMIKMNPA DGSMCKAETS
QAEKCMMPEC HTIPCLLSPW SEWSDCSVTC GKGMRTRQRM LKSLAELGDC NEDLEQVEKC
MLPECPIDCE LTEWSQWSEC NKSCGKGHVI RTRMIQMEPQ FGGAPCPETV QRKKCRIRKC
LRNPSIQKLR WREARESRRS EQLKEESEGE QFPGCRMRPW TAWSECTKLC GGGIQERYMT
VKKRFKSSQF TSCKDKKEIR ACNVHPC
