NELL1_HUMAN
ID NELL1_HUMAN Reviewed; 810 AA.
AC Q92832; B2CKC1; Q4VB90; Q4VB91; Q6NSY8; Q9Y472;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Protein kinase C-binding protein NELL1;
DE AltName: Full=NEL-like protein 1;
DE AltName: Full=Nel-related protein 1;
DE Flags: Precursor;
GN Name=NELL1; Synonyms=NRP1;
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] (ISOFORM 1), AND VARIANT GLN-82.
RC TISSUE=Brain;
RX PubMed=8975702; DOI=10.1006/geno.1996.0628;
RA Watanabe T.K., Katagiri T., Suzuki M., Shimizu F., Fujiwara T.,
RA Kanemoto N., Nakamura Y., Hirai Y., Maekawa H., Takahashi E.;
RT "Cloning and characterization of two novel human cDNAs (NELL1 and NELL2)
RT encoding proteins with six EGF-like repeats.";
RL Genomics 38:273-276(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-82.
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-82.
RG NIEHS SNPs program;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP GLN-82.
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 NUCLEOTIDE SEQUENCE [MRNA] OF 383-810 (ISOFORMS 1/2).
RA Ting K., Vastardis H., Mulliken J.B., Bertolami C., Wen Z., Young M.,
RA Tieu A., Kwong E.;
RT "Nel homolog gene expression in craniofacial anomalies.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION IN OSTEOBLAST DIFFERENTIATION, INTERACTION WITH ATRAID, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21723284; DOI=10.1016/j.febslet.2011.06.024;
RA Zou X., Shen J., Chen F., Ting K., Zheng Z., Pang S., Zara J.N.,
RA Adams J.S., Soo C., Zhang X.;
RT "NELL-1 binds to APR3 affecting human osteoblast proliferation and
RT differentiation.";
RL FEBS Lett. 585:2410-2418(2011).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-553.
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: Plays a role in the control of cell growth and
CC differentiation. Promotes osteoblast cell differentiation and terminal
CC mineralization. {ECO:0000269|PubMed:21723284}.
CC -!- SUBUNIT: Homotrimer. Binds to PKC beta-1 (By similarity). Interacts
CC with ATRAID; the interaction promotes osteoblast cell differentiation
CC and mineralization. {ECO:0000250, ECO:0000269|PubMed:21723284}.
CC -!- INTERACTION:
CC Q92832; Q6UW56: ATRAID; NbExp=4; IntAct=EBI-947754, EBI-723802;
CC Q92832; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-947754, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21723284}. Nucleus
CC envelope {ECO:0000269|PubMed:21723284}. Secreted {ECO:0000250}.
CC Note=Colocalizes with ATRAID on the nuclear envelope and the
CC perinuclear region.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q92832-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92832-2; Sequence=VSP_039954;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB06946.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D83017; BAA11680.1; -; mRNA.
DR EMBL; AK313445; BAG36234.1; -; mRNA.
DR EMBL; EU518937; ACB21040.1; -; Genomic_DNA.
DR EMBL; AC010811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC067794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68328.1; -; Genomic_DNA.
DR EMBL; BC069674; AAH69674.1; -; mRNA.
DR EMBL; BC096100; AAH96100.1; -; mRNA.
DR EMBL; BC096101; AAH96101.1; -; mRNA.
DR EMBL; BC096102; AAH96102.1; -; mRNA.
DR EMBL; U57523; AAB06946.1; ALT_FRAME; mRNA.
DR CCDS; CCDS44555.1; -. [Q92832-2]
DR CCDS; CCDS7855.1; -. [Q92832-1]
DR RefSeq; NP_001275642.1; NM_001288713.1.
DR RefSeq; NP_001275643.1; NM_001288714.1.
DR RefSeq; NP_006148.2; NM_006157.4. [Q92832-1]
DR RefSeq; NP_963845.1; NM_201551.2. [Q92832-2]
DR PDB; 6POL; X-ray; 1.80 A; B/D/F=390-517.
DR PDBsum; 6POL; -.
DR AlphaFoldDB; Q92832; -.
DR SMR; Q92832; -.
DR BioGRID; 110820; 35.
DR IntAct; Q92832; 43.
DR MINT; Q92832; -.
DR STRING; 9606.ENSP00000298925; -.
DR GlyGen; Q92832; 12 sites.
DR iPTMnet; Q92832; -.
DR PhosphoSitePlus; Q92832; -.
DR SwissPalm; Q92832; -.
DR BioMuta; NELL1; -.
DR DMDM; 311033486; -.
DR MassIVE; Q92832; -.
DR PaxDb; Q92832; -.
DR PeptideAtlas; Q92832; -.
DR PRIDE; Q92832; -.
DR ProteomicsDB; 75509; -. [Q92832-1]
DR ProteomicsDB; 75510; -. [Q92832-2]
DR Antibodypedia; 25294; 160 antibodies from 25 providers.
DR DNASU; 4745; -.
DR Ensembl; ENST00000357134.10; ENSP00000349654.5; ENSG00000165973.19. [Q92832-1]
DR Ensembl; ENST00000532434.5; ENSP00000437170.1; ENSG00000165973.19. [Q92832-2]
DR GeneID; 4745; -.
DR KEGG; hsa:4745; -.
DR MANE-Select; ENST00000357134.10; ENSP00000349654.5; NM_006157.5; NP_006148.2.
DR UCSC; uc001mqe.5; human. [Q92832-1]
DR CTD; 4745; -.
DR DisGeNET; 4745; -.
DR GeneCards; NELL1; -.
DR HGNC; HGNC:7750; NELL1.
DR HPA; ENSG00000165973; Tissue enhanced (brain, kidney).
DR MIM; 602319; gene.
DR neXtProt; NX_Q92832; -.
DR OpenTargets; ENSG00000165973; -.
DR PharmGKB; PA31552; -.
DR VEuPathDB; HostDB:ENSG00000165973; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00810000125439; -.
DR HOGENOM; CLU_006887_0_0_1; -.
DR InParanoid; Q92832; -.
DR OMA; XGGVLVK; -.
DR OrthoDB; 767046at2759; -.
DR PhylomeDB; Q92832; -.
DR TreeFam; TF323325; -.
DR PathwayCommons; Q92832; -.
DR SignaLink; Q92832; -.
DR BioGRID-ORCS; 4745; 15 hits in 1059 CRISPR screens.
DR ChiTaRS; NELL1; human.
DR GeneWiki; NELL1; -.
DR GenomeRNAi; 4745; -.
DR Pharos; Q92832; Tbio.
DR PRO; PR:Q92832; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q92832; protein.
DR Bgee; ENSG00000165973; Expressed in endothelial cell and 138 other tissues.
DR ExpressionAtlas; Q92832; baseline and differential.
DR Genevisible; Q92832; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0005080; F:protein kinase C binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IDA:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF00093; VWC; 2.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 5.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00214; VWC; 4.
DR SMART; SM00215; VWC_out; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS01208; VWFC_1; 2.
DR PROSITE; PS50184; VWFC_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cytoplasm; Differentiation;
KW Disulfide bond; EGF-like domain; Glycoprotein; Nucleus; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..810
FT /note="Protein kinase C-binding protein NELL1"
FT /id="PRO_0000007664"
FT DOMAIN 64..227
FT /note="Laminin G-like"
FT DOMAIN 271..332
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 434..475
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 476..516
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 517..547
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 549..587
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 596..631
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 692..750
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 511
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 732
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 395..407
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 401..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 418..432
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 438..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 445..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 462..474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 480..493
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 487..502
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 504..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 519..529
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 523..535
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 537..546
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 553..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 560..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 577..594
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 600..613
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 607..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 624..630
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 549..595
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039954"
FT VARIANT 82
FT /note="R -> Q (in dbSNP:rs8176785)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8975702,
FT ECO:0000269|Ref.3"
FT /id="VAR_047828"
FT VARIANT 211
FT /note="F -> V (in dbSNP:rs35809043)"
FT /id="VAR_047829"
FT VARIANT 287
FT /note="V -> I (in dbSNP:rs11820003)"
FT /id="VAR_047830"
FT VARIANT 354
FT /note="R -> W (in dbSNP:rs8176786)"
FT /id="VAR_020167"
FT VARIANT 553
FT /note="C -> F (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035834"
FT CONFLICT 383
FT /note="N -> D (in Ref. 7; AAB06946)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="Y -> H (in Ref. 7; AAB06946)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="S -> C (in Ref. 7; AAB06946)"
FT /evidence="ECO:0000305"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 411..418
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 457..462
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:6POL"
FT TURN 479..483
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 491..495
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 497..504
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:6POL"
FT STRAND 512..517
FT /evidence="ECO:0007829|PDB:6POL"
SQ SEQUENCE 810 AA; 89635 MW; 15E09F9954DA8629 CRC64;
MPMDLILVVW FCVCTARTVV GFGMDPDLQM DIVTELDLVN TTLGVAQVSG MHNASKAFLF
QDIEREIHAA PHVSEKLIQL FRNKSEFTIL ATVQQKPSTS GVILSIRELE HSYFELESSG
LRDEIRYHYI HNGKPRTEAL PYRMADGQWH KVALSVSASH LLLHVDCNRI YERVIDPPDT
NLPPGINLWL GQRNQKHGLF KGIIQDGKII FMPNGYITQC PNLNHTCPTC SDFLSLVQGI
MDLQELLAKM TAKLNYAETR LSQLENCHCE KTCQVSGLLY RDQDSWVDGD HCRNCTCKSG
AVECRRMSCP PLNCSPDSLP VHIAGQCCKV CRPKCIYGGK VLAEGQRILT KSCRECRGGV
LVKITEMCPP LNCSEKDHIL PENQCCRVCR GHNFCAEGPK CGENSECKNW NTKATCECKS
GYISVQGDSA YCEDIDECAA KMHYCHANTV CVNLPGLYRC DCVPGYIRVD DFSCTEHDEC
GSGQHNCDEN AICTNTVQGH SCTCKPGYVG NGTICRAFCE EGCRYGGTCV APNKCVCPSG
FTGSHCEKDI DECSEGIIEC HNHSRCVNLP GWYHCECRSG FHDDGTYSLS GESCIDIDEC
ALRTHTCWND SACINLAGGF DCLCPSGPSC SGDCPHEGGL KHNGQVWTLK EDRCSVCSCK
DGKIFCRRTA CDCQNPSADL FCCPECDTRV TSQCLDQNGH KLYRSGDNWT HSCQQCRCLE
GEVDCWPLTC PNLSCEYTAI LEGECCPRCV SDPCLADNIT YDIRKTCLDS YGVSRLSGSV
WTMAGSPCTT CKCKNGRVCC SVDFECLQNN
