ID   ICE2_HUMAN              Reviewed;         982 AA.
AC   Q659A1; B2RU08; Q05CT1; Q3B7W6; Q63HP4; Q658Q0; Q68CN8; Q6IPW7; Q6UX23;
AC   Q71H65; Q96CY5; Q9HAA2;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   24-JAN-2024, entry version 135.
DE   RecName: Full=Little elongation complex subunit 2;
DE   AltName: Full=Interactor of little elongator complex ELL subunit 2;
DE   AltName: Full=NMDA receptor-regulated protein 2;
GN   Name=ICE2; Synonyms=BRCC1, NARG2; ORFNames=UNQ3101/PRO10100;
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).
RC   TISSUE=Mammary cancer;
RA   Gokhale P.C., Dritschilo A., Rahman A., Ahmad I., Kasid U.N.;
RT   "Novel transcript in human breast cancer cells.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryo, and Kidney;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Adipose tissue, Bone marrow, Fetal kidney, and Heart;
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   [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] (ISOFORM 1).
RC   TISSUE=Bone, Brain, Ovary, and Testis;
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   IDENTIFICATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15606750; DOI=10.1111/j.1432-1033.2004.04414.x;
RA   Sugiura N., Dadashev V., Corriveau R.A.;
RT   "NARG2 encodes a novel nuclear protein with (S/T)PXX motifs that is
RT   expressed during development.";
RL   Eur. J. Biochem. 271:4629-4637(2004).
RN   [8]
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(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   IDENTIFICATION IN THE LEC COMPLEX, AND INTERACTION WITH ELL.
RX   PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
RA   Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
RA   Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P.,
RA   Eissenberg J.C., Shilatifard A.;
RT   "The little elongation complex regulates small nuclear RNA transcription.";
RL   Mol. Cell 44:954-965(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-326, 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   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE LEC COMPLEX, AND
RP   INTERACTION WITH ICE1.
RX   PubMed=23932780; DOI=10.1016/j.molcel.2013.07.003;
RA   Hu D., Smith E.R., Garruss A.S., Mohaghegh N., Varberg J.M., Lin C.,
RA   Jackson J., Gao X., Saraf A., Florens L., Washburn M.P., Eissenberg J.C.,
RA   Shilatifard A.;
RT   "The little elongation complex functions at initiation and elongation
RT   phases of snRNA gene transcription.";
RL   Mol. Cell 51:493-505(2013).
RN   [14]
RP   IDENTIFICATION BY 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).
CC   -!- FUNCTION: Component of the little elongation complex (LEC), a complex
CC       required to regulate small nuclear RNA (snRNA) gene transcription by
CC       RNA polymerase II and III. {ECO:0000269|PubMed:23932780}.
CC   -!- SUBUNIT: Component of the little elongation complex (LEC), at least
CC       composed of ELL (ELL, ELL2 or ELL3), ZC3H8, ICE1 and ICE2. Interacts
CC       with ICE1 (via C-terminus domain). Interacts with ELL.
CC       {ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23932780}.
CC   -!- INTERACTION:
CC       Q659A1; P55199: ELL; NbExp=5; IntAct=EBI-4322746, EBI-1245868;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23932780}.
CC       Note=Colocalizes with COIL in subnuclear Cajal and histone locus
CC       bodies. Translocates in the LEC complex to Cajal and histone locus
CC       bodies at snRNA genes in a ICE1-dependent manner. Associates to
CC       transcriptionally active chromatin at snRNA genes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q659A1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q659A1-2; Sequence=VSP_041612, VSP_041613;
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in lung and testis.
CC       {ECO:0000269|PubMed:15606750}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal brain, kidney, liver and lung.
CC       {ECO:0000269|PubMed:15606750}.
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   -!- SIMILARITY: Belongs to the ICE2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH13684.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH20918.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAI07428.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC       Sequence=AAQ88910.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
CC       Sequence=BAB13948.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAH18700.1; Type=Erroneous translation; Note=Wrong choice of CDS.; 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; AF502591; AAQ07460.1; -; mRNA.
DR   EMBL; AY358546; AAQ88910.1; ALT_SEQ; mRNA.
DR   EMBL; CR749852; CAH18700.1; ALT_SEQ; mRNA.
DR   EMBL; BX647873; CAH56197.1; -; mRNA.
DR   EMBL; AK021958; BAB13948.1; ALT_INIT; mRNA.
DR   EMBL; AK055752; BAG51567.1; -; mRNA.
DR   EMBL; AL833122; CAH56202.1; -; mRNA.
DR   EMBL; AL832046; CAH56220.1; -; mRNA.
DR   EMBL; CH471082; EAW77589.1; -; Genomic_DNA.
DR   EMBL; BC013684; AAH13684.1; ALT_INIT; mRNA.
DR   EMBL; BC020918; AAH20918.1; ALT_SEQ; mRNA.
DR   EMBL; BC071685; AAH71685.1; -; mRNA.
DR   EMBL; BC107427; AAI07428.1; ALT_SEQ; mRNA.
DR   EMBL; BC140894; AAI40895.1; -; mRNA.
DR   CCDS; CCDS10176.1; -. [Q659A1-1]
DR   RefSeq; NP_001018099.1; NM_001018089.2.
DR   RefSeq; NP_078887.2; NM_024611.5. [Q659A1-1]
DR   RefSeq; XP_005254718.1; XM_005254661.1.
DR   RefSeq; XP_011520311.1; XM_011522009.1. [Q659A1-1]
DR   RefSeq; XP_016878058.1; XM_017022569.1. [Q659A1-1]
DR   AlphaFoldDB; Q659A1; -.
DR   BioGRID; 122789; 82.
DR   ComplexPortal; CPX-2712; Little elongation complex, ELL variant.
DR   ComplexPortal; CPX-2713; Little elongation complex, ELL2 variant.
DR   ComplexPortal; CPX-2714; Little elongation complex, ELL3 variant.
DR   IntAct; Q659A1; 36.
DR   STRING; 9606.ENSP00000261520; -.
DR   iPTMnet; Q659A1; -.
DR   PhosphoSitePlus; Q659A1; -.
DR   BioMuta; ICE2; -.
DR   DMDM; 156632596; -.
DR   EPD; Q659A1; -.
DR   jPOST; Q659A1; -.
DR   MassIVE; Q659A1; -.
DR   MaxQB; Q659A1; -.
DR   PaxDb; 9606-ENSP00000261520; -.
DR   PeptideAtlas; Q659A1; -.
DR   ProteomicsDB; 65932; -. [Q659A1-1]
DR   ProteomicsDB; 65933; -. [Q659A1-2]
DR   Pumba; Q659A1; -.
DR   Antibodypedia; 25471; 158 antibodies from 20 providers.
DR   DNASU; 79664; -.
DR   Ensembl; ENST00000261520.9; ENSP00000261520.4; ENSG00000128915.12. [Q659A1-1]
DR   Ensembl; ENST00000558181.5; ENSP00000453593.1; ENSG00000128915.12. [Q659A1-2]
DR   Ensembl; ENST00000560668.5; ENSP00000453303.1; ENSG00000128915.12. [Q659A1-2]
DR   GeneID; 79664; -.
DR   KEGG; hsa:79664; -.
DR   MANE-Select; ENST00000261520.9; ENSP00000261520.4; NM_024611.6; NP_078887.2.
DR   UCSC; uc002agp.5; human. [Q659A1-1]
DR   AGR; HGNC:29885; -.
DR   CTD; 79664; -.
DR   DisGeNET; 79664; -.
DR   GeneCards; ICE2; -.
DR   HGNC; HGNC:29885; ICE2.
DR   HPA; ENSG00000128915; Tissue enhanced (parathyroid).
DR   MIM; 610835; gene.
DR   neXtProt; NX_Q659A1; -.
DR   OpenTargets; ENSG00000128915; -.
DR   PharmGKB; PA134960292; -.
DR   VEuPathDB; HostDB:ENSG00000128915; -.
DR   eggNOG; ENOG502QUWA; Eukaryota.
DR   GeneTree; ENSGT00390000006883; -.
DR   HOGENOM; CLU_327237_0_0_1; -.
DR   InParanoid; Q659A1; -.
DR   OMA; LPFHQQH; -.
DR   OrthoDB; 1368245at2759; -.
DR   PhylomeDB; Q659A1; -.
DR   TreeFam; TF106272; -.
DR   PathwayCommons; Q659A1; -.
DR   Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR   SignaLink; Q659A1; -.
DR   SIGNOR; Q659A1; -.
DR   BioGRID-ORCS; 79664; 358 hits in 1156 CRISPR screens.
DR   ChiTaRS; ICE2; human.
DR   GenomeRNAi; 79664; -.
DR   Pharos; Q659A1; Tbio.
DR   PRO; PR:Q659A1; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q659A1; Protein.
DR   Bgee; ENSG00000128915; Expressed in colonic epithelium and 189 other cell types or tissues.
DR   ExpressionAtlas; Q659A1; baseline and differential.
DR   GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR   GO; GO:0035363; C:histone locus body; IDA:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IMP:UniProtKB.
DR   GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0042796; P:snRNA transcription by RNA polymerase III; IMP:UniProtKB.
DR   InterPro; IPR019535; ICE2_C.
DR   PANTHER; PTHR14633; LITTLE ELONGATION COMPLEX SUBUNIT 2; 1.
DR   PANTHER; PTHR14633:SF3; LITTLE ELONGATION COMPLEX SUBUNIT 2; 1.
DR   Pfam; PF10505; NARG2_C; 1.
DR   Genevisible; Q659A1; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..982
FT                   /note="Little elongation complex subunit 2"
FT                   /id="PRO_0000297964"
FT   REGION          410..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          473..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          930..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..493
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        930..968
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         326
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         571
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UZ18"
FT   MOD_RES         573
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3UZ18"
FT   VAR_SEQ         50..73
FT                   /note="RIGENLNASASSVENEPAVSSATQ -> ESRGVMWTCWLNTQRFLQIPKLLE
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_041612"
FT   VAR_SEQ         74..982
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_041613"
FT   CONFLICT        272
FT                   /note="L -> P (in Ref. 4; CAH18700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        316
FT                   /note="S -> L (in Ref. 4; CAH18700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        355
FT                   /note="T -> P (in Ref. 4; CAH56220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        621
FT                   /note="T -> S (in Ref. 4; CAH56220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        753
FT                   /note="T -> A (in Ref. 4; CAH18700)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        906
FT                   /note="W -> R (in Ref. 3; BAB13948)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        947
FT                   /note="P -> S (in Ref. 4; CAH56197)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   982 AA;  110011 MW;  09B36E742FC77597 CRC64;
     MSSKMVISEP GLNWDISPKN GLKTFFSREN YKDHSMAPSL KELRVLSNRR IGENLNASAS
     SVENEPAVSS ATQAKEKVKT TIGMVLLPKP RVPYPRFSRF SQREQRSYVD LLVKYAKIPA
     NSKAVGINKN DYLQYLDMKK HVNEEVTEFL KFLQNSAKKC AQDYNMLSDD ARLFTEKILR
     ACIEQVKKYS EFYTLHEVTS LMGFFPFRVE MGLKLEKTLL ALGSVKYVKT VFPSMPIKLQ
     LSKDDIATIE TSEQTAEAMH YDISKDPNAE KLVSRYHPQI ALTSQSLFTL LNNHGPTYKE
     QWEIPVCIQV IPVAGSKPVK VIYINSPLPQ KKMTMRERNQ IFHEVPLKFM MSKNTSVPVS
     AVFMDKPEEF ISEMDMSCEV NECRKIESLE NLYLDFDDDV TELETFGVTT TKVSKSPSPA
     STSTVPNMTD APTAPKAGTT TVAPSAPDIS ANSRSLSQIL MEQLQKEKQL VTGMDGGPEE
     CKNKDDQGFE SCEKVSNSDK PLIQDSDLKT SDALQLENSQ EIETSNKNDM TIDILHADGE
     RPNVLENLDN SKEKTVGSEA AKTEDTVLCS SDTDEECLII DTECKNNSDG KTAVVGSNLS
     SRPASPNSSS GQASVGNQTN TACSPEESCV LKKPIKRVYK KFDPVGEILK MQDELLKPIS
     RKVPELPLMN LENSKQPSVS EQLSGPSDSS SWPKSGWPSA FQKPKGRLPY ELQDYVEDTS
     EYLAPQEGNF VYKLFSLQDL LLLVRCSVQR IETRPRSKKR KKIRRQFPVY VLPKVEYQAC
     YGVEALTESE LCRLWTESLL HSNSSFYVGH IDAFTSKLFL LEEITSEELK EKLSALKISN
     LFNILQHILK KLSSLQEGSY LLSHAAEDSS LLIYKASDGK VTRTAYNLYK THCGLPGVPS
     SLSVPWVPLD PSLLLPYHIH HGRIPCTFPP KSLDTTTQQK IGGTRMPTRS HRNPVSMETK
     SSCLPAQQVE TEGVAPHKRK IT
//