RALY_MOUSE
ID RALY_MOUSE Reviewed; 312 AA.
AC Q64012; A2AU63; Q99K76; Q9CXH8; Q9QZX6;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=RNA-binding protein Raly;
DE AltName: Full=Maternally-expressed hnRNP C-related protein;
DE AltName: Full=hnRNP associated with lethal yellow protein;
GN Name=Raly; Synonyms=Merc;
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] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND INVOLVEMENT IN A(Y).
RC TISSUE=Embryo;
RX PubMed=8319910; DOI=10.1101/gad.7.7a.1203;
RA Michaud E.J., Bultman S.J., Stubbs L.J., Woychik R.P.;
RT "The embryonic lethality of homozygous lethal yellow mice (Ay/Ay) is
RT associated with the disruption of a novel RNA-binding protein.";
RL Genes Dev. 7:1203-1213(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN A(Y).
RX PubMed=8050375; DOI=10.1242/dev.120.6.1695;
RA Duhl D.M., Stevens M.E., Vrieling H., Saxon P.J., Miller M.W.,
RA Epstein C.J., Barsh G.S.;
RT "Pleiotropic effects of the mouse lethal yellow (Ay) mutation explained by
RT deletion of a maternally expressed gene and the simultaneous production of
RT agouti fusion RNAs.";
RL Development 120:1695-1708(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
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 MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 100-135 (ISOFORM 2).
RX PubMed=10500250; DOI=10.1016/s0167-4781(99)00126-8;
RA Khrebtukova I., Kuklin A., Woychik R.P., Michaud E.J.;
RT "Alternative processing of the human and mouse raly genes.";
RL Biochim. Biophys. Acta 1447:107-112(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268; SER-270; THR-274;
RP THR-292 AND THR-304, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 THR-274, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; THR-268; SER-270 AND
RP THR-274, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268; SER-270; THR-274;
RP THR-292; SER-294; SER-301 AND THR-304, AND IDENTIFICATION BY MASS
RP 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).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44 AND LYS-165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=27251289; DOI=10.1038/nature17674;
RA Sallam T., Jones M.C., Gilliland T., Zhang L., Wu X., Eskin A., Sandhu J.,
RA Casero D., Vallim T.Q., Hong C., Katz M., Lee R., Whitelegge J.,
RA Tontonoz P.;
RT "Feedback modulation of cholesterol metabolism by the lipid-responsive non-
RT coding RNA LeXis.";
RL Nature 534:124-128(2016).
CC -!- FUNCTION: RNA-binding protein that acts as a transcriptional cofactor
CC for cholesterol biosynthetic genes in the liver (PubMed:27251289).
CC Binds the lipid-responsive non-coding RNA LeXis and is required for
CC LeXis-mediated effect on cholesterogenesis (PubMed:27251289). May be a
CC heterogeneous nuclear ribonucleoprotein (hnRNP) (By similarity).
CC {ECO:0000250|UniProtKB:Q9UKM9, ECO:0000269|PubMed:27251289}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts (through
CC its RNA-binding domain) with FUS (through its RNA-binding domain); both
CC are components of the same RNPs. {ECO:0000250|UniProtKB:Q9UKM9}.
CC -!- INTERACTION:
CC Q64012; Q61545: Ewsr1; NbExp=2; IntAct=EBI-6878379, EBI-1606991;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27251289}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q64012-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q64012-2; Sequence=VSP_005805;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, testis, lung,
CC spleen and kidney. Weakly expressed in liver.
CC {ECO:0000269|PubMed:8319910}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the unfertilized egg, in the
CC blastocyst, as well as in the developing embryo and fetus. Expressed in
CC developing skin. {ECO:0000269|PubMed:8319910}.
CC -!- DISEASE: Note=Defects in Raly are the cause of lethal yellow mutation
CC (A(y)), a dominant allele that cause embryonic lethality when
CC homozygous, and pleiotropic effects when heterozygous, including yellow
CC pelage, obesity, non-insulin dependent diabetes and increased tumor
CC susceptibility. A(y) is due to a 170 kb deletion that removes all but
CC the promoter and non-coding first exon of Raly and links them to the
CC ASIP/Agouti gene. {ECO:0000269|PubMed:8050375,
CC ECO:0000269|PubMed:8319910}.
CC -!- SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily.
CC {ECO:0000305}.
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DR EMBL; S72641; AAC60688.1; -; mRNA.
DR EMBL; L17076; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK014356; BAB29294.1; -; mRNA.
DR EMBL; AL929024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004851; AAH04851.1; -; mRNA.
DR EMBL; BC016587; AAH16587.1; -; mRNA.
DR EMBL; AF148458; AAF04488.1; -; mRNA.
DR CCDS; CCDS16939.1; -. [Q64012-2]
DR CCDS; CCDS50767.1; -. [Q64012-1]
DR PIR; I53142; I53142.
DR RefSeq; NP_001132983.1; NM_001139511.1. [Q64012-2]
DR RefSeq; NP_001132984.1; NM_001139512.1. [Q64012-2]
DR RefSeq; NP_001132985.1; NM_001139513.1. [Q64012-1]
DR RefSeq; NP_075619.2; NM_023130.3. [Q64012-2]
DR RefSeq; XP_006499076.1; XM_006499013.3. [Q64012-1]
DR RefSeq; XP_006499077.1; XM_006499014.3. [Q64012-1]
DR RefSeq; XP_006499078.1; XM_006499015.2. [Q64012-1]
DR RefSeq; XP_006499079.1; XM_006499016.2. [Q64012-2]
DR RefSeq; XP_017172120.1; XM_017316631.1. [Q64012-2]
DR AlphaFoldDB; Q64012; -.
DR SMR; Q64012; -.
DR BioGRID; 202579; 8.
DR IntAct; Q64012; 8.
DR MINT; Q64012; -.
DR STRING; 10090.ENSMUSP00000058105; -.
DR iPTMnet; Q64012; -.
DR PhosphoSitePlus; Q64012; -.
DR EPD; Q64012; -.
DR jPOST; Q64012; -.
DR MaxQB; Q64012; -.
DR PaxDb; Q64012; -.
DR PeptideAtlas; Q64012; -.
DR PRIDE; Q64012; -.
DR ProteomicsDB; 300349; -. [Q64012-1]
DR ProteomicsDB; 300350; -. [Q64012-2]
DR Antibodypedia; 10794; 252 antibodies from 30 providers.
DR DNASU; 19383; -.
DR Ensembl; ENSMUST00000029120; ENSMUSP00000029120; ENSMUSG00000027593. [Q64012-1]
DR Ensembl; ENSMUST00000058089; ENSMUSP00000058105; ENSMUSG00000027593. [Q64012-2]
DR Ensembl; ENSMUST00000109701; ENSMUSP00000105323; ENSMUSG00000027593. [Q64012-2]
DR Ensembl; ENSMUST00000116389; ENSMUSP00000112090; ENSMUSG00000027593. [Q64012-1]
DR GeneID; 19383; -.
DR KEGG; mmu:19383; -.
DR UCSC; uc008njv.2; mouse. [Q64012-1]
DR CTD; 22913; -.
DR MGI; MGI:97850; Raly.
DR VEuPathDB; HostDB:ENSMUSG00000027593; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000157601; -.
DR InParanoid; Q64012; -.
DR OMA; MEEQRQN; -.
DR OrthoDB; 1182824at2759; -.
DR PhylomeDB; Q64012; -.
DR TreeFam; TF330974; -.
DR BioGRID-ORCS; 19383; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Raly; mouse.
DR PRO; PR:Q64012; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q64012; protein.
DR Bgee; ENSMUSG00000027593; Expressed in floor plate of midbrain and 265 other tissues.
DR ExpressionAtlas; Q64012; baseline and differential.
DR Genevisible; Q64012; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IMP:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1903506; P:regulation of nucleic acid-templated transcription; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd12604; RRM_RALY; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR017347; hnRNP_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034502; RALY_RRM.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037992; hnRNP-C_Raly; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UKM9"
FT CHAIN 2..312
FT /note="RNA-binding protein Raly"
FT /id="PRO_0000081747"
FT DOMAIN 21..92
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 214..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..216
FT /evidence="ECO:0000255"
FT COMPBIAS 229..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKM9"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 165
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 268
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKM9"
FT CROSSLNK 94
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKM9"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKM9"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKM9"
FT CROSSLNK 165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKM9"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKM9"
FT CROSSLNK 191
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UKM9"
FT VAR_SEQ 110..125
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:8050375,
FT ECO:0000303|PubMed:8319910"
FT /id="VSP_005805"
FT CONFLICT 249
FT /note="S -> G (in Ref. 1; AAC60688 and 5; AAH04851/
FT AAH16587)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="T -> I (in Ref. 1; AAC60688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 312 AA; 33188 MW; A2A8FD35476BFC44 CRC64;
MSLKIQTSNV TNKNDPKSIN SRVFIGNLNT AVVKKSDVET IFSKYGRVAG CSVHKGYAFV
QYANERHARA AVLGENGRVL AGQTLDINMA GEPKPNRPKG LKRAATAIYS GYSFDYDYYQ
DYFCARLFDY RGRLSPVPVP RAVPVKRPRV TVPLVRRVKT TIPVKLFARS TAVTTGSAKI
KLKSSELQTI KTELTQIKSN IDALLGRLEQ IAEEQKANPD GKKKGDSSSG GGGGSSGGGG
SSNVGGGSSG GSGSCSSSSR LPAPQEDTAS EAGTPQGEVQ TRDDGDEEGL LTHSEEELEH
SQDTDAEDGA LQ
