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RNA polymerase-associated protein CTR9 homolog (SH2 domain-binding protein 1) (Tetratricopeptide repeat-containing, SH2-binding phosphoprotein of 150 kDa) (TPR-containing, SH2-binding phosphoprotein of 150 kDa) (p150TSP)

 CTR9_MOUSE              Reviewed;        1173 AA.
Q62018; Q3UFF5; Q3UY40; Q66JX4; Q7TPS6; Q8BND9; Q8BRD1; Q8C9W7;
Q8C9Y3; Q8CHI1;
04-APR-2006, integrated into UniProtKB/Swiss-Prot.
04-APR-2006, sequence version 2.
28-MAR-2018, entry version 150.
RecName: Full=RNA polymerase-associated protein CTR9 homolog;
AltName: Full=SH2 domain-binding protein 1;
AltName: Full=Tetratricopeptide repeat-containing, SH2-binding phosphoprotein of 150 kDa;
Short=TPR-containing, SH2-binding phosphoprotein of 150 kDa;
Short=p150TSP;
Name=Ctr9; Synonyms=Kiaa0155, Sh2bp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
PHOSPHORYLATION.
TISSUE=Lymphoma;
PubMed=8636124; DOI=10.1074/jbc.271.12.6952;
Malek S.N., Yang C.H., Earnshaw W.C., Kozak C.A., Desiderio S.;
"p150TSP, a conserved nuclear phosphoprotein that contains multiple
tetratricopeptide repeats and binds specifically to SH2 domains.";
J. Biol. Chem. 271:6952-6962(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
SCALE MRNA] OF 1-955 (ISOFORM 1).
STRAIN=C57BL/6J;
TISSUE=Olfactory bulb, Pancreas, Spinal ganglion, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-936 (ISOFORM 1).
STRAIN=129, and C3H/He; TISSUE=Mammary tumor, and Osteoblast;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-1173 (ISOFORM 3), AND
TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=12465718; DOI=10.1093/dnares/9.5.179;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
I. The complete nucleotide sequences of 100 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 9:179-188(2002).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[6]
FUNCTION, AND INTERACTION WITH STAT3.
PubMed=17911113; DOI=10.1074/jbc.M705411200;
Youn M.Y., Yoo H.S., Kim M.J., Hwang S.Y., Choi Y., Desiderio S.V.,
Yoo J.Y.;
"hCTR9, a component of Paf1 complex, participates in the transcription
of interleukin 6-responsive genes through regulation of STAT3-DNA
interactions.";
J. Biol. Chem. 282:34727-34734(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
FUNCTION.
PubMed=19345177; DOI=10.1016/j.stem.2009.03.009;
Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M.,
Heninger A.K., de Vries I., Kittler R., Junqueira M., Shevchenko A.,
Schulz H., Hubner N., Doss M.X., Sachinidis A., Hescheler J.,
Iacone R., Anastassiadis K., Stewart A.F., Pisabarro M.T.,
Caldarelli A., Poser I., Theis M., Buchholz F.;
"A genome-scale RNAi screen for Oct4 modulators defines a role of the
Paf1 complex for embryonic stem cell identity.";
Cell Stem Cell 4:403-415(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-970;
SER-1037; SER-1039; SER-1041; SER-1079; SER-1083 AND SER-1085, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
INTERACTION WITH SETD5.
PubMed=27864380; DOI=10.1242/dev.141465;
Osipovich A.B., Gangula R., Vianna P.G., Magnuson M.A.;
"Setd5 is essential for mammalian development and the co-
transcriptional regulation of histone acetylation.";
Development 143:4595-4607(2016).
[12]
SUBUNIT.
PubMed=27749823; DOI=10.1038/ncb3424;
Strikoudis A., Lazaris C., Trimarchi T., Galvao Neto A.L., Yang Y.,
Ntziachristos P., Rothbart S., Buckley S., Dolgalev I., Stadtfeld M.,
Strahl B.D., Dynlacht B.D., Tsirigos A., Aifantis I.;
"Regulation of transcriptional elongation in pluripotency and cell
differentiation by the PHD-finger protein Phf5a.";
Nat. Cell Biol. 18:1127-1138(2016).
-!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
functions during transcription by RNA polymerase II and is
implicated in regulation of development and maintenance of
embryonic stem cell pluripotency. PAF1C associates with RNA
polymerase II through interaction with POLR2A CTD non-
phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and
is involved in transcriptional elongation, acting both
indepentently and synergistically with TCEA1 and in cooperation
with the DSIF complex and HTATSF1. PAF1C is required for
transcription of Hox and Wnt target genes. PAF1C is involved in
hematopoiesis and stimulates transcriptional activity of
KMT2A/MLL1. PAF1C is involved in histone modifications such as
ubiquitination of histone H2B and methylation on histone H3 'Lys-
4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein
ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which
mediate monoubiquitination of 'Lys-120' of histone H2B
(H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be
coupled to transcription. PAF1C is involved in mRNA 3' end
formation probably through association with cleavage and poly(A)
factors. Required for mono- and trimethylation on histone H3 'Lys-
4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3).
Required for Hox gene transcription (By similarity). Required for
the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes
involved in stem cell pluripotency; this function is synergistic
with CXXC1 indicative for an involvement of the SET1 complex.
Involved in transcriptional regulation of IL6-responsive genes and
in JAK-STAT pathway; may regulate DNA-association of STAT3.
{ECO:0000250, ECO:0000269|PubMed:17911113,
ECO:0000269|PubMed:19345177}.
-!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73,
PAF1, LEO1, CTR9, RTF1 and WDR61. The PAF1 complex interacts with
PHF5A (PubMed:27749823). Interacts with KMT2A/MLL1 (By
similarity). Interacts with STAT3 (PubMed:17911113). Interacts
with SETD5 (PubMed:27864380). {ECO:0000250|UniProtKB:Q6PD62,
ECO:0000269|PubMed:17911113, ECO:0000269|PubMed:27749823,
ECO:0000269|PubMed:27864380}.
-!- SUBCELLULAR LOCATION: Nucleus speckle
{ECO:0000269|PubMed:8636124}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q62018-1; Sequence=Displayed;
Name=2;
IsoId=Q62018-2; Sequence=VSP_017846, VSP_017847;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q62018-3; Sequence=VSP_017848, VSP_017849;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:12465718}.
-!- SEQUENCE CAUTION:
Sequence=AAH53910.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 937.; Evidence={ECO:0000305};
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EMBL; L49502; AAC42083.1; -; mRNA.
EMBL; AK040205; BAC30540.1; -; mRNA.
EMBL; AK040331; BAC30566.1; -; mRNA.
EMBL; AK045101; BAC32223.1; -; mRNA.
EMBL; AK083921; BAC39065.2; -; mRNA.
EMBL; AK134990; BAE22373.1; -; mRNA.
EMBL; AK148536; BAE28606.1; -; mRNA.
EMBL; BC053910; AAH53910.1; ALT_SEQ; mRNA.
EMBL; BC080719; AAH80719.1; -; mRNA.
EMBL; AB093211; BAC41395.1; -; Transcribed_RNA.
CCDS; CCDS21750.1; -. [Q62018-1]
PIR; T42719; T42719.
RefSeq; NP_033457.2; NM_009431.2. [Q62018-1]
UniGene; Mm.255858; -.
ProteinModelPortal; Q62018; -.
SMR; Q62018; -.
BioGrid; 204339; 9.
IntAct; Q62018; 5.
MINT; Q62018; -.
STRING; 10090.ENSMUSP00000005749; -.
iPTMnet; Q62018; -.
PhosphoSitePlus; Q62018; -.
EPD; Q62018; -.
PaxDb; Q62018; -.
PeptideAtlas; Q62018; -.
PRIDE; Q62018; -.
Ensembl; ENSMUST00000005749; ENSMUSP00000005749; ENSMUSG00000005609. [Q62018-1]
GeneID; 22083; -.
KEGG; mmu:22083; -.
UCSC; uc009jfw.1; mouse. [Q62018-2]
UCSC; uc009jfx.1; mouse. [Q62018-1]
CTD; 9646; -.
MGI; MGI:109345; Ctr9.
eggNOG; KOG2002; Eukaryota.
eggNOG; COG0457; LUCA.
GeneTree; ENSGT00390000005097; -.
HOVERGEN; HBG081372; -.
InParanoid; Q62018; -.
KO; K15176; -.
OMA; WLNLAHI; -.
OrthoDB; EOG091G01GC; -.
PhylomeDB; Q62018; -.
TreeFam; TF314342; -.
Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
ChiTaRS; Ctr9; mouse.
PRO; PR:Q62018; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000005609; -.
Genevisible; Q62018; MM.
GO; GO:0016593; C:Cdc73/Paf1 complex; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0035327; C:transcriptionally active chromatin; IDA:UniProtKB.
GO; GO:0000993; F:RNA polymerase II core binding; IBA:GO_Central.
GO; GO:0042169; F:SH2 domain binding; IDA:MGI.
GO; GO:0001832; P:blastocyst growth; IMP:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0001711; P:endodermal cell fate commitment; IMP:UniProtKB.
GO; GO:0033523; P:histone H2B ubiquitination; ISO:MGI.
GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
GO; GO:0010390; P:histone monoubiquitination; ISO:MGI.
GO; GO:0001826; P:inner cell mass cell differentiation; IMP:MGI.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0007259; P:JAK-STAT cascade; IMP:UniProtKB.
GO; GO:1900364; P:negative regulation of mRNA polyadenylation; ISO:MGI.
GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:2001168; P:positive regulation of histone H2B ubiquitination; ISO:MGI.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
GO; GO:2001162; P:positive regulation of histone H3-K79 methylation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:2000653; P:regulation of genetic imprinting; IMP:MGI.
GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0001829; P:trophectodermal cell differentiation; IMP:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 1.25.40.10; -; 3.
InterPro; IPR031101; Ctr9.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR019734; TPR_repeat.
PANTHER; PTHR14027; PTHR14027; 2.
Pfam; PF13181; TPR_8; 4.
SMART; SM00028; TPR; 10.
SUPFAM; SSF48452; SSF48452; 3.
PROSITE; PS50005; TPR; 10.
PROSITE; PS50293; TPR_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Nucleus; Phosphoprotein;
Reference proteome; Repeat; TPR repeat; Transcription;
Transcription regulation; Wnt signaling pathway.
CHAIN 1 1173 RNA polymerase-associated protein CTR9
homolog.
/FTId=PRO_0000231589.
REPEAT 41 75 TPR 1.
REPEAT 129 162 TPR 2.
REPEAT 163 196 TPR 3.
REPEAT 198 231 TPR 4.
REPEAT 235 268 TPR 5.
REPEAT 306 339 TPR 6.
REPEAT 341 374 TPR 7.
REPEAT 412 444 TPR 8.
REPEAT 451 484 TPR 9.
REPEAT 497 530 TPR 10.
REPEAT 531 564 TPR 11.
REPEAT 566 598 TPR 12.
REPEAT 613 646 TPR 13.
REPEAT 647 680 TPR 14.
REPEAT 681 714 TPR 15.
REPEAT 717 750 TPR 16.
COMPBIAS 904 908 Poly-Gly.
COMPBIAS 933 936 Poly-Lys.
COMPBIAS 944 951 Poly-Glu.
COMPBIAS 959 962 Poly-Arg.
COMPBIAS 971 976 Poly-Glu.
COMPBIAS 1015 1172 Ser-rich.
MOD_RES 925 925 Phosphothreonine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 932 932 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PD62}.
MOD_RES 941 941 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 943 943 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PD62}.
MOD_RES 970 970 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1020 1020 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PD62}.
MOD_RES 1021 1021 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PD62}.
MOD_RES 1037 1037 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1039 1039 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1041 1041 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1079 1079 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1083 1083 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1085 1085 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1095 1095 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PD62}.
MOD_RES 1100 1100 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PD62}.
VAR_SEQ 704 721 YENCLRKFYKHQNTEVVL -> VTSLLLRIVACNVEPWLP
(in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_017846.
VAR_SEQ 722 1173 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_017847.
VAR_SEQ 816 860 Missing (in isoform 3).
{ECO:0000303|PubMed:12465718}.
/FTId=VSP_017848.
VAR_SEQ 995 1032 Missing (in isoform 3).
{ECO:0000303|PubMed:12465718}.
/FTId=VSP_017849.
CONFLICT 144 144 K -> Q (in Ref. 1; AAC42083).
{ECO:0000305}.
CONFLICT 223 223 R -> S (in Ref. 3; AAH53910).
{ECO:0000305}.
CONFLICT 242 242 E -> Q (in Ref. 2; BAC32223).
{ECO:0000305}.
CONFLICT 390 390 D -> Y (in Ref. 3; AAH53910).
{ECO:0000305}.
CONFLICT 719 719 V -> I (in Ref. 2; BAE22373).
{ECO:0000305}.
CONFLICT 877 877 Q -> R (in Ref. 3; AAH80719).
{ECO:0000305}.
CONFLICT 900 900 E -> K (in Ref. 3; AAH80719).
{ECO:0000305}.
SEQUENCE 1173 AA; 133408 MW; 2FB84564F1BEFD79 CRC64;
MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YYKQGKTEEF
VKLLEAARID GNLDYRDHEK DQMTCLDTLA AYYVQQARKE KNKDNKKDLI TQATLLYTMA
DKIIMYDQNH LLGRACFCLL EGDKMDQADA QFHFVLNQSP NNIPALLGKA CISFNKKDYR
GALAYYKKAL RTNPGCPAEV RLGMGHCFVK LNKLEKARLA FSRALELNSK CVGALVGLAV
LELNNKEADS IKNGVQLLSR AYTIDPSNPM VLNHLANHFF FKKDYSKVQH LALHAFHNTE
VEAMQAESCY QLARSFHVQE DYDQAFQYYY QATQFASSSF VLPFFGLGQM YIYRGDKENA
SQCFEKVLKA YPNNYETMKI LGSLYAASED QEKRDIAKGH LKKVTEQYPD DVEAWIELAQ
ILEQTDIQGA LSAYGTATRI LQEKVQADVP PEILNNVGAL HFRLGNLGEA KKYFLASLDR
AKAEAEHDEH YYNAISVTTS YNLARLYEAM CEFHEAEKLY KNILREHPNY VDCYLRLGAM
ARDKGNFYEA SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPATQSD
TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDAKNLYAA NGIGAVLAHK
GYFREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA VQMYENCLRK FYKHQNTEVV
LYLARALFKC GKLQECKQTL LKARHVAPSD TVLMFNVALV LQRLATSVLK DEKSNLKEVL
NAVKELELAH RYFSYLSKVG DKMRFDLALA ASEARQCSDL LSQAQYHVAR ARKQDEEERE
LRAKQEQEKE LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNILM FTGETEATKE
KKRGGGGGRR SKKGGEFDEF VNDDTDDDLP VSKKKKRRKG SGSEQEGEEE EGGERKKKRR
RRPPKGEEGS EEEETENGPK PKKRRPPRAE KKKAPKPERL PPSMKGKIKS KAIISSSDDS
SDEDKLKIAD EGHPRNSNSD SDDDERPNRR ASSESDSDDN QNKSGSEAGS PRRSGRQESD
EDSDSDQPSR KRRRSGSEQS DNESVQSGRS PSGASENEND SRPASPSAES DHESEQGSDN
EGSGQGSGNE SEPEGSNNEA SDRGSEHGSD DSD


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