SP140_HUMAN
ID SP140_HUMAN Reviewed; 867 AA.
AC Q13342; E7ESH9; E7EUR5; E9PFJ6; Q0VGE5; Q13341; Q3KR17; Q4ZG66; Q53TG1;
AC Q6NSG4; Q92881; Q96TG3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Nuclear body protein SP140 {ECO:0000312|HGNC:HGNC:17133};
DE AltName: Full=Lymphoid-restricted homolog of Sp100 {ECO:0000303|PubMed:8695863};
DE Short=LYSp100 {ECO:0000303|PubMed:8695863};
DE AltName: Full=Nuclear autoantigen Sp-140 {ECO:0000303|PubMed:8910577};
DE AltName: Full=Speckled 140 kDa {ECO:0000303|PubMed:8910577};
GN Name=SP140 {ECO:0000312|HGNC:HGNC:17133};
GN Synonyms=LYSP100 {ECO:0000303|PubMed:8695863};
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] (ISOFORMS LYSP100-A AND LYSP100-B), SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8695863;
RA Dent A.L., Yewdell J., Puvion-Dutilleul F., Koken M.H.M., de The H.,
RA Staudt L.M.;
RT "LYSP100-associated nuclear domains (LANDs): description of a new class of
RT subnuclear structures and their relationship to PML nuclear bodies.";
RL Blood 88:1423-1426(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SP140), VARIANT LYS-516, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY INTERFERON.
RC TISSUE=Placenta;
RX PubMed=8910577; DOI=10.1074/jbc.271.46.29198;
RA Bloch D.B., de la Monte S.M., Guigaouri P., Filippov A., Bloch K.D.;
RT "Identification and characterization of a leukocyte-specific component of
RT the nuclear body.";
RL J. Biol. Chem. 271:29198-29204(1996).
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 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6), AND VARIANT
RP LYS-516.
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 STRUCTURE BY NMR OF 687-738, FUNCTION, PHOSPHORYLATION AT THR-726, AND
RP INTERACTION WITH PIN1.
RX PubMed=24267382; DOI=10.1111/febs.12588;
RA Zucchelli C., Tamburri S., Quilici G., Palagano E., Berardi A., Saare M.,
RA Peterson P., Bachi A., Musco G.;
RT "Structure of human Sp140 PHD finger: an atypical fold interacting with
RT Pin1.";
RL FEBS J. 281:216-231(2014).
CC -!- FUNCTION: Component of the nuclear body, also known as nuclear domain
CC 10, PML oncogenic domain, and KR body (PubMed:8910577). May be involved
CC in the pathogenesis of acute promyelocytic leukemia and viral infection
CC (PubMed:8910577). May play a role in chromatin-mediated regulation of
CC gene expression although it does not bind to histone H3 tails
CC (PubMed:24267382). {ECO:0000269|PubMed:24267382,
CC ECO:0000269|PubMed:8910577, ECO:0000303|PubMed:8910577}.
CC -!- SUBUNIT: Interacts with PIN1. {ECO:0000269|PubMed:24267382}.
CC -!- INTERACTION:
CC Q13342; Q16236: NFE2L2; NbExp=4; IntAct=EBI-2865100, EBI-2007911;
CC Q13342; Q13526: PIN1; NbExp=4; IntAct=EBI-2865100, EBI-714158;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8695863,
CC ECO:0000269|PubMed:8910577}. Nucleus, PML body
CC {ECO:0000269|PubMed:8695863, ECO:0000269|PubMed:8910577}. Cytoplasm
CC {ECO:0000269|PubMed:8695863}. Note=Localized to nuclear structures
CC termed LANDS, for LYSp100-associated nuclear domains. LANDS are
CC globular, electron-dense structures most often found in the
CC nucleoplasm, but also found at the nuclear membrane and in the
CC cytoplasm, suggesting that these structures may traffic between the
CC cytoplasm and the nucleus (PubMed:8695863). Also colocalizes with PML
CC in a subset of PML nuclear bodies (PubMed:8910577).
CC {ECO:0000269|PubMed:8695863, ECO:0000269|PubMed:8910577}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=LYSp100-B {ECO:0000303|PubMed:8695863};
CC IsoId=Q13342-1; Sequence=Displayed;
CC Name=LYSp100-A {ECO:0000303|PubMed:8695863};
CC IsoId=Q13342-2; Sequence=VSP_000560, VSP_000561, VSP_000562;
CC Name=Sp140 {ECO:0000303|PubMed:8695863};
CC IsoId=Q13342-3; Sequence=VSP_055922, VSP_000558, VSP_000559;
CC Name=4;
CC IsoId=Q13342-4; Sequence=VSP_043235, VSP_043236;
CC Name=5;
CC IsoId=Q13342-5; Sequence=VSP_055924;
CC Name=6;
CC IsoId=Q13342-6; Sequence=VSP_055923, VSP_000560;
CC -!- TISSUE SPECIFICITY: High levels in spleen and peripheral blood
CC leukocytes, much lower levels in tonsils, thymus, prostate, ovary,
CC small intestine, and colon (PubMed:8695863, PubMed:8910577.) Very low
CC levels in heart, brain, placenta, lung, liver, skeletal muscle, kidney,
CC and pancreas (PubMed:8910577). Not detected in brain, liver and muscle
CC (PubMed:8695863). {ECO:0000269|PubMed:8695863,
CC ECO:0000269|PubMed:8910577}.
CC -!- INDUCTION: By gamma-interferon. {ECO:0000269|PubMed:8910577}.
CC -!- PTM: Phosphorylation at Thr-726 promotes binding of PIN1 and subsequent
CC isomerization of Pro-727. {ECO:0000269|PubMed:24267382}.
CC -!- MISCELLANEOUS: This antigen is recognized by autoantibodies from
CC patients with primary biliary cirrhosis. {ECO:0000269|PubMed:8910577}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18617.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAX93282.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U36499; AAB18616.1; -; mRNA.
DR EMBL; U36500; AAB18617.1; ALT_FRAME; mRNA.
DR EMBL; U63420; AAC50817.1; -; mRNA.
DR EMBL; AC009949; AAX88868.1; -; Genomic_DNA.
DR EMBL; AC009950; AAX93282.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471063; EAW70922.1; -; Genomic_DNA.
DR EMBL; BC105743; AAI05744.1; -; mRNA.
DR EMBL; BC105960; AAI05961.1; -; mRNA.
DR EMBL; BC070160; AAH70160.1; -; mRNA.
DR CCDS; CCDS33392.1; -. [Q13342-4]
DR CCDS; CCDS42831.1; -. [Q13342-1]
DR CCDS; CCDS63149.1; -. [Q13342-3]
DR CCDS; CCDS63150.1; -. [Q13342-5]
DR CCDS; CCDS63151.1; -. [Q13342-6]
DR PIR; G02099; G02099.
DR RefSeq; NP_001005176.1; NM_001005176.2. [Q13342-4]
DR RefSeq; NP_001265380.1; NM_001278451.1. [Q13342-5]
DR RefSeq; NP_001265381.1; NM_001278452.1. [Q13342-6]
DR RefSeq; NP_001265382.1; NM_001278453.1. [Q13342-3]
DR RefSeq; NP_009168.4; NM_007237.4. [Q13342-1]
DR PDB; 2MD7; NMR; -; B=687-738.
DR PDB; 2MD8; NMR; -; C=687-738.
DR PDB; 6G8R; X-ray; 2.74 A; B=687-862.
DR PDBsum; 2MD7; -.
DR PDBsum; 2MD8; -.
DR PDBsum; 6G8R; -.
DR AlphaFoldDB; Q13342; -.
DR BMRB; Q13342; -.
DR SMR; Q13342; -.
DR BioGRID; 116422; 8.
DR IntAct; Q13342; 8.
DR MINT; Q13342; -.
DR STRING; 9606.ENSP00000375899; -.
DR ChEMBL; CHEMBL3108643; -.
DR iPTMnet; Q13342; -.
DR PhosphoSitePlus; Q13342; -.
DR BioMuta; SP140; -.
DR DMDM; 218511671; -.
DR EPD; Q13342; -.
DR jPOST; Q13342; -.
DR MassIVE; Q13342; -.
DR MaxQB; Q13342; -.
DR PaxDb; Q13342; -.
DR PeptideAtlas; Q13342; -.
DR PRIDE; Q13342; -.
DR ProteomicsDB; 17997; -.
DR ProteomicsDB; 18479; -.
DR ProteomicsDB; 20120; -.
DR ProteomicsDB; 59329; -. [Q13342-1]
DR ProteomicsDB; 59330; -. [Q13342-2]
DR ProteomicsDB; 59331; -. [Q13342-3]
DR ProteomicsDB; 59332; -. [Q13342-4]
DR ABCD; Q13342; 1 sequenced antibody.
DR Antibodypedia; 1754; 160 antibodies from 26 providers.
DR DNASU; 11262; -.
DR Ensembl; ENST00000343805.10; ENSP00000342096.6; ENSG00000079263.19. [Q13342-6]
DR Ensembl; ENST00000373645.3; ENSP00000362749.3; ENSG00000079263.19. [Q13342-4]
DR Ensembl; ENST00000392045.8; ENSP00000375899.3; ENSG00000079263.19. [Q13342-1]
DR Ensembl; ENST00000417495.7; ENSP00000393618.3; ENSG00000079263.19. [Q13342-3]
DR Ensembl; ENST00000420434.7; ENSP00000398210.3; ENSG00000079263.19. [Q13342-5]
DR GeneID; 11262; -.
DR KEGG; hsa:11262; -.
DR MANE-Select; ENST00000392045.8; ENSP00000375899.3; NM_007237.5; NP_009168.4.
DR UCSC; uc002vqj.4; human. [Q13342-1]
DR CTD; 11262; -.
DR DisGeNET; 11262; -.
DR GeneCards; SP140; -.
DR HGNC; HGNC:17133; SP140.
DR HPA; ENSG00000079263; Group enriched (intestine, lymphoid tissue).
DR MalaCards; SP140; -.
DR MIM; 608602; gene.
DR neXtProt; NX_Q13342; -.
DR OpenTargets; ENSG00000079263; -.
DR PharmGKB; PA38205; -.
DR VEuPathDB; HostDB:ENSG00000079263; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162129; -.
DR HOGENOM; CLU_015844_1_0_1; -.
DR InParanoid; Q13342; -.
DR OMA; IRGGHER; -.
DR OrthoDB; 377499at2759; -.
DR PhylomeDB; Q13342; -.
DR TreeFam; TF335091; -.
DR PathwayCommons; Q13342; -.
DR SignaLink; Q13342; -.
DR BioGRID-ORCS; 11262; 9 hits in 1091 CRISPR screens.
DR ChiTaRS; SP140; human.
DR GenomeRNAi; 11262; -.
DR Pharos; Q13342; Tbio.
DR PRO; PR:Q13342; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q13342; protein.
DR Bgee; ENSG00000079263; Expressed in lymph node and 101 other tissues.
DR ExpressionAtlas; Q13342; baseline and differential.
DR Genevisible; Q13342; HS.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; TAS:ProtInc.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.10.390.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR IDEAL; IID00667; -.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR004865; HSR_dom.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR InterPro; IPR043563; Sp110/Sp140/Sp140L.
DR InterPro; IPR030411; Sp140.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46386; PTHR46386; 2.
DR PANTHER; PTHR46386:SF6; PTHR46386:SF6; 2.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF03172; HSR; 1.
DR Pfam; PF01342; SAND; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF63763; SSF63763; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51414; HSR; 1.
DR PROSITE; PS50864; SAND; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Bromodomain; Cytoplasm; DNA-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..867
FT /note="Nuclear body protein SP140"
FT /id="PRO_0000211206"
FT DOMAIN 22..138
FT /note="HSR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00747"
FT DOMAIN 580..661
FT /note="SAND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT DOMAIN 796..829
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 690..736
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 260..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 495..514
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 266..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..509
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 726
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24267382"
FT VAR_SEQ 136..172
FT /note="VCYEHSPLQMNNVNDLEDRPRLLPYGKQENSNACHEM -> ENLSSSAVLCQ
FT LVSPNKDWRSHEESLAHTGTLRRSCM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043235"
FT VAR_SEQ 173..867
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043236"
FT VAR_SEQ 219..221
FT /note="Missing (in isoform Sp140)"
FT /evidence="ECO:0000303|PubMed:8910577"
FT /id="VSP_055922"
FT VAR_SEQ 222..247
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055923"
FT VAR_SEQ 248..297
FT /note="Missing (in isoform Sp140)"
FT /evidence="ECO:0000303|PubMed:8910577"
FT /id="VSP_000558"
FT VAR_SEQ 326..386
FT /note="Missing (in isoform Sp140)"
FT /evidence="ECO:0000303|PubMed:8910577"
FT /id="VSP_000559"
FT VAR_SEQ 353..386
FT /note="Missing (in isoform LYSp100-A and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8695863"
FT /id="VSP_000560"
FT VAR_SEQ 387..413
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055924"
FT VAR_SEQ 405..446
FT /note="SSSLARRGSVSSELENHPMNEEGESEELASSLLYDNVPGAEQ -> QKQGRK
FT VIKRVAQWILWILQTTPLWENPRGKEEKRGGMAGAE (in isoform LYSp100-
FT A)"
FT /evidence="ECO:0000303|PubMed:8695863"
FT /id="VSP_000561"
FT VAR_SEQ 447..867
FT /note="Missing (in isoform LYSp100-A)"
FT /evidence="ECO:0000303|PubMed:8695863"
FT /id="VSP_000562"
FT VARIANT 356
FT /note="L -> F (in dbSNP:rs3820975)"
FT /id="VAR_055555"
FT VARIANT 512
FT /note="M -> T (in dbSNP:rs4972945)"
FT /id="VAR_055556"
FT VARIANT 516
FT /note="E -> K (in dbSNP:rs4972946)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8910577"
FT /id="VAR_055557"
FT VARIANT 558
FT /note="R -> C (in dbSNP:rs11887179)"
FT /id="VAR_055558"
FT CONFLICT 186
FT /note="P -> A (in Ref. 1; AAB18616/AAB18617 and 2;
FT AAC50817)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..358
FT /note="LSA -> FST (in Ref. 1; AAB18617)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="V -> D (in Ref. 5; AAI05744)"
FT /evidence="ECO:0000305"
FT CONFLICT 838
FT /note="D -> G (in Ref. 1; AAB18617)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="E -> G (in Ref. 1; AAB18617)"
FT /evidence="ECO:0000305"
FT TURN 694..696
FT /evidence="ECO:0007829|PDB:6G8R"
FT STRAND 706..709
FT /evidence="ECO:0007829|PDB:6G8R"
FT TURN 714..716
FT /evidence="ECO:0007829|PDB:6G8R"
FT STRAND 717..719
FT /evidence="ECO:0007829|PDB:6G8R"
FT STRAND 722..724
FT /evidence="ECO:0007829|PDB:2MD7"
FT STRAND 725..727
FT /evidence="ECO:0007829|PDB:6G8R"
FT HELIX 731..735
FT /evidence="ECO:0007829|PDB:6G8R"
FT HELIX 747..752
FT /evidence="ECO:0007829|PDB:6G8R"
FT HELIX 757..772
FT /evidence="ECO:0007829|PDB:6G8R"
FT HELIX 776..780
FT /evidence="ECO:0007829|PDB:6G8R"
FT HELIX 784..787
FT /evidence="ECO:0007829|PDB:6G8R"
FT HELIX 801..809
FT /evidence="ECO:0007829|PDB:6G8R"
FT HELIX 816..831
FT /evidence="ECO:0007829|PDB:6G8R"
FT TURN 840..843
FT /evidence="ECO:0007829|PDB:6G8R"
FT HELIX 844..857
FT /evidence="ECO:0007829|PDB:6G8R"
SQ SEQUENCE 867 AA; 98223 MW; 355601D1D4689A74 CRC64;
MAQQGQQGQM ASGDSNLNFR MVAEIQNVEG QNLQEQVCPE PIFRFFRENK VEIASAITRP
FPFLMGLRDR SFISEQMYEH FQEAFRNLVP VTRVMYCVLS ELEKTFGWSH LEALFSRINL
MAYPDLNEIY RSFQNVCYEH SPLQMNNVND LEDRPRLLPY GKQENSNACH EMDDIAVPQE
ALSSSPRCEP GFSSESCEQL ALPKAGGGDA EDAPSLLPGG GVSCKLAIQI DEGESEEMPK
LLPYDTEVLE SNGMIDAART YSTAPGEKQG EEEGRNSPRK RNQDKEKYQE SPEGRDKETF
DLKTPQVTNE GEPEKGLCLL PGEGEEGSDD CSEMCDGEEP QEASSSLARC GSVSCLSAET
FDLKTPQVTN EGEPEKELSL LPGEGEEGSD DCSEMCDGEE RQEASSSLAR RGSVSSELEN
HPMNEEGESE ELASSLLYDN VPGAEQSAYE NEKCSCVMCF SEEVPGSPEA RTESDQACGT
MDTVDIANNS TLGKPKRKRR KKRGHGWSRM RMRRQENSQQ NDNSKADGQV VSSEKKANVN
LKDLSKIRGR KRGKPGTRFT QSDRAAQKRV RSRASRKHKD ETVDFKAPLL PVTCGGVKGI
LHKKKLQQGI LVKCIQTEDG KWFTPTEFEI KGGHARSKNW RLSVRCGGWP LRWLMENGFL
PDPPRIRYRK KKRILKSQNN SSVDPCMRNL DECEVCRDGG ELFCCDTCSR VFHEDCHIPP
VEAERTPWNC IFCRMKESPG SQQCCQESEV LERQMCPEEQ LKCEFLLLKV YCCSESSFFA
KIPYYYYIRE ACQGLKEPMW LDKIKKRLNE HGYPQVEGFV QDMRLIFQNH RASYKYKDFG
QMGFRLEAEF EKNFKEVFAI QETNGNN
