LRRC4_HUMAN
ID LRRC4_HUMAN Reviewed; 653 AA.
AC Q9HBW1; A4D0Y9; Q14DU9; Q6ZMI8; Q96A85;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Leucine-rich repeat-containing protein 4;
DE AltName: Full=Brain tumor-associated protein BAG;
DE AltName: Full=Nasopharyngeal carcinoma-associated gene 14 protein;
DE AltName: Full=Netrin-G2 ligand;
DE Short=NGL-2;
DE Flags: Precursor;
GN Name=LRRC4; Synonyms=BAG; ORFNames=NAG14, UNQ554/PRO1111;
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.
RX PubMed=15967442; DOI=10.1016/j.febslet.2005.05.058;
RA Zhang Q., Wang J., Fan S., Wang L., Cao L., Tang K., Peng C., Li Z., Li W.,
RA Gan K., Liu Z., Li X., Shen S., Li G.;
RT "Expression and functional characterization of LRRC4, a novel brain-
RT specific member of the LRR superfamily.";
RL FEBS Lett. 579:3674-3682(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang J.;
RL Thesis (2000), Zhongshan Medical University / Guangzhou, China.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
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 [7]
RP STRUCTURE BY NMR OF 351-442.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the Ig-like domain of human leucine-rich repeat-
RT containing protein 4.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-444 IN COMPLEX WITH NTNG2, AND
RP DISULFIDE BONDS.
RX PubMed=21946559; DOI=10.1038/emboj.2011.346;
RA Seiradake E., Coles C.H., Perestenko P.V., Harlos K., McIlhinney R.A.,
RA Aricescu A.R., Jones E.Y.;
RT "Structural basis for cell surface patterning through NetrinG-NGL
RT interactions.";
RL EMBO J. 30:4479-4488(2011).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] ALA-579.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Synaptic adhesion protein. Regulates the formation of
CC exitatory synapses through the recruitment of pre-and-postsynaptic
CC proteins. Organize the lamina/pathway-specific differentiation of
CC dendrites. Plays an important role for auditory synaptic responses.
CC Involved in the suppression of glioma (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DLG4 (By similarity). Interacts (via LRR
CC repeats) with NTNG2. Forms a complex with DLG4 and with NMDA receptors.
CC {ECO:0000250, ECO:0000269|PubMed:21946559}.
CC -!- INTERACTION:
CC Q9HBW1; Q9Y2I2: NTNG1; NbExp=2; IntAct=EBI-7444327, EBI-7444396;
CC Q9HBW1; Q96CW9: NTNG2; NbExp=4; IntAct=EBI-7444327, EBI-750795;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC Postsynaptic cell membrane {ECO:0000250}. Note=LRRC4 and DLG4 are
CC interdependent for synaptic localization. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in brain.
CC {ECO:0000269|PubMed:15967442}.
CC -!- DOMAIN: The last 4 C-terminal residues bind to the first 2 PDZ domains
CC of DLG4. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; AF196976; AAG28019.2; -; mRNA.
DR EMBL; AJ297858; CAC82651.1; -; mRNA.
DR EMBL; AY358307; AAQ88674.1; -; mRNA.
DR EMBL; AK172751; BAD18737.1; -; mRNA.
DR EMBL; AK314047; BAG36756.1; -; mRNA.
DR EMBL; CH236947; EAL24316.1; -; Genomic_DNA.
DR EMBL; BC111561; AAI11562.1; -; mRNA.
DR EMBL; BC111745; AAI11746.1; -; mRNA.
DR CCDS; CCDS5799.1; -.
DR RefSeq; NP_071426.1; NM_022143.4.
DR RefSeq; XP_011514763.1; XM_011516461.2.
DR RefSeq; XP_016867994.1; XM_017012505.1.
DR PDB; 2DL9; NMR; -; A=353-442.
DR PDB; 3ZYI; X-ray; 2.60 A; A=1-444.
DR PDBsum; 2DL9; -.
DR PDBsum; 3ZYI; -.
DR AlphaFoldDB; Q9HBW1; -.
DR SMR; Q9HBW1; -.
DR BioGRID; 122061; 21.
DR IntAct; Q9HBW1; 13.
DR MINT; Q9HBW1; -.
DR STRING; 9606.ENSP00000249363; -.
DR GlyConnect; 1453; 1 N-Linked glycan (1 site).
DR GlyGen; Q9HBW1; 9 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q9HBW1; -.
DR PhosphoSitePlus; Q9HBW1; -.
DR BioMuta; LRRC4; -.
DR DMDM; 51701696; -.
DR MassIVE; Q9HBW1; -.
DR PaxDb; Q9HBW1; -.
DR PeptideAtlas; Q9HBW1; -.
DR PRIDE; Q9HBW1; -.
DR ProteomicsDB; 81601; -.
DR Antibodypedia; 55653; 109 antibodies from 25 providers.
DR DNASU; 64101; -.
DR Ensembl; ENST00000249363.4; ENSP00000249363.3; ENSG00000128594.8.
DR GeneID; 64101; -.
DR KEGG; hsa:64101; -.
DR MANE-Select; ENST00000249363.4; ENSP00000249363.3; NM_022143.5; NP_071426.1.
DR UCSC; uc003vmk.4; human.
DR CTD; 64101; -.
DR DisGeNET; 64101; -.
DR GeneCards; LRRC4; -.
DR HGNC; HGNC:15586; LRRC4.
DR HPA; ENSG00000128594; Tissue enhanced (brain).
DR MIM; 610486; gene.
DR neXtProt; NX_Q9HBW1; -.
DR OpenTargets; ENSG00000128594; -.
DR PharmGKB; PA30463; -.
DR VEuPathDB; HostDB:ENSG00000128594; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000159260; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; Q9HBW1; -.
DR OMA; QVWILCV; -.
DR OrthoDB; 282791at2759; -.
DR PhylomeDB; Q9HBW1; -.
DR TreeFam; TF324303; -.
DR PathwayCommons; Q9HBW1; -.
DR SignaLink; Q9HBW1; -.
DR SIGNOR; Q9HBW1; -.
DR BioGRID-ORCS; 64101; 12 hits in 1064 CRISPR screens.
DR EvolutionaryTrace; Q9HBW1; -.
DR GeneWiki; LRRC4; -.
DR GenomeRNAi; 64101; -.
DR Pharos; Q9HBW1; Tbio.
DR PRO; PR:Q9HBW1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9HBW1; protein.
DR Bgee; ENSG00000128594; Expressed in ventricular zone and 149 other tissues.
DR ExpressionAtlas; Q9HBW1; baseline and differential.
DR Genevisible; Q9HBW1; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:1904861; P:excitatory synapse assembly; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; IBA:GO_Central.
DR GO; GO:0099560; P:synaptic membrane adhesion; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR026882; Lrrc4.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR24369:SF9; PTHR24369:SF9; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..653
FT /note="Leucine-rich repeat-containing protein 4"
FT /id="PRO_0000014833"
FT TOPO_DOM 39..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..75
FT /note="LRRNT"
FT REPEAT 76..97
FT /note="LRR 1"
FT REPEAT 100..121
FT /note="LRR 2"
FT REPEAT 124..145
FT /note="LRR 3"
FT REPEAT 148..169
FT /note="LRR 4"
FT REPEAT 172..194
FT /note="LRR 5"
FT REPEAT 197..218
FT /note="LRR 6"
FT REPEAT 219..240
FT /note="LRR 7"
FT REPEAT 243..264
FT /note="LRR 8"
FT REPEAT 267..288
FT /note="LRR 9"
FT DOMAIN 300..352
FT /note="LRRCT"
FT DOMAIN 353..442
FT /note="Ig-like"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 450
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..52
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21946559"
FT DISULFID 50..61
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21946559"
FT DISULFID 304..329
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21946559"
FT DISULFID 306..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21946559"
FT DISULFID 374..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:21946559"
FT VARIANT 579
FT /note="T -> A (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035519"
FT CONFLICT 4
FT /note="L -> S (in Ref. 4; BAD18737)"
FT /evidence="ECO:0000305"
FT CONFLICT 253..257
FT /note="QVSLI -> H (in Ref. 2; CAC82651)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="N -> D (in Ref. 4; BAD18737)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="L -> F (in Ref. 4; BAD18737)"
FT /evidence="ECO:0000305"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3ZYI"
FT TURN 92..97
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:3ZYI"
FT TURN 116..121
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3ZYI"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3ZYI"
FT TURN 164..169
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3ZYI"
FT TURN 189..194
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3ZYI"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:3ZYI"
FT TURN 259..264
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:3ZYI"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:3ZYI"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:3ZYI"
FT TURN 333..337
FT /evidence="ECO:0007829|PDB:3ZYI"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:2DL9"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:2DL9"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:3ZYI"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:2DL9"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:2DL9"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:2DL9"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:2DL9"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:2DL9"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:2DL9"
FT STRAND 420..427
FT /evidence="ECO:0007829|PDB:3ZYI"
FT STRAND 432..440
FT /evidence="ECO:0007829|PDB:3ZYI"
SQ SEQUENCE 653 AA; 72717 MW; 38159C81F6850E37 CRC64;
MKLLWQVTVH HHTWNAILLP FVYLTAQVWI LCAAIAAAAS AGPQNCPSVC SCSNQFSKVV
CTRRGLSEVP QGIPSNTRYL NLMENNIQMI QADTFRHLHH LEVLQLGRNS IRQIEVGAFN
GLASLNTLEL FDNWLTVIPS GAFEYLSKLR ELWLRNNPIE SIPSYAFNRV PSLMRLDLGE
LKKLEYISEG AFEGLFNLKY LNLGMCNIKD MPNLTPLVGL EELEMSGNHF PEIRPGSFHG
LSSLKKLWVM NSQVSLIERN AFDGLASLVE LNLAHNNLSS LPHDLFTPLR YLVELHLHHN
PWNCDCDILW LAWWLREYIP TNSTCCGRCH APMHMRGRYL VEVDQASFQC SAPFIMDAPR
DLNISEGRMA ELKCRTPPMS SVKWLLPNGT VLSHASRHPR ISVLNDGTLN FSHVLLSDTG
VYTCMVTNVA GNSNASAYLN VSTAELNTSN YSFFTTVTVE TTEISPEDTT RKYKPVPTTS
TGYQPAYTTS TTVLIQTTRV PKQVAVPATD TTDKMQTSLD EVMKTTKIII GCFVAVTLLA
AAMLIVFYKL RKRHQQRSTV TAARTVEIIQ VDEDIPAATS AAATAAPSGV SGEGAVVLPT
IHDHINYNTY KPAHGAHWTE NSLGNSLHPT VTTISEPYII QTHTKDKVQE TQI
