ID   NET1_HUMAN              Reviewed;         604 AA.
AC   O95631; E9KL51;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   27-MAR-2024, entry version 188.
DE   RecName: Full=Netrin-1;
DE   AltName: Full=Epididymis tissue protein Li 131P;
DE   Flags: Precursor;
GN   Name=NTN1; Synonyms=NTN1L;
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], INTERACTION WITH DCC, TISSUE SPECIFICITY, AND
RP   VARIANTS HIS-351 AND GLU-489.
RC   TISSUE=Brain stem, and Liver;
RX   PubMed=9950216;
RA   Meyerhardt J.A., Caca K., Eckstrand B.C., Hu G., Lengauer C., Banavali S.,
RA   Look A.T., Fearon E.R.;
RT   "Netrin-1: interaction with deleted in colorectal cancer (DCC) and
RT   alterations in brain tumors and neuroblastomas.";
RL   Cell Growth Differ. 10:35-42(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Epididymis;
RX   PubMed=20736409; DOI=10.1074/mcp.m110.001719;
RA   Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C.,
RA   Jin S., Liu J., Zhu P., Liu Y.;
RT   "Systematic mapping and functional analysis of a family of human epididymal
RT   secretory sperm-located proteins.";
RL   Mol. Cell. Proteomics 9:2517-2528(2010).
RN   [4]
RP   FUNCTION.
RX   PubMed=15343335; DOI=10.1038/nature02788;
RA   Mazelin L., Bernet A., Bonod-Bidaud C., Pays L., Arnaud S., Gespach C.,
RA   Bredesen D.E., Scoazec J.-Y., Mehlen P.;
RT   "Netrin-1 controls colorectal tumorigenesis by regulating apoptosis.";
RL   Nature 431:80-84(2004).
RN   [5]
RP   INTERACTION WITH DSCAM.
RX   PubMed=19196994; DOI=10.1073/pnas.0811083106;
RA   Liu G., Li W., Wang L., Kar A., Guan K.L., Rao Y., Wu J.Y.;
RT   "DSCAM functions as a netrin receptor in commissural axon pathfinding.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:2951-2956(2009).
RN   [6]
RP   SUBCELLULAR LOCATION, INVOLVEMENT IN MRMV4, VARIANTS MRMV4 ILE-518 DEL;
RP   ARG-601 AND SER-601, AND CHARACTERIZATION OF VARIANTS MRMV4 ILE-518 DEL;
RP   ARG-601 AND SER-601.
RX   PubMed=28945198; DOI=10.1172/jci95442;
RA   Meneret A., Franz E.A., Trouillard O., Oliver T.C., Zagar Y.,
RA   Robertson S.P., Welniarz Q., Gardner R.J.M., Gallea C., Srour M.,
RA   Depienne C., Jasoni C.L., Dubacq C., Riant F., Lamy J.C., Morel M.P.,
RA   Guerois R., Andreani J., Fouquet C., Doulazmi M., Vidailhet M.,
RA   Rouleau G.A., Brice A., Chedotal A., Dusart I., Roze E., Markie D.;
RT   "Mutations in the netrin-1 gene cause congenital mirror movements.";
RL   J. Clin. Invest. 127:3923-3936(2017).
RN   [7]
RP   FUNCTION.
RX   PubMed=28483977; DOI=10.1523/jneurosci.2617-16.2017;
RA   Shao Q., Yang T., Huang H., Alarmanazi F., Liu G.;
RT   "Uncoupling of UNC5C with Polymerized TUBB3 in Microtubules Mediates
RT   Netrin-1 Repulsion.";
RL   J. Neurosci. 37:5620-5633(2017).
CC   -!- FUNCTION: Netrins control guidance of CNS commissural axons and
CC       peripheral motor axons. Its association with either DCC or some UNC5
CC       receptors will lead to axon attraction or repulsion, respectively.
CC       Binding to UNC5C might cause dissociation of UNC5C from polymerized
CC       TUBB3 in microtubules and thereby lead to increased microtubule
CC       dynamics and axon repulsion (PubMed:28483977). Involved in dorsal root
CC       ganglion axon projection towards the spinal cord (PubMed:28483977). It
CC       also serves as a survival factor via its association with its receptors
CC       which prevent the initiation of apoptosis. Involved in tumorigenesis by
CC       regulating apoptosis (PubMed:15343335). {ECO:0000269|PubMed:15343335,
CC       ECO:0000269|PubMed:28483977}.
CC   -!- SUBUNIT: Binds to its receptors; DCC, UNC5A, UNC5B, UNC5C and probably
CC       UNC5D (PubMed:9950216). Binds to its receptor; DSCAM (PubMed:19196994).
CC       Interacts with APP (By similarity). {ECO:0000250|UniProtKB:O09118,
CC       ECO:0000269|PubMed:19196994, ECO:0000269|PubMed:9950216,
CC       ECO:0000303|PubMed:9950216}.
CC   -!- INTERACTION:
CC       O95631; PRO_0000000089 [P05067]: APP; NbExp=3; IntAct=EBI-2678626, EBI-20829246;
CC       O95631; PRO_0000000092 [P05067]: APP; NbExp=6; IntAct=EBI-2678626, EBI-821758;
CC       O95631; P43146: DCC; NbExp=4; IntAct=EBI-2678626, EBI-1222919;
CC       O95631; Q8NBI3: DRAXIN; NbExp=3; IntAct=EBI-2678626, EBI-10827752;
CC       O95631; Q8IZJ1-2: UNC5B; NbExp=2; IntAct=EBI-2678626, EBI-10832046;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28945198}. Cytoplasm
CC       {ECO:0000269|PubMed:28945198}. Note=Mainly secreted.
CC       {ECO:0000269|PubMed:28945198}.
CC   -!- TISSUE SPECIFICITY: Widely expressed in normal adult tissues with
CC       highest levels in heart, small intestine, colon, liver and prostate.
CC       Reduced expression in brain tumors and neuroblastomas. Expressed in
CC       epididymis (at protein level). {ECO:0000269|PubMed:20736409,
CC       ECO:0000269|PubMed:9950216}.
CC   -!- DISEASE: Mirror movements 4 (MRMV4) [MIM:618264]: A disorder
CC       characterized by contralateral involuntary movements that mirror
CC       voluntary ones. While mirror movements are occasionally found in young
CC       children, persistence beyond the age of 10 is abnormal. Mirror
CC       movements occur more commonly in the upper extremities. MRMV4
CC       inheritance is autosomal dominant. {ECO:0000269|PubMed:28945198}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
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; U75586; AAD09221.1; -; mRNA.
DR   EMBL; GU727649; ADU87650.1; -; mRNA.
DR   EMBL; AC090610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC005695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS11148.1; -.
DR   RefSeq; NP_004813.2; NM_004822.2.
DR   RefSeq; XP_006721658.1; XM_006721595.3.
DR   PDB; 4URT; X-ray; 3.10 A; A=39-453.
DR   PDB; 6FKQ; X-ray; 3.07 A; A=39-453.
DR   PDB; 7NDG; EM; 5.98 A; A/D/G=25-453.
DR   PDB; 7NE0; X-ray; 3.25 A; A=24-453.
DR   PDB; 7NE1; X-ray; 3.15 A; A=24-453.
DR   PDBsum; 4URT; -.
DR   PDBsum; 6FKQ; -.
DR   PDBsum; 7NDG; -.
DR   PDBsum; 7NE0; -.
DR   PDBsum; 7NE1; -.
DR   AlphaFoldDB; O95631; -.
DR   EMDB; EMD-12286; -.
DR   SASBDB; O95631; -.
DR   SMR; O95631; -.
DR   BioGRID; 114816; 17.
DR   DIP; DIP-46273N; -.
DR   IntAct; O95631; 9.
DR   STRING; 9606.ENSP00000173229; -.
DR   ChEMBL; CHEMBL1741307; -.
DR   GlyConnect; 1542; 1 N-Linked glycan (1 site).
DR   GlyCosmos; O95631; 4 sites, 1 glycan.
DR   GlyGen; O95631; 7 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (3 sites).
DR   iPTMnet; O95631; -.
DR   PhosphoSitePlus; O95631; -.
DR   BioMuta; NTN1; -.
DR   jPOST; O95631; -.
DR   MassIVE; O95631; -.
DR   MaxQB; O95631; -.
DR   PaxDb; 9606-ENSP00000173229; -.
DR   PeptideAtlas; O95631; -.
DR   ProteomicsDB; 50967; -.
DR   Pumba; O95631; -.
DR   Antibodypedia; 24762; 427 antibodies from 41 providers.
DR   DNASU; 9423; -.
DR   Ensembl; ENST00000173229.7; ENSP00000173229.2; ENSG00000065320.9.
DR   GeneID; 9423; -.
DR   KEGG; hsa:9423; -.
DR   MANE-Select; ENST00000173229.7; ENSP00000173229.2; NM_004822.3; NP_004813.2.
DR   UCSC; uc002glw.4; human.
DR   AGR; HGNC:8029; -.
DR   CTD; 9423; -.
DR   DisGeNET; 9423; -.
DR   GeneCards; NTN1; -.
DR   GeneReviews; NTN1; -.
DR   HGNC; HGNC:8029; NTN1.
DR   HPA; ENSG00000065320; Tissue enhanced (heart).
DR   MalaCards; NTN1; -.
DR   MIM; 601614; gene.
DR   MIM; 618264; phenotype.
DR   neXtProt; NX_O95631; -.
DR   OpenTargets; ENSG00000065320; -.
DR   Orphanet; 238722; Familial congenital mirror movements.
DR   PharmGKB; PA31813; -.
DR   VEuPathDB; HostDB:ENSG00000065320; -.
DR   eggNOG; KOG3512; Eukaryota.
DR   GeneTree; ENSGT00940000153882; -.
DR   HOGENOM; CLU_018213_2_0_1; -.
DR   InParanoid; O95631; -.
DR   OMA; NSCVACN; -.
DR   OrthoDB; 2916807at2759; -.
DR   PhylomeDB; O95631; -.
DR   TreeFam; TF352481; -.
DR   PathwayCommons; O95631; -.
DR   Reactome; R-HSA-373752; Netrin-1 signaling.
DR   Reactome; R-HSA-376172; DSCAM interactions.
DR   Reactome; R-HSA-418885; DCC mediated attractive signaling.
DR   Reactome; R-HSA-418886; Netrin mediated repulsion signals.
DR   Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
DR   Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR   SignaLink; O95631; -.
DR   SIGNOR; O95631; -.
DR   BioGRID-ORCS; 9423; 16 hits in 1152 CRISPR screens.
DR   ChiTaRS; NTN1; human.
DR   GeneWiki; NTN1; -.
DR   GenomeRNAi; 9423; -.
DR   Pharos; O95631; Tbio.
DR   PRO; PR:O95631; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; O95631; Protein.
DR   Bgee; ENSG00000065320; Expressed in mucosa of stomach and 147 other cell types or tissues.
DR   ExpressionAtlas; O95631; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR   GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0033564; P:anterior/posterior axon guidance; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0032488; P:Cdc42 protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0061643; P:chemorepulsion of axon; ISS:UniProtKB.
DR   GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
DR   GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR   GO; GO:0060603; P:mammary gland duct morphogenesis; IEA:Ensembl.
DR   GO; GO:0097475; P:motor neuron migration; IEA:Ensembl.
DR   GO; GO:0030517; P:negative regulation of axon extension; IEA:Ensembl.
DR   GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
DR   GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR   GO; GO:2000147; P:positive regulation of cell motility; ISS:UniProtKB.
DR   GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
DR   GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR   GO; GO:1903975; P:regulation of glial cell migration; IEA:Ensembl.
DR   GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006930; P:substrate-dependent cell migration, cell extension; ISS:UniProtKB.
DR   CDD; cd00055; EGF_Lam; 3.
DR   CDD; cd03579; NTR_netrin-1_like; 1.
DR   Gene3D; 2.40.50.120; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR018933; Netrin_module_non-TIMP.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00053; Laminin_EGF; 3.
DR   Pfam; PF00055; Laminin_N; 1.
DR   Pfam; PF01759; NTR; 1.
DR   SMART; SM00643; C345C; 1.
DR   SMART; SM00180; EGF_Lam; 3.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF50242; TIMP-like; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 3.
DR   PROSITE; PS50027; EGF_LAM_2; 3.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
DR   PROSITE; PS50189; NTR; 1.
DR   Genevisible; O95631; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Cytoplasm; Disease variant; Disulfide bond;
KW   Glycoprotein; Laminin EGF-like domain; Reference proteome; Repeat;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..604
FT                   /note="Netrin-1"
FT                   /id="PRO_0000017082"
FT   DOMAIN          47..284
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT   DOMAIN          285..340
FT                   /note="Laminin EGF-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          341..403
FT                   /note="Laminin EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          404..453
FT                   /note="Laminin EGF-like 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT   DOMAIN          472..601
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   MOTIF           530..532
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        417
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        119..152
FT                   /evidence="ECO:0000250"
FT   DISULFID        285..294
FT                   /evidence="ECO:0000250"
FT   DISULFID        287..304
FT                   /evidence="ECO:0000250"
FT   DISULFID        306..315
FT                   /evidence="ECO:0000250"
FT   DISULFID        318..338
FT                   /evidence="ECO:0000250"
FT   DISULFID        341..350
FT                   /evidence="ECO:0000250"
FT   DISULFID        343..368
FT                   /evidence="ECO:0000250"
FT   DISULFID        371..380
FT                   /evidence="ECO:0000250"
FT   DISULFID        383..401
FT                   /evidence="ECO:0000250"
FT   DISULFID        404..416
FT                   /evidence="ECO:0000250"
FT   DISULFID        406..423
FT                   /evidence="ECO:0000250"
FT   DISULFID        425..434
FT                   /evidence="ECO:0000250"
FT   DISULFID        437..451
FT                   /evidence="ECO:0000250"
FT   DISULFID        472..544
FT                   /evidence="ECO:0000250"
FT   DISULFID        491..601
FT                   /evidence="ECO:0000250"
FT   VARIANT         351
FT                   /note="R -> H (in a neuroblastoma sample;
FT                   dbSNP:rs531668666)"
FT                   /evidence="ECO:0000269|PubMed:9950216"
FT                   /id="VAR_014279"
FT   VARIANT         489
FT                   /note="K -> E (in a neuroblastoma sample)"
FT                   /evidence="ECO:0000269|PubMed:9950216"
FT                   /id="VAR_014280"
FT   VARIANT         518
FT                   /note="Missing (in MRMV4; changed localization; exclusively
FT                   detected in the cytoplasm; dbSNP:rs1567749982)"
FT                   /evidence="ECO:0000269|PubMed:28945198"
FT                   /id="VAR_082026"
FT   VARIANT         601
FT                   /note="C -> R (in MRMV4; changed localization; exclusively
FT                   detected in the cytoplasm; dbSNP:rs1567750186)"
FT                   /evidence="ECO:0000269|PubMed:28945198"
FT                   /id="VAR_082027"
FT   VARIANT         601
FT                   /note="C -> S (in MRMV4; changed localization; exclusively
FT                   detected in the cytoplasm; dbSNP:rs1567750187)"
FT                   /evidence="ECO:0000269|PubMed:28945198"
FT                   /id="VAR_082028"
FT   CONFLICT        299
FT                   /note="D -> T (in Ref. 1; AAD09221)"
FT                   /evidence="ECO:0000305"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   TURN            58..61
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          65..67
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          75..83
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          86..94
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          96..98
FT                   /evidence="ECO:0007829|PDB:7NE0"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   HELIX           106..109
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:7NE1"
FT   STRAND          132..153
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          156..166
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          172..179
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   HELIX           181..185
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:4URT"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:4URT"
FT   STRAND          212..215
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          217..221
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   TURN            222..225
FT                   /evidence="ECO:0007829|PDB:4URT"
FT   HELIX           232..234
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   HELIX           236..241
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          243..254
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          257..259
FT                   /evidence="ECO:0007829|PDB:4URT"
FT   HELIX           265..269
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          275..285
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          292..296
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          302..305
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          310..312
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   TURN            344..346
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          350..352
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   HELIX           354..359
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          366..368
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   TURN            372..374
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          375..380
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          387..389
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          391..393
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   HELIX           398..400
FT                   /evidence="ECO:0007829|PDB:7NE1"
FT   STRAND          401..403
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   TURN            408..410
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   TURN            418..420
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          425..428
FT                   /evidence="ECO:0007829|PDB:7NE0"
FT   TURN            431..434
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          447..449
FT                   /evidence="ECO:0007829|PDB:6FKQ"
FT   STRAND          451..453
FT                   /evidence="ECO:0007829|PDB:4URT"
SQ   SEQUENCE   604 AA;  67748 MW;  9827C09D0D783B27 CRC64;
     MMRAVWEALA ALAAVACLVG AVRGGPGLSM FAGQAAQPDP CSDENGHPRR CIPDFVNAAF
     GKDVRVSSTC GRPPARYCVV SERGEERLRS CHLCNASDPK KAHPPAFLTD LNNPHNLTCW
     QSENYLQFPH NVTLTLSLGK KFEVTYVSLQ FCSPRPESMA IYKSMDYGRT WVPFQFYSTQ
     CRKMYNRPHR APITKQNEQE AVCTDSHTDM RPLSGGLIAF STLDGRPSAH DFDNSPVLQD
     WVTATDIRVA FSRLHTFGDE NEDDSELARD SYFYAVSDLQ VGGRCKCNGH AARCVRDRDD
     SLVCDCRHNT AGPECDRCKP FHYDRPWQRA TAREANECVA CNCNLHARRC RFNMELYKLS
     GRKSGGVCLN CRHNTAGRHC HYCKEGYYRD MGKPITHRKA CKACDCHPVG AAGKTCNQTT
     GQCPCKDGVT GITCNRCAKG YQQSRSPIAP CIKIPVAPPT TAASSVEEPE DCDSYCKASK
     GKLKINMKKY CKKDYAVQIH ILKADKAGDW WKFTVNIISV YKQGTSRIRR GDQSLWIRSR
     DIACKCPKIK PLKKYLLLGN AEDSPDQSGI VADKSSLVIQ WRDTWARRLR KFQQREKKGK
     CKKA
//