RPRD2_MOUSE
ID RPRD2_MOUSE Reviewed; 1469 AA.
AC Q6NXI6; Q3U3L8; Q6ZQA7;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Regulation of nuclear pre-mRNA domain-containing protein 2;
GN Name=Rprd2; Synonyms=Kiaa0460;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-491 (ISOFORM 2).
RC STRAIN=NOD; TISSUE=Dendritic cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-1469 (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-738 AND THR-742, AND
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-633; SER-738;
RP SER-777 AND SER-1086, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-612; SER-738;
RP THR-742; SER-749 AND THR-751, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1432 AND ARG-1438, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- SUBUNIT: Associates with the RNA polymerase II complex. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6NXI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NXI6-2; Sequence=VSP_019548;
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DR EMBL; BC067054; AAH67054.1; -; mRNA.
DR EMBL; AK129150; BAC97960.1; -; mRNA.
DR EMBL; AK154692; BAE32767.1; -; mRNA.
DR CCDS; CCDS38549.1; -. [Q6NXI6-1]
DR RefSeq; NP_001074762.1; NM_001081293.1. [Q6NXI6-1]
DR RefSeq; XP_006502291.1; XM_006502228.3.
DR AlphaFoldDB; Q6NXI6; -.
DR SMR; Q6NXI6; -.
DR STRING; 10090.ENSMUSP00000088297; -.
DR iPTMnet; Q6NXI6; -.
DR PhosphoSitePlus; Q6NXI6; -.
DR EPD; Q6NXI6; -.
DR jPOST; Q6NXI6; -.
DR MaxQB; Q6NXI6; -.
DR PaxDb; Q6NXI6; -.
DR PeptideAtlas; Q6NXI6; -.
DR PRIDE; Q6NXI6; -.
DR ProteomicsDB; 299948; -. [Q6NXI6-1]
DR ProteomicsDB; 299949; -. [Q6NXI6-2]
DR Antibodypedia; 10548; 64 antibodies from 17 providers.
DR Ensembl; ENSMUST00000090791; ENSMUSP00000088297; ENSMUSG00000028106. [Q6NXI6-1]
DR GeneID; 75137; -.
DR KEGG; mmu:75137; -.
DR UCSC; uc008qkx.1; mouse. [Q6NXI6-1]
DR UCSC; uc008qky.1; mouse. [Q6NXI6-2]
DR CTD; 23248; -.
DR MGI; MGI:1922387; Rprd2.
DR VEuPathDB; HostDB:ENSMUSG00000028106; -.
DR eggNOG; KOG2669; Eukaryota.
DR GeneTree; ENSGT00950000183094; -.
DR HOGENOM; CLU_004610_0_0_1; -.
DR InParanoid; Q6NXI6; -.
DR OMA; NYSHRAQ; -.
DR OrthoDB; 1091009at2759; -.
DR PhylomeDB; Q6NXI6; -.
DR TreeFam; TF320926; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 75137; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Rprd2; mouse.
DR PRO; PR:Q6NXI6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6NXI6; protein.
DR Bgee; ENSMUSG00000028106; Expressed in secondary oocyte and 232 other tissues.
DR ExpressionAtlas; Q6NXI6; baseline and differential.
DR Genevisible; Q6NXI6; MM.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR GO; GO:0031124; P:mRNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR006569; CID_dom.
DR InterPro; IPR032337; CREPT.
DR InterPro; IPR008942; ENTH_VHS.
DR Pfam; PF04818; CID; 1.
DR Pfam; PF16566; CREPT; 1.
DR SMART; SM00582; RPR; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS51391; CID; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Methylation; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT CHAIN 2..1469
FT /note="Regulation of nuclear pre-mRNA domain-containing
FT protein 2"
FT /id="PRO_0000244356"
FT DOMAIN 19..149
FT /note="CID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00724"
FT REGION 329..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 942..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1298
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1328
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 536
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 617
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 742
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 751
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 984
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 1086
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 1375
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q5VT52"
FT MOD_RES 1432
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1438
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 146..189
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_019548"
FT CONFLICT 491
FT /note="V -> K (in Ref. 2; BAC97960)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="S -> N (in Ref. 3; BAE32767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1469 AA; 156586 MW; 1EF4A65F32873748 CRC64;
MAAGGGGGSS KASSSSASSA GALESSLDRK FQSVTNTMES IQGLSSWCIE NKKHHSTIVY
HWMKWLRRST YPHRLNLFYL ANDVIQNCKR KNAIIFRESF ADVLPEAAAL VKDPSVSKSI
ERIFKIWEDR NVYPEDMIVA LREALMDRAA SHNARLQKLQ CFPGTTFKTQ KQLKENLNKQ
PNKQWKKSQT STNPKAALKS KIVAEFRSQA LIEELLMYKR SEDQIELKEK QLSTMRVDVC
STETLKCLKD KTGGKKFSKE FEEASSKLEE FVNGLDKQVK NGPSLTEALE NAGIFYEAQY
KEVKVVANAY KTFANRVNNL KKKLDQLKST LPDPEESPVP SPSMDAPSPT GSESPFQGMG
GEEPQSPAME SDKSATPEPV TDNRDVEDME LSDVEDDGSK IIVEDRKEKP VEKPAVSTGV
PTKSTESVSK ASPCAPPSVP TTAAPPLPKP LSTALLSPSP TLVLPNLANV DLAKISSILS
SLTSVMKNTG VSSASRPSPG IPTSPSNLSS GLKTPAPATT PSHNPLANIL SKVEITPESI
LSALSKTQTQ SAPALQGLSS LLQSVTANPV PASEVTSQST TASPASTTGS AVKGRNLLSS
TQSFIPKSFN YSPSSSTSEV SSTSASKASV GQSPVLPSTT FKLPSSSLGF TGTHNPSPAA
PPTEVAVCQS SEVSKPKPES ESTSPSLEMK IHNFLKGNPG FSGLNLNIPI LSSLGSSAPS
EGHASDFQRG PTSTSVDSID GTPVRDERSG TPTQDEMMDK PTSSSVDTMS LLSKIISPGS
STPSSTRSPP PGRDESYPQE LPNSVSTYRP FGLGSDSPYK QPSGGVERPS SLMDSSQEKL
FPDTSFQEDE DYRDFEYSGP PPSAMMNLEK KPAKSILKSS KLSDATEYQP ILSSYNHRAQ
EFGVKSAFPP SVRALLDSSE NCDRLSSPPG LFGAFNIRGN EPGSERSPSP SKNDAFFTPD
SNHSGLSQST AGHLTLPQTQ YPDSPHSVPH RSIFSSQSTL AAPAGHPPTS GVEKVLASTI
STTSTIEFKN MLKNASRKPS DDKHFGQTPN KGTSSDGVSL SNLTQPSLPT TDQQQEEHYR
IETRVSSSCL DLPDSTEEKG APIETLGYHN AANRRMSGEP IKTVESIRVP GKGNRGHGRE
VSRVGWFDLS TPGSSFDNGP SSASELASLG GGGSGGLTGF KTTPYKERAP QFQESVTSFR
SNSFNSTFEH HLPPSPLEHG APFQREPVGP SSAPPAPPKD HGGIFSREAP THLPSVDLSN
PFTKEASLAH AGPPPPPGEH SGVPFPPPPP PPPPGELSSG GTGVPFATPA PPPPPVDHSG
VVPFPTPPLP EHGVTGAVSV FPKDHSSLLQ GTMAEHFGVL TGPRDLNGPG LNRSRESLSL
PSHPLEHLGP ALGGGGGGNT SSSGLPLSPA HRDAIGRSGM ILRSPRPDFR PREAFLGRDP
FHSLKRPRPP FVRGPPFFAP KRPFFPPRY
