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   27-MAR-2024, entry version 173.
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}.
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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; 25.
DR   IntAct; Q9HCB6; 7.
DR   STRING; 9606.ENSP00000460236; -.
DR   GlyConnect; 1768; 5 N-Linked glycans (1 site).
DR   GlyCosmos; Q9HCB6; 13 sites, 7 glycans.
DR   GlyGen; Q9HCB6; 14 sites, 5 N-linked glycans (1 site), 3 O-linked glycans (4 sites).
DR   iPTMnet; Q9HCB6; -.
DR   PhosphoSitePlus; Q9HCB6; -.
DR   BioMuta; SPON1; -.
DR   DMDM; 52783472; -.
DR   EPD; Q9HCB6; -.
DR   jPOST; Q9HCB6; -.
DR   MassIVE; Q9HCB6; -.
DR   PaxDb; 9606-ENSP00000460236; -.
DR   PeptideAtlas; Q9HCB6; -.
DR   ProteomicsDB; 81664; -.
DR   Pumba; Q9HCB6; -.
DR   Antibodypedia; 62004; 178 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   AGR; HGNC:11252; -.
DR   CTD; 10418; -.
DR   DisGeNET; 10418; -.
DR   GeneCards; SPON1; -.
DR   HGNC; HGNC:11252; SPON1.
DR   HPA; ENSG00000262655; Low tissue specificity.
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; MMPPKEG; -.
DR   OrthoDB; 5404502at2759; -.
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; 9 hits in 255 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 195 other cell types or tissues.
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: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; 2.60.40.2130; F-spondin domain; 1.
DR   Gene3D; 2.60.40.4060; Reeler domain; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 6.
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   NCBIfam; NF038123; NF038123_dom; 1.
DR   PANTHER; PTHR11311; SPONDIN; 1.
DR   PANTHER; PTHR11311:SF16; SPONDIN-1; 1.
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; TSP-1 type 1 repeat; 6.
DR   PROSITE; PS51019; REELIN; 1.
DR   PROSITE; PS51020; SPONDIN; 1.
DR   PROSITE; PS50092; TSP1; 6.
DR   Genevisible; Q9HCB6; HS.
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
//