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NLE1_HUMAN
ID   NLE1_HUMAN              Reviewed;         485 AA.
AC   Q9NVX2; O60868; Q59GJ8; Q9BU54;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 4.
DT   03-AUG-2022, entry version 184.
DE   RecName: Full=Notchless protein homolog 1;
GN   Name=NLE1; ORFNames=HUSSY-07;
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] (ISOFORM 1), AND VARIANTS ALA-6 AND
RP   LYS-169.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-6 AND
RP   LYS-169.
RC   TISSUE=Lung, and Placenta;
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   [5]
RP   PROTEIN SEQUENCE OF 2-12 AND 87-99, CLEAVAGE OF INITIATOR METHIONINE,
RP   ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP   SPECTROMETRY, AND VARIANT ALA-6.
RC   TISSUE=Cervix carcinoma;
RA   Bienvenut W.V.;
RL   Submitted (AUG-2005) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 400-485.
RC   TISSUE=Brain;
RX   PubMed=11124703;
RX   DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h;
RA   Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N.,
RA   Zimbello R., Lanfranchi G., Valle G.;
RT   "Characterization of 16 novel human genes showing high similarity to yeast
RT   sequences.";
RL   Yeast 18:69-80(2001).
RN   [7]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA   Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA   Greco A., Hochstrasser D.F., Diaz J.-J.;
RT   "Functional proteomic analysis of human nucleolus.";
RL   Mol. Biol. Cell 13:4100-4109(2002).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, VARIANT [LARGE SCALE ANALYSIS]
RP   ALA-6, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, VARIANT [LARGE SCALE ANALYSIS]
RP   ALA-6, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, VARIANT [LARGE SCALE ANALYSIS]
RP   ALA-6, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [13]
RP   INTERACTION WITH MDN1.
RX   PubMed=26601951; DOI=10.1074/jbc.m115.693259;
RA   Romes E.M., Sobhany M., Stanley R.E.;
RT   "The crystal structure of the ubiquitin-like domain of ribosome assembly
RT   factor Ytm1 and characterization of its interaction with the AAA-ATPase
RT   Midasin.";
RL   J. Biol. Chem. 291:882-893(2016).
RN   [14]
RP   VARIANT [LARGE SCALE ANALYSIS] LYS-319.
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 regulating Notch activity. Plays a role in
CC       regulating the expression of CDKN1A and several members of the Wnt
CC       pathway, probably via its effects on Notch activity. Required during
CC       embryogenesis for inner mass cell survival (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Associates with the pre-60S ribosomal particle. Interacts (via
CC       WD repeats) with uL18 (By similarity). Interacts (via UBL domain) with
CC       MDN1 (via VWFA/MIDAS domain) (PubMed:26601951).
CC       {ECO:0000250|UniProtKB:P25382, ECO:0000269|PubMed:26601951}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC       ECO:0000269|Ref.5}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NVX2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NVX2-2; Sequence=VSP_040555;
CC   -!- SIMILARITY: Belongs to the NLE1/RSA4 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD92348.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK001320; BAA91621.1; -; mRNA.
DR   EMBL; AB209111; BAD92348.1; ALT_INIT; mRNA.
DR   EMBL; AC022916; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002884; AAH02884.2; -; mRNA.
DR   EMBL; BC012075; AAH12075.1; -; mRNA.
DR   EMBL; AJ005257; CAA06444.1; -; mRNA.
DR   CCDS; CCDS11291.1; -. [Q9NVX2-1]
DR   CCDS; CCDS45647.1; -. [Q9NVX2-2]
DR   RefSeq; NP_001014445.1; NM_001014445.2. [Q9NVX2-2]
DR   RefSeq; NP_060566.2; NM_018096.4. [Q9NVX2-1]
DR   RefSeq; XP_016880266.1; XM_017024777.1. [Q9NVX2-2]
DR   PDB; 6WAJ; X-ray; 1.90 A; A=1-97.
DR   PDBsum; 6WAJ; -.
DR   AlphaFoldDB; Q9NVX2; -.
DR   SMR; Q9NVX2; -.
DR   BioGRID; 119980; 103.
DR   IntAct; Q9NVX2; 22.
DR   MINT; Q9NVX2; -.
DR   STRING; 9606.ENSP00000413572; -.
DR   iPTMnet; Q9NVX2; -.
DR   PhosphoSitePlus; Q9NVX2; -.
DR   BioMuta; NLE1; -.
DR   DMDM; 296439488; -.
DR   SWISS-2DPAGE; Q9NVX2; -.
DR   EPD; Q9NVX2; -.
DR   jPOST; Q9NVX2; -.
DR   MassIVE; Q9NVX2; -.
DR   MaxQB; Q9NVX2; -.
DR   PaxDb; Q9NVX2; -.
DR   PeptideAtlas; Q9NVX2; -.
DR   PRIDE; Q9NVX2; -.
DR   ProteomicsDB; 82876; -. [Q9NVX2-1]
DR   ProteomicsDB; 82877; -. [Q9NVX2-2]
DR   Antibodypedia; 15565; 246 antibodies from 31 providers.
DR   DNASU; 54475; -.
DR   Ensembl; ENST00000442241.9; ENSP00000413572.3; ENSG00000073536.18. [Q9NVX2-1]
DR   Ensembl; ENST00000586869.5; ENSP00000466588.1; ENSG00000073536.18. [Q9NVX2-2]
DR   GeneID; 54475; -.
DR   KEGG; hsa:54475; -.
DR   MANE-Select; ENST00000442241.9; ENSP00000413572.3; NM_018096.5; NP_060566.2.
DR   UCSC; uc002hiy.3; human. [Q9NVX2-1]
DR   CTD; 54475; -.
DR   DisGeNET; 54475; -.
DR   GeneCards; NLE1; -.
DR   HGNC; HGNC:19889; NLE1.
DR   HPA; ENSG00000073536; Low tissue specificity.
DR   neXtProt; NX_Q9NVX2; -.
DR   OpenTargets; ENSG00000073536; -.
DR   PharmGKB; PA142671263; -.
DR   VEuPathDB; HostDB:ENSG00000073536; -.
DR   eggNOG; KOG0271; Eukaryota.
DR   GeneTree; ENSGT00940000157881; -.
DR   HOGENOM; CLU_000288_57_16_1; -.
DR   InParanoid; Q9NVX2; -.
DR   OMA; HINCLAW; -.
DR   OrthoDB; 723347at2759; -.
DR   PhylomeDB; Q9NVX2; -.
DR   TreeFam; TF300668; -.
DR   PathwayCommons; Q9NVX2; -.
DR   SignaLink; Q9NVX2; -.
DR   BioGRID-ORCS; 54475; 745 hits in 1083 CRISPR screens.
DR   ChiTaRS; NLE1; human.
DR   GeneWiki; NLE1; -.
DR   GenomeRNAi; 54475; -.
DR   Pharos; Q9NVX2; Tbio.
DR   PRO; PR:Q9NVX2; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9NVX2; protein.
DR   Bgee; ENSG00000073536; Expressed in body of pancreas and 97 other tissues.
DR   ExpressionAtlas; Q9NVX2; baseline and differential.
DR   Genevisible; Q9NVX2; HS.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR   GO; GO:0001826; P:inner cell mass cell differentiation; IEA:Ensembl.
DR   GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR   GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR001632; Gprotein_B.
DR   InterPro; IPR012972; NLE.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF08154; NLE; 1.
DR   Pfam; PF00400; WD40; 7.
DR   PRINTS; PR00319; GPROTEINB.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 8.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 4.
DR   PROSITE; PS50082; WD_REPEATS_2; 7.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW   Notch signaling pathway; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   CHAIN           2..485
FT                   /note="Notchless protein homolog 1"
FT                   /id="PRO_0000051098"
FT   REPEAT          112..151
FT                   /note="WD 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          154..193
FT                   /note="WD 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          197..241
FT                   /note="WD 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          244..282
FT                   /note="WD 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          325..366
FT                   /note="WD 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          370..409
FT                   /note="WD 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          412..451
FT                   /note="WD 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          454..485
FT                   /note="WD 8"
FT                   /evidence="ECO:0000255"
FT   REGION          14..96
FT                   /note="Ubiquitin-like (UBL) domain"
FT                   /evidence="ECO:0000250|UniProtKB:P25382"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT   MOD_RES         79
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   VAR_SEQ         1..292
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_040555"
FT   VARIANT         6
FT                   /note="P -> A (in dbSNP:rs1471615)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5,
FT                   ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT                   /id="VAR_060327"
FT   VARIANT         169
FT                   /note="R -> K (in dbSNP:rs7215209)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_060328"
FT   VARIANT         319
FT                   /note="Q -> K (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs75635495)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035886"
FT   VARIANT         406
FT                   /note="Y -> H (in dbSNP:rs2306513)"
FT                   /id="VAR_057616"
FT   VARIANT         434
FT                   /note="S -> N (in dbSNP:rs2306512)"
FT                   /id="VAR_057617"
FT   CONFLICT        321
FT                   /note="S -> F (in Ref. 2; BAD92348)"
FT                   /evidence="ECO:0000305"
FT   STRAND          16..22
FT                   /evidence="ECO:0007829|PDB:6WAJ"
FT   STRAND          28..36
FT                   /evidence="ECO:0007829|PDB:6WAJ"
FT   HELIX           41..52
FT                   /evidence="ECO:0007829|PDB:6WAJ"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:6WAJ"
FT   HELIX           73..78
FT                   /evidence="ECO:0007829|PDB:6WAJ"
FT   STRAND          86..94
FT                   /evidence="ECO:0007829|PDB:6WAJ"
SQ   SEQUENCE   485 AA;  53320 MW;  E2E638B13884BC07 CRC64;
     MAAAVPDEAV ARDVQRLLVQ FQDEGGQLLG SPFDVPVDIT PDRLQLVCNA LLAQEDPLPL
     AFFVHDAEIV SSLGKTLESQ AVETEKVLDI IYQPQAIFRV RAVTRCTSSL EGHSEAVISV
     AFSPTGKYLA SGSGDTTVRF WDLSTETPHF TCKGHRHWVL SISWSPDGRK LASGCKNGQI
     LLWDPSTGKQ VGRTLAGHSK WITGLSWEPL HANPECRYVA SSSKDGSVRI WDTTAGRCER
     ILTGHTQSVT CLRWGGDGLL YSASQDRTIK VWRAHDGVLC RTLQGHGHWV NTMALSTDYA
     LRTGAFEPAE ASVNPQDLQG SLQELKERAL SRYNLVRGQG PERLVSGSDD FTLFLWSPAE
     DKKPLTRMTG HQALINQVLF SPDSRIVASA SFDKSIKLWD GRTGKYLASL RGHVAAVYQI
     AWSADSRLLV SGSSDSTLKV WDVKAQKLAM DLPGHADEVY AVDWSPDGQR VASGGKDKCL
     RIWRR
 
 
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