CASC3_MOUSE
ID CASC3_MOUSE Reviewed; 698 AA.
AC Q8K3W3; A3KFP7; Q3UT99; Q8K219; Q99NF0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Protein CASC3;
DE AltName: Full=Cancer susceptibility candidate gene 3 protein homolog;
DE AltName: Full=Metastatic lymph node gene 51 protein homolog;
DE Short=MLN 51 homolog;
DE AltName: Full=Protein barentsz {ECO:0000303|PubMed:12843282};
DE Short=Btz {ECO:0000303|PubMed:12843282};
DE Short=mBtz {ECO:0000303|PubMed:12843282};
GN Name=Casc3; Synonyms=Mln51;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12080473; DOI=10.1038/sj.onc.1205611;
RA Degot S.F., Regnier C.H., Wendling C., Chenard M.-P., Rio M.-C.,
RA Tomasetto C.L.;
RT "Metastatic lymph node 51, a novel nucleo-cytoplasmic protein overexpressed
RT in breast cancer.";
RL Oncogene 21:4422-4434(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH STAU1, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-464.
RC STRAIN=BALB/cJ;
RX PubMed=12843282; DOI=10.1523/jneurosci.23-13-05778.2003;
RA Macchi P., Kroening S., Palacios I.M., Baldassa S., Grunewald B.,
RA Ambrosino C., Goetze B., Lupas A., St Johnston D., Kiebler M.;
RT "Barentsz, a new component of the Staufen-containing ribonucleoprotein
RT particles in mammalian cells, interacts with Staufen in an RNA-dependent
RT manner.";
RL J. Neurosci. 23:5778-5788(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 40-697.
RC STRAIN=Czech II, and FVB/N; TISSUE=Brain, Kidney, and Mammary tumor;
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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-145 AND SER-263, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome. Core component of the splicing-dependent multiprotein exon
CC junction complex (EJC) deposited at splice junctions on mRNAs. The EJC
CC is a dynamic structure consisting of core proteins and several
CC peripheral nuclear and cytoplasmic associated factors that join the
CC complex only transiently either during EJC assembly or during
CC subsequent mRNA metabolism. The EJC marks the position of the exon-exon
CC junction in the mature mRNA for the gene expression machinery and the
CC core components remain bound to spliced mRNAs throughout all stages of
CC mRNA metabolism thereby influencing downstream processes including
CC nuclear mRNA export, subcellular mRNA localization, translation
CC efficiency and nonsense-mediated mRNA decay (NMD). Stimulates the
CC ATPase and RNA-helicase activities of EIF4A3. Plays a role in the
CC stress response by participating in cytoplasmic stress granules
CC assembly and by favoring cell recovery following stress. Component of
CC the dendritic ribonucleoprotein particles (RNPs) in hippocampal
CC neurons. May play a role in mRNA transport. Binds spliced mRNA in
CC sequence-independent manner, 20-24 nucleotides upstream of mRNA exon-
CC exon junctions. Binds poly(G) and poly(U) RNA homomer.
CC {ECO:0000250|UniProtKB:O15234}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Component of the mRNA
CC splicing-dependent exon junction complex (EJC), which contains at least
CC CASC3, EIF4A3, MAGOH, NXF1 and RBM8A/Y14. Identified in a complex
CC composed of the EJC core, UPF3B and UPF2. The EJC core can also
CC interact with UPF3A (in vitro) (By similarity). Forms homooligomers (By
CC similarity). Interacts with STAU in an RNA-dependent manner
CC (PubMed:12843282). Interacts with DHX34; the interaction is RNA-
CC independent (By similarity). {ECO:0000250|UniProtKB:O15234,
CC ECO:0000250|UniProtKB:Q8K3X0, ECO:0000269|PubMed:12843282}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12843282}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:12843282}. Nucleus
CC {ECO:0000269|PubMed:12843282}. Nucleus speckle
CC {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:O15234}. Cytoplasm, Cytoplasmic
CC ribonucleoprotein granule {ECO:0000269|PubMed:12843282}. Cell
CC projection, dendrite {ECO:0000269|PubMed:12843282}. Note=Shuttles
CC between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner
CC (PubMed:12843282). Transported to the cytoplasm as part of the exon
CC junction complex (EJC) bound to mRNA. In nuclear speckles, colocalizes
CC with MAGOH. Under stress conditions, colocalizes with FMR1 and TIA1,
CC but not MAGOH and RBM8A EJC core factors, in cytoplasmic stress
CC granules (By similarity). In the dendrites of hippocampal neurons,
CC localizes to dendritic ribonucleoprotein granules (Probable).
CC {ECO:0000250|UniProtKB:O15234, ECO:0000269|PubMed:12843282,
CC ECO:0000305|PubMed:12843282}.
CC -!- TISSUE SPECIFICITY: High levels in heart, brain, including hippocampus
CC and cerebellum, liver, kidney and testis; lower levels in muscle, lung
CC and spleen. {ECO:0000269|PubMed:12843282}.
CC -!- DOMAIN: The coiled coil domain may be involved in oligomerization.
CC {ECO:0000250}.
CC -!- PTM: ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated
CC protein is recognized by RNF146, followed by ubiquitination (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its
CC degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CASC3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH60672.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF526276; AAM88396.1; -; mRNA.
DR EMBL; AJ292072; CAC27775.1; -; mRNA.
DR EMBL; AK139608; BAE24081.1; -; mRNA.
DR EMBL; AL590963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL16170.1; -; Genomic_DNA.
DR EMBL; BC034533; AAH34533.1; -; mRNA.
DR EMBL; BC060672; AAH60672.1; ALT_INIT; mRNA.
DR EMBL; BC141296; AAI41297.1; -; mRNA.
DR CCDS; CCDS36302.1; -.
DR RefSeq; NP_619601.2; NM_138660.2.
DR AlphaFoldDB; Q8K3W3; -.
DR BioGRID; 228651; 6.
DR ComplexPortal; CPX-635; Exon junction core complex, Magoh variant.
DR ComplexPortal; CPX-683; Exon junction core complex, Magohb variant.
DR IntAct; Q8K3W3; 1.
DR STRING; 10090.ENSMUSP00000017384; -.
DR iPTMnet; Q8K3W3; -.
DR PhosphoSitePlus; Q8K3W3; -.
DR EPD; Q8K3W3; -.
DR jPOST; Q8K3W3; -.
DR MaxQB; Q8K3W3; -.
DR PaxDb; Q8K3W3; -.
DR PeptideAtlas; Q8K3W3; -.
DR PRIDE; Q8K3W3; -.
DR ProteomicsDB; 265533; -.
DR Antibodypedia; 16438; 290 antibodies from 29 providers.
DR Ensembl; ENSMUST00000017384; ENSMUSP00000017384; ENSMUSG00000078676.
DR Ensembl; ENSMUST00000169695; ENSMUSP00000130926; ENSMUSG00000078676.
DR GeneID; 192160; -.
DR KEGG; mmu:192160; -.
DR UCSC; uc007lhq.1; mouse.
DR CTD; 22794; -.
DR MGI; MGI:2179723; Casc3.
DR VEuPathDB; HostDB:ENSMUSG00000078676; -.
DR eggNOG; KOG4264; Eukaryota.
DR GeneTree; ENSGT00390000006930; -.
DR HOGENOM; CLU_018976_0_0_1; -.
DR InParanoid; Q8K3W3; -.
DR OMA; MIQDPHM; -.
DR OrthoDB; 486761at2759; -.
DR PhylomeDB; Q8K3W3; -.
DR TreeFam; TF329663; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR BioGRID-ORCS; 192160; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Casc3; mouse.
DR PRO; PR:Q8K3W3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K3W3; protein.
DR Bgee; ENSMUSG00000078676; Expressed in embryonic post-anal tail and 242 other tissues.
DR Genevisible; Q8K3W3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0035145; C:exon-exon junction complex; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0008298; P:intracellular mRNA localization; IDA:MGI.
DR GO; GO:0006406; P:mRNA export from nucleus; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:2000622; P:regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISO:MGI.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR018545; Btz_dom.
DR InterPro; IPR028544; CASC3.
DR PANTHER; PTHR13434; PTHR13434; 1.
DR Pfam; PF09405; Btz; 1.
DR SMART; SM01044; Btz; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Cell projection; Coiled coil; Cytoplasm; mRNA processing;
KW mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Spliceosome;
KW Stress response; Translation regulation; Transport; Ubl conjugation.
FT CHAIN 1..698
FT /note="Protein CASC3"
FT /id="PRO_0000089325"
FT REGION 1..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..280
FT /note="Necessary for RNA-binding, interaction with MAGOH
FT and localization in nucleus speckles"
FT /evidence="ECO:0000250"
FT REGION 134..280
FT /note="Sufficient to form the EJC"
FT /evidence="ECO:0000250"
FT REGION 241..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..698
FT /note="Necessary for localization in cytoplasmic stress
FT granules"
FT /evidence="ECO:0000250"
FT REGION 488..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 629..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 98..127
FT /evidence="ECO:0000255"
FT MOTIF 201..207
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255"
FT MOTIF 251..259
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255"
FT MOTIF 457..466
FT /note="Nuclear export signal"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..610
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..649
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..689
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 354
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15234"
FT MUTAGEN 464
FT /note="L->A: Accumulation in the nucleus."
FT /evidence="ECO:0000269|PubMed:12843282"
FT CONFLICT 297
FT /note="N -> D (in Ref. 3; BAE24081)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="S -> G (in Ref. 6; AAH34533)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="L -> V (in Ref. 3; BAE24081)"
FT /evidence="ECO:0000305"
FT CONFLICT 638
FT /note="Missing (in Ref. 2; CAC27775 and 6; AAH60672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 698 AA; 75770 MW; 3B718FC297A5E0F3 CRC64;
MADRRRQRAS QDTEDEESGA SGSDSGSPAR GGGSCSGSVG GGGSGSLPSQ RGGRGGGLHL
RRVESGGAKS AEESECESED GMEGDAVLSD YESAEDSEGE EDYSEEENSK VELKSEANDA
ADSSAKEKGE EKPESKGTVT GERQSGDGQE STEPVENKVG KKGPKHLDDD EDRKNPAYIP
RKGLFFEHDL RGQTQEEEVR PKGRQRKLWK DEGRWEHDKF REDEQAPKSR QELIALYGYD
IRSAHNPDDI KPRRIRKPRF GSSPQRDPNW IGDRSSKSHR HQGPGGNLPP RTFINRNTAG
TGRMSASRNY SRSGGFKDGR TSFRPVEVAG QHGGRSAETL KHEASYRSRR LEQTPVRDPS
PEPDAPLLGS PEKEEVASET PAAVPDITPP APDRPIEKKS YSRARRTRTK VGDAVKAAEE
VPPPSEGLAS TATVPETTPA AKTGNWEAPV DSTTGGLEQD VAQLNIAEQS WSPSQPSFLQ
PRELRGVPNH IHMGAGPPPQ FNRMEEMGVQ SGRAKRYSSQ RQRPVPEPPA PPVHISIMEG
HYYDPLQFQG PIYTHGDSPA PLPPQGMIVQ PEMHLPHPGL HPHQSPGPLP NPGLYPPPVS
MSPGQPPPQQ LLAPTYFSAP GVMNFGNPNY PYAPGALPPP PPPHLYPNTQ APPQVYGGVT
YYNPAQQQVQ PKPSPPRRTP QPVSIKPPPP EVVSRGSS
