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   27-MAR-2024, entry version 197.
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).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25593309; DOI=10.1101/gad.252189.114;
RA   Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W.,
RA   Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.;
RT   "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of
RT   transcription-associated DNA damage that promotes homologous
RT   recombination.";
RL   Genes Dev. 29:197-211(2015).
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:25593309,
CC       ECO:0000269|PubMed:8695863, ECO:0000269|PubMed:8910577}. Nucleus, PML
CC       body {ECO:0000269|PubMed:8695863, ECO:0000269|PubMed:8910577}.
CC       Cytoplasm {ECO:0000269|PubMed:8695863}. Note=Localized to nuclear
CC       structures termed LANDS, for LYSp100-associated nuclear domains. LANDS
CC       are 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};
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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; 9606-ENSP00000375899; -.
DR   PeptideAtlas; 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; 184 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   AGR; HGNC:17133; -.
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; LGNSDEC; -.
DR   OrthoDB; 38708at2759; -.
DR   PhylomeDB; Q13342; -.
DR   TreeFam; TF335091; -.
DR   PathwayCommons; Q13342; -.
DR   SignaLink; Q13342; -.
DR   BioGRID-ORCS; 11262; 13 hits in 1179 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 103 other cell types or tissues.
DR   ExpressionAtlas; Q13342; baseline and differential.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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   CDD; cd05501; Bromo_SP100C_like; 1.
DR   CDD; cd15626; PHD_SP110_140; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.10.390.10; SAND domain-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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-like.
DR   InterPro; IPR030411; Sp140_Bromo.
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; NUCLEAR BODY PROTEIN SP140; 1.
DR   PANTHER; PTHR46386:SF8; NUCLEAR BODY PROTEIN SP140; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF03172; HSR; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF01342; SAND; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00258; SAND; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF63763; SAND domain-like; 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.
DR   Genevisible; Q13342; HS.
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
FT                   LYSp100-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
//