LRC4C_HUMAN
ID LRC4C_HUMAN Reviewed; 640 AA.
AC Q9HCJ2; A8K0T1; Q7L0N3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Leucine-rich repeat-containing protein 4C;
DE AltName: Full=Netrin-G1 ligand;
DE Short=NGL-1;
DE Flags: Precursor;
GN Name=LRRC4C; Synonyms=KIAA1580, NGL1; ORFNames=UNQ292/PRO331;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
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 [6]
RP FUNCTION, INTERACTION WITH NTNG1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=14595443; DOI=10.1038/nn1148;
RA Lin J.C., Ho W.-H., Gurney A.L., Rosenthal A.;
RT "The netrin-G1 ligand NGL-1 promotes the outgrowth of thalamocortical
RT axons.";
RL Nat. Neurosci. 6:1270-1276(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 44-444 IN COMPLEX WITH NTNG1, AND
RP SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: May promote neurite outgrowth of developing thalamic neurons.
CC {ECO:0000269|PubMed:14595443}.
CC -!- SUBUNIT: Interacts with NTNG1 and WHRN. {ECO:0000269|PubMed:14595443,
CC ECO:0000269|PubMed:21946559}.
CC -!- INTERACTION:
CC Q9HCJ2; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-3925442, EBI-11522760;
CC Q9HCJ2; O95393: BMP10; NbExp=3; IntAct=EBI-3925442, EBI-3922513;
CC Q9HCJ2; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-3925442, EBI-12244618;
CC Q9HCJ2; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-3925442, EBI-12256978;
CC Q9HCJ2; Q8NC01: CLEC1A; NbExp=3; IntAct=EBI-3925442, EBI-11996768;
CC Q9HCJ2; Q6UXB4: CLEC4G; NbExp=3; IntAct=EBI-3925442, EBI-2114729;
CC Q9HCJ2; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-3925442, EBI-11522780;
CC Q9HCJ2; Q9UPQ8: DOLK; NbExp=4; IntAct=EBI-3925442, EBI-8645574;
CC Q9HCJ2; Q8N682: DRAM1; NbExp=3; IntAct=EBI-3925442, EBI-10305400;
CC Q9HCJ2; P54852: EMP3; NbExp=3; IntAct=EBI-3925442, EBI-3907816;
CC Q9HCJ2; P29033: GJB2; NbExp=3; IntAct=EBI-3925442, EBI-3905204;
CC Q9HCJ2; O95214: LEPROTL1; NbExp=3; IntAct=EBI-3925442, EBI-750776;
CC Q9HCJ2; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-3925442, EBI-2820517;
CC Q9HCJ2; P30301: MIP; NbExp=3; IntAct=EBI-3925442, EBI-8449636;
CC Q9HCJ2; Q9Y2I2: NTNG1; NbExp=4; IntAct=EBI-3925442, EBI-7444396;
CC Q9HCJ2; Q96CW9: NTNG2; NbExp=2; IntAct=EBI-3925442, EBI-750795;
CC Q9HCJ2; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-3925442, EBI-12092917;
CC Q9HCJ2; Q04941: PLP2; NbExp=3; IntAct=EBI-3925442, EBI-608347;
CC Q9HCJ2; A2A2V5: SERTM1; NbExp=3; IntAct=EBI-3925442, EBI-17284533;
CC Q9HCJ2; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-3925442, EBI-12188413;
CC Q9HCJ2; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-3925442, EBI-10244848;
CC Q9HCJ2; Q13190: STX5; NbExp=3; IntAct=EBI-3925442, EBI-714206;
CC Q9HCJ2; Q9GZX9: TWSG1; NbExp=3; IntAct=EBI-3925442, EBI-10304067;
CC Q9HCJ2; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-3925442, EBI-12190699;
CC Q9HCJ2; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-3925442, EBI-751210;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:14595443, ECO:0000269|PubMed:21946559}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:14595443,
CC ECO:0000269|PubMed:21946559}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the cerebral cortex, including
CC frontal, parietal and occipital lobes. Putamen, amygdala, hippocampus
CC and medulla oblongata show moderate expression. Caudate nucleus and
CC thalamus express small amounts, whereas other brain regions show very
CC weak or no expression. {ECO:0000269|PubMed:14595443}.
CC -!- DOMAIN: The LRR region is both necessary and sufficient for the
CC interaction with NTNG1.
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DR EMBL; AB046800; BAB13406.1; -; mRNA.
DR EMBL; AY358293; AAQ88660.1; -; mRNA.
DR EMBL; AK289646; BAF82335.1; -; mRNA.
DR EMBL; CH471064; EAW68107.1; -; Genomic_DNA.
DR EMBL; BC041374; AAH41374.3; -; mRNA.
DR CCDS; CCDS31464.1; -.
DR RefSeq; NP_001245348.1; NM_001258419.1.
DR RefSeq; NP_065980.1; NM_020929.2.
DR RefSeq; XP_011518540.1; XM_011520238.2.
DR RefSeq; XP_011518541.1; XM_011520239.2.
DR RefSeq; XP_011518542.1; XM_011520240.2.
DR RefSeq; XP_011518543.1; XM_011520241.2.
DR RefSeq; XP_011518544.1; XM_011520242.2.
DR RefSeq; XP_011518545.1; XM_011520243.2.
DR RefSeq; XP_011518546.1; XM_011520244.2.
DR RefSeq; XP_016873559.1; XM_017018070.1.
DR RefSeq; XP_016873560.1; XM_017018071.1.
DR RefSeq; XP_016873561.1; XM_017018072.1.
DR RefSeq; XP_016873562.1; XM_017018073.1.
DR RefSeq; XP_016873563.1; XM_017018074.1.
DR RefSeq; XP_016873564.1; XM_017018075.1.
DR RefSeq; XP_016873565.1; XM_017018076.1.
DR RefSeq; XP_016873566.1; XM_017018077.1.
DR RefSeq; XP_016873567.1; XM_017018078.1.
DR RefSeq; XP_016873568.1; XM_017018079.1.
DR PDB; 3ZYJ; X-ray; 3.25 A; A/C=44-444.
DR PDBsum; 3ZYJ; -.
DR AlphaFoldDB; Q9HCJ2; -.
DR SMR; Q9HCJ2; -.
DR BioGRID; 121715; 59.
DR IntAct; Q9HCJ2; 49.
DR MINT; Q9HCJ2; -.
DR STRING; 9606.ENSP00000278198; -.
DR iPTMnet; Q9HCJ2; -.
DR PhosphoSitePlus; Q9HCJ2; -.
DR BioMuta; LRRC4C; -.
DR DMDM; 57012973; -.
DR jPOST; Q9HCJ2; -.
DR MassIVE; Q9HCJ2; -.
DR PaxDb; Q9HCJ2; -.
DR PeptideAtlas; Q9HCJ2; -.
DR PRIDE; Q9HCJ2; -.
DR ProteomicsDB; 81737; -.
DR Antibodypedia; 26031; 209 antibodies from 26 providers.
DR DNASU; 57689; -.
DR Ensembl; ENST00000278198.2; ENSP00000278198.1; ENSG00000148948.8.
DR Ensembl; ENST00000527150.5; ENSP00000436976.1; ENSG00000148948.8.
DR Ensembl; ENST00000528697.6; ENSP00000437132.1; ENSG00000148948.8.
DR Ensembl; ENST00000530763.5; ENSP00000434761.1; ENSG00000148948.8.
DR Ensembl; ENST00000619527.4; ENSP00000480903.1; ENSG00000148948.8.
DR GeneID; 57689; -.
DR KEGG; hsa:57689; -.
DR MANE-Select; ENST00000528697.6; ENSP00000437132.1; NM_001258419.2; NP_001245348.1.
DR UCSC; uc031pzt.2; human.
DR CTD; 57689; -.
DR DisGeNET; 57689; -.
DR GeneCards; LRRC4C; -.
DR HGNC; HGNC:29317; LRRC4C.
DR HPA; ENSG00000148948; Group enriched (brain, retina).
DR MIM; 608817; gene.
DR neXtProt; NX_Q9HCJ2; -.
DR OpenTargets; ENSG00000148948; -.
DR PharmGKB; PA142671534; -.
DR VEuPathDB; HostDB:ENSG00000148948; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000157405; -.
DR HOGENOM; CLU_000288_18_24_1; -.
DR InParanoid; Q9HCJ2; -.
DR OMA; TYKTAYN; -.
DR OrthoDB; 282791at2759; -.
DR PhylomeDB; Q9HCJ2; -.
DR TreeFam; TF324303; -.
DR PathwayCommons; Q9HCJ2; -.
DR SignaLink; Q9HCJ2; -.
DR SIGNOR; Q9HCJ2; -.
DR BioGRID-ORCS; 57689; 11 hits in 1065 CRISPR screens.
DR ChiTaRS; LRRC4C; human.
DR GenomeRNAi; 57689; -.
DR Pharos; Q9HCJ2; Tbio.
DR PRO; PR:Q9HCJ2; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9HCJ2; protein.
DR Bgee; ENSG00000148948; Expressed in middle temporal gyrus and 153 other tissues.
DR ExpressionAtlas; Q9HCJ2; baseline and differential.
DR Genevisible; Q9HCJ2; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:SynGO-UCL.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IGI:SynGO-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0050770; P:regulation of axonogenesis; IDA:UniProtKB.
DR GO; GO:0099560; P:synaptic membrane adhesion; IGI:SynGO-UCL.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
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; IPR013106; Ig_V-set.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR026878; LRRC4C.
DR InterPro; IPR000372; LRRNT.
DR PANTHER; PTHR24369:SF8; PTHR24369:SF8; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13306; LRR_5; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00406; IGv; 1.
DR SMART; SM00369; LRR_TYP; 8.
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; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..640
FT /note="Leucine-rich repeat-containing protein 4C"
FT /id="PRO_0000015108"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 45..76
FT /note="LRRNT"
FT REPEAT 77..98
FT /note="LRR 1"
FT REPEAT 101..122
FT /note="LRR 2"
FT REPEAT 125..146
FT /note="LRR 3"
FT REPEAT 149..170
FT /note="LRR 4"
FT REPEAT 173..195
FT /note="LRR 5"
FT REPEAT 198..219
FT /note="LRR 6"
FT REPEAT 220..241
FT /note="LRR 7"
FT REPEAT 244..265
FT /note="LRR 8"
FT REPEAT 268..289
FT /note="LRR 9"
FT DOMAIN 301..353
FT /note="LRRCT"
FT DOMAIN 354..442
FT /note="Ig-like C2-type"
FT REGION 463..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C031"
FT DISULFID 375..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT TURN 165..170
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT TURN 190..195
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT TURN 236..241
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT TURN 334..338
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:3ZYJ"
FT STRAND 434..444
FT /evidence="ECO:0007829|PDB:3ZYJ"
SQ SEQUENCE 640 AA; 71950 MW; 6058974872636838 CRC64;
MLNKMTLHPQ QIMIGPRFNR ALFDPLLVVL LALQLLVVAG LVRAQTCPSV CSCSNQFSKV
ICVRKNLREV PDGISTNTRL LNLHENQIQI IKVNSFKHLR HLEILQLSRN HIRTIEIGAF
NGLANLNTLE LFDNRLTTIP NGAFVYLSKL KELWLRNNPI ESIPSYAFNR IPSLRRLDLG
ELKRLSYISE GAFEGLSNLR YLNLAMCNLR EIPNLTPLIK LDELDLSGNH LSAIRPGSFQ
GLMHLQKLWM IQSQIQVIER NAFDNLQSLV EINLAHNNLT LLPHDLFTPL HHLERIHLHH
NPWNCNCDIL WLSWWIKDMA PSNTACCARC NTPPNLKGRY IGELDQNYFT CYAPVIVEPP
ADLNVTEGMA AELKCRASTS LTSVSWITPN GTVMTHGAYK VRIAVLSDGT LNFTNVTVQD
TGMYTCMVSN SVGNTTASAT LNVTAATTTP FSYFSTVTVE TMEPSQDEAR TTDNNVGPTP
VVDWETTNVT TSLTPQSTRS TEKTFTIPVT DINSGIPGID EVMKTTKIII GCFVAITLMA
AVMLVIFYKM RKQHHRQNHH APTRTVEIIN VDDEITGDTP MESHLPMPAI EHEHLNHYNS
YKSPFNHTTT VNTINSIHSS VHEPLLIRMN SKDNVQETQI
