HECW2_HUMAN
ID HECW2_HUMAN Reviewed; 1572 AA.
AC Q9P2P5; B8ZZB4; Q17RT5; Q68DF8; Q9NPS9;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=E3 ubiquitin-protein ligase HECW2;
DE EC=2.3.2.26;
DE AltName: Full=HECT, C2 and WW domain-containing protein 2;
DE AltName: Full=HECT-type E3 ubiquitin transferase HECW2;
DE AltName: Full=NEDD4-like E3 ubiquitin-protein ligase 2;
GN Name=HECW2; Synonyms=KIAA1301, NEDL2;
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).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1352-1572 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart, and Lung;
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 FUNCTION, INTERACTION WITH TP73, AND TISSUE SPECIFICITY.
RX PubMed=12890487; DOI=10.1016/s0006-291x(03)01347-0;
RA Miyazaki K., Ozaki T., Kato C., Hanamoto T., Fujita T., Irino S.,
RA Watanabe K., Nakagawa T., Nakagawara A.;
RT "A novel HECT-type E3 ubiquitin ligase, NEDL2, stabilizes p73 and enhances
RT its transcriptional activity.";
RL Biochem. Biophys. Res. Commun. 308:106-113(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FZR1, AND UBIQUITINATION.
RX PubMed=24163370; DOI=10.1074/jbc.m113.472076;
RA Lu L., Hu S., Wei R., Qiu X., Lu K., Fu Y., Li H., Xing G., Li D., Peng R.,
RA He F., Zhang L.;
RT "The HECT type ubiquitin ligase NEDL2 is degraded by anaphase-promoting
RT complex/cyclosome (APC/C)-Cdh1, and its tight regulation maintains the
RT metaphase to anaphase transition.";
RL J. Biol. Chem. 288:35637-35650(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; SER-852 AND SER-909, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1175, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP INVOLVEMENT IN NDHSAL, AND VARIANTS NDHSAL GLN-1191; VAL-1193; TRP-1330 AND
RP GLY-1445.
RX PubMed=27389779; DOI=10.1136/jmedgenet-2016-103943;
RA Berko E.R., Cho M.T., Eng C., Shao Y., Sweetser D.A., Waxler J.,
RA Robin N.H., Brewer F., Donkervoort S., Mohassel P., Boennemann C.G.,
RA Bialer M., Moore C., Wolfe L.A., Tifft C.J., Shen Y., Retterer K.,
RA Millan F., Chung W.K.;
RT "De novo missense variants in HECW2 are associated with neurodevelopmental
RT delay and hypotonia.";
RL J. Med. Genet. 54:84-86(2017).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC TP73. Acts to stabilize TP73 and enhance activation of transcription by
CC TP73 (PubMed:12890487). Involved in the regulation of mitotic
CC metaphase/anaphase transition (PubMed:24163370).
CC {ECO:0000269|PubMed:12890487, ECO:0000269|PubMed:24163370}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with TP73 (PubMed:12890487). Interacts with FZR1
CC (PubMed:24163370). {ECO:0000269|PubMed:12890487,
CC ECO:0000269|PubMed:24163370}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:24163370}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2P5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2P5-2; Sequence=VSP_059106, VSP_059107, VSP_059108;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in adult brain, lung and
CC heart. {ECO:0000269|PubMed:12890487}.
CC -!- PTM: Ubiquitinated and degraded during mitotic exit by APC/C-Cdh1.
CC {ECO:0000269|PubMed:24163370}.
CC -!- DISEASE: Neurodevelopmental disorder with hypotonia, seizures, and
CC absent language (NDHSAL) [MIM:617268]: A neurodevelopmental disorder
CC characterized by severely delayed psychomotor development, absent
CC speech, epilepsy, encephalopathy, hypotonia, dystonia/dyskinesia, and
CC macrocephaly. Brain imaging show cerebral atrophy, enlarged ventricles,
CC and white matter abnormalities. {ECO:0000269|PubMed:27389779}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92539.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH18262.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AB037722; BAA92539.1; ALT_INIT; mRNA.
DR EMBL; AL390186; CAB99103.1; -; mRNA.
DR EMBL; CR749424; CAH18262.1; ALT_SEQ; mRNA.
DR EMBL; AC020571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC074090; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117194; AAI17195.1; -; mRNA.
DR EMBL; BC117198; AAI17199.1; -; mRNA.
DR CCDS; CCDS33354.1; -. [Q9P2P5-1]
DR PIR; T51886; T51886.
DR RefSeq; NP_065811.1; NM_020760.2. [Q9P2P5-1]
DR RefSeq; XP_016860052.1; XM_017004563.1.
DR PDB; 2LFE; NMR; -; A=43-162.
DR PDBsum; 2LFE; -.
DR AlphaFoldDB; Q9P2P5; -.
DR SMR; Q9P2P5; -.
DR BioGRID; 121581; 319.
DR IntAct; Q9P2P5; 13.
DR MINT; Q9P2P5; -.
DR STRING; 9606.ENSP00000260983; -.
DR iPTMnet; Q9P2P5; -.
DR PhosphoSitePlus; Q9P2P5; -.
DR BioMuta; HECW2; -.
DR DMDM; 126215718; -.
DR EPD; Q9P2P5; -.
DR jPOST; Q9P2P5; -.
DR MassIVE; Q9P2P5; -.
DR MaxQB; Q9P2P5; -.
DR PaxDb; Q9P2P5; -.
DR PeptideAtlas; Q9P2P5; -.
DR PRIDE; Q9P2P5; -.
DR ProteomicsDB; 83874; -. [Q9P2P5-1]
DR ProteomicsDB; 83875; -. [Q9P2P5-2]
DR Antibodypedia; 34059; 189 antibodies from 26 providers.
DR DNASU; 57520; -.
DR Ensembl; ENST00000260983.8; ENSP00000260983.2; ENSG00000138411.13. [Q9P2P5-1]
DR Ensembl; ENST00000644256.1; ENSP00000494649.1; ENSG00000138411.13. [Q9P2P5-1]
DR Ensembl; ENST00000644978.2; ENSP00000495418.1; ENSG00000138411.13. [Q9P2P5-1]
DR Ensembl; ENST00000647236.1; ENSP00000494800.1; ENSG00000138411.13. [Q9P2P5-2]
DR GeneID; 57520; -.
DR KEGG; hsa:57520; -.
DR MANE-Select; ENST00000644978.2; ENSP00000495418.1; NM_001348768.2; NP_001335697.1.
DR UCSC; uc002utl.2; human. [Q9P2P5-1]
DR CTD; 57520; -.
DR DisGeNET; 57520; -.
DR GeneCards; HECW2; -.
DR HGNC; HGNC:29853; HECW2.
DR HPA; ENSG00000138411; Low tissue specificity.
DR MalaCards; HECW2; -.
DR MIM; 617245; gene.
DR MIM; 617268; phenotype.
DR neXtProt; NX_Q9P2P5; -.
DR OpenTargets; ENSG00000138411; -.
DR PharmGKB; PA134925001; -.
DR VEuPathDB; HostDB:ENSG00000138411; -.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000155466; -.
DR HOGENOM; CLU_002173_14_0_1; -.
DR InParanoid; Q9P2P5; -.
DR OMA; TAGQHRE; -.
DR OrthoDB; 117748at2759; -.
DR PhylomeDB; Q9P2P5; -.
DR TreeFam; TF313938; -.
DR PathwayCommons; Q9P2P5; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9P2P5; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 57520; 15 hits in 1113 CRISPR screens.
DR ChiTaRS; HECW2; human.
DR GenomeRNAi; 57520; -.
DR Pharos; Q9P2P5; Tbio.
DR PRO; PR:Q9P2P5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9P2P5; protein.
DR Bgee; ENSG00000138411; Expressed in left ventricle myocardium and 165 other tissues.
DR ExpressionAtlas; Q9P2P5; baseline and differential.
DR Genevisible; Q9P2P5; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0048814; P:regulation of dendrite morphogenesis; IBA:GO_Central.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
DR CDD; cd08691; C2_NEDL1-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037795; C2_HECW.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
DR InterPro; IPR032348; HECW_N.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF16562; HECW_N; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Phosphoprotein; Reference proteome; Repeat; Transferase;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..1572
FT /note="E3 ubiquitin-protein ligase HECW2"
FT /id="PRO_0000277667"
FT DOMAIN 167..301
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 807..840
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 985..1018
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 1237..1572
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 341..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..1068
FT /note="Interaction with TP73"
FT /evidence="ECO:0000269|PubMed:12890487"
FT REGION 1024..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 847..874
FT /evidence="ECO:0000255"
FT COMPBIAS 382..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1540
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..131
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_059106"
FT VAR_SEQ 191..213
FT /note="DLRAVGLKKGMFFNPDPYLKMSI -> ARKEEQFPHLCPPRAGETVYYHQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_059107"
FT VAR_SEQ 214..1572
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_059108"
FT VARIANT 1191
FT /note="R -> Q (in NDHSAL; dbSNP:rs878854416)"
FT /evidence="ECO:0000269|PubMed:27389779"
FT /id="VAR_077905"
FT VARIANT 1193
FT /note="F -> V (in NDHSAL; dbSNP:rs878854422)"
FT /evidence="ECO:0000269|PubMed:27389779"
FT /id="VAR_077906"
FT VARIANT 1330
FT /note="R -> W (in NDHSAL; dbSNP:rs878854417)"
FT /evidence="ECO:0000269|PubMed:27389779"
FT /id="VAR_077907"
FT VARIANT 1445
FT /note="E -> G (in NDHSAL; dbSNP:rs878854424)"
FT /evidence="ECO:0000269|PubMed:27389779"
FT /id="VAR_077908"
FT CONFLICT 1074
FT /note="Q -> H (in Ref. 2; CAH18262)"
FT /evidence="ECO:0000305"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:2LFE"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2LFE"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:2LFE"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2LFE"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2LFE"
FT STRAND 133..144
FT /evidence="ECO:0007829|PDB:2LFE"
FT TURN 145..148
FT /evidence="ECO:0007829|PDB:2LFE"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:2LFE"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:2LFE"
SQ SEQUENCE 1572 AA; 175769 MW; DCFF0146ADFAF8BE CRC64;
MASSAREHLL FVRRRNPQMR YTLSPENLQS LAAQSSMPEN MTLQRANSDT DLVTSESRSS
LTASMYEYTL GQAQNLIIFW DIKEEVDPSD WIGLYHIDEN SPANFWDSKN RGVTGTQKGQ
IVWRIEPGPY FMEPEIKICF KYYHGISGAL RATTPCITVK NPAVMMGAEG MEGGASGNLH
SRKLVSFTLS DLRAVGLKKG MFFNPDPYLK MSIQPGKKSS FPTCAHHGQE RRSTIISNTT
NPIWHREKYS FFALLTDVLE IEIKDKFAKS RPIIKRFLGK LTIPVQRLLE RQAIGDQMLS
YNLGRRLPAD HVSGYLQFKV EVTSSVHEDA SPEAVGTILG VNSVNGDLGS PSDDEDMPGS
HHDSQVCSNG PVSEDSAADG TPKHSFRTSS TLEIDTEELT STSSRTSPPR GRQDSLNDYL
DAIEHNGHSR PGTATCSERS MGASPKLRSS FPTDTRLNAM LHIDSDEEDH EFQQDLGYPS
SLEEEGGLIM FSRASRADDG SLTSQTKLED NPVENEEAST HEAASFEDKP ENLPELAESS
LPAGPAPEEG EGGPEPQPSA DQGSAELCGS QEVDQPTSGA DTGTSDASGG SRRAVSETES
LDQGSEPSQV SSETEPSDPA RTESVSEAST RPEGESDLEC ADSSCNESVT TQLSSVDTRC
SSLESARFPE TPAFSSQEEE DGACAAEPTS SGPAEGSQES VCTAGSLPVV QVPSGEDEGP
GAESATVPDQ EELGEVWQRR GSLEGAAAAA ESPPQEEGSA GEAQGTCEGA TAQEEGATGG
SQANGHQPLR SLPSVRQDVS RYQRVDEALP PNWEARIDSH GRIFYVDHVN RTTTWQRPTA
PPAPQVLQRS NSIQQMEQLN RRYQSIRRTM TNERPEENTN AIDGAGEEAD FHQASADFRR
ENILPHSTSR SRITLLLQSP PVKFLISPEF FTVLHSNPSA YRMFTNNTCL KHMITKVRRD
THHFERYQHN RDLVGFLNMF ANKQLELPRG WEMKHDHQGK AFFVDHNSRT TTFIDPRLPL
QSSRPTSALV HRQHLTRQRS HSAGEVGEDS RHAGPPVLPR PSSTFNTVSR PQYQDMVPVA
YNDKIVAFLR QPNIFEILQE RQPDLTRNHS LREKIQFIRT EGTPGLVRLS SDADLVMLLS
LFEEEIMSYV PPHALLHPSY CQSPRGSPVS SPQNSPGTQR ANARAPAPYK RDFEAKLRNF
YRKLETKGYG QGPGKLKLII RRDHLLEDAF NQIMGYSRKD LQRNKLYVTF VGEEGLDYSG
PSREFFFLVS RELFNPYYGL FEYSANDTYT VQISPMSAFV DNHHEWFRFS GRILGLALIH
QYLLDAFFTR PFYKALLRIL CDLSDLEYLD EEFHQSLQWM KDNDIHDILD LTFTVNEEVF
GQITERELKP GGANIPVTEK NKKEYIERMV KWRIERGVVQ QTESLVRGFY EVVDARLVSV
FDARELELVI AGTAEIDLSD WRNNTEYRGG YHDNHIVIRW FWAAVERFNN EQRLRLLQFV
TGTSSIPYEG FASLRGSNGP RRFCVEKWGK ITALPRAHTC FNRLDLPPYP SFSMLYEKLL
TAVEETSTFG LE
