NET1_HUMAN
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 03-AUG-2022, entry version 179.
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.
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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 SASBDB; O95631; -.
DR SMR; O95631; -.
DR BioGRID; 114816; 17.
DR DIP; DIP-46273N; -.
DR IntAct; O95631; 9.
DR STRING; 9606.ENSP00000173229; -.
DR GlyConnect; 1542; 1 N-Linked glycan (1 site).
DR GlyGen; O95631; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; O95631; -.
DR PhosphoSitePlus; O95631; -.
DR BioMuta; NTN1; -.
DR jPOST; O95631; -.
DR MassIVE; O95631; -.
DR MaxQB; O95631; -.
DR PaxDb; O95631; -.
DR PeptideAtlas; O95631; -.
DR PRIDE; O95631; -.
DR ProteomicsDB; 50967; -.
DR Antibodypedia; 24762; 359 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 CTD; 9423; -.
DR DisGeNET; 9423; -.
DR GeneCards; NTN1; -.
DR GeneReviews; NTN1; -.
DR HGNC; HGNC:8029; NTN1.
DR HPA; ENSG00000065320; Tissue enhanced (brain, heart muscle).
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; YFSQFSM; -.
DR OrthoDB; 858946at2759; -.
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; 13 hits in 1074 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 146 other tissues.
DR ExpressionAtlas; O95631; baseline and differential.
DR Genevisible; O95631; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
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:0009887; P:animal organ morphogenesis; 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:0016358; P:dendrite development; IBA:GO_Central.
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:0008045; P:motor neuron axon guidance; IBA:GO_Central.
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:0006930; P:substrate-dependent cell migration, cell extension; ISS:UniProtKB.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 3.
DR Gene3D; 2.40.50.120; -; 1.
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 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; SSF49785; SSF49785; 1.
DR SUPFAM; SSF50242; SSF50242; 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.
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
