U2AFM_HUMAN
ID U2AFM_HUMAN Reviewed; 482 AA.
AC Q15696; Q14D69;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2;
DE AltName: Full=CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 2;
DE AltName: Full=Renal carcinoma antigen NY-REN-20;
DE AltName: Full=U2(RNU2) small nuclear RNA auxiliary factor 1-like 2;
DE AltName: Full=U2AF35-related protein;
DE Short=URP;
GN Name=ZRSR2; Synonyms=U2AF1-RS2, U2AF1L2, U2AF1RS2, URP;
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].
RC TISSUE=Brain;
RX PubMed=8586425; DOI=10.1006/geno.1995.9879;
RA Kitagawa K., Wang X., Hatada I., Yamaoka T., Nojima H., Inazawa J., Abe T.,
RA Mitsuya K., Oshimura M., Murata A., Monden M., Mukai T.;
RT "Isolation and mapping of human homologues of an imprinted mouse gene
RT U2af1-rs1.";
RL Genomics 30:257-263(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND INTERACTION WITH SRSF1;
RP SRSF2; SRPK1 AND U2AF2.
RX PubMed=9237760; DOI=10.1038/41137;
RA Tronchere H., Wang J., Fu X.D.;
RT "A protein related to splicing factor U2AF35 that interacts with U2AF65 and
RT SR proteins in splicing of pre-mRNA.";
RL Nature 388:397-400(1997).
RN [5]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [6]
RP IDENTIFICATION IN THE U11/U12 SPLICEOSOME COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15146077; DOI=10.1261/rna.7320604;
RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S.,
RA Tuschl T., Luehrmann R.;
RT "The human 18S U11/U12 snRNP contains a set of novel proteins not found in
RT the U2-dependent spliceosome.";
RL RNA 10:929-941(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP 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 FUNCTION, IDENTIFICATION IN THE U11/U12 SPLICEOSOME COMPLEX, AND
RP RNA-BINDING.
RX PubMed=21041408; DOI=10.1101/gad.1974810;
RA Shen H., Zheng X., Luecke S., Green M.R.;
RT "The U2AF35-related protein Urp contacts the 3' splice site to promote U12-
RT type intron splicing and the second step of U2-type intron splicing.";
RL Genes Dev. 24:2389-2394(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND IDENTIFICATION BY
RP 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-45 AND LYS-62, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Pre-mRNA-binding protein required for splicing of both
CC U2- and U12-type introns. Selectively interacts with the 3'-splice site
CC of U2- and U12-type pre-mRNAs and promotes different steps in U2 and
CC U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP-dependent
CC manner and is required for assembly of the prespliceosome, a precursor
CC to other spliceosomal complexes. For U2-type introns, it is selectively
CC and specifically required for the second step of splicing.
CC {ECO:0000269|PubMed:21041408, ECO:0000269|PubMed:9237760}.
CC -!- SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-type
CC spliceosome. Interacts (via RS domain) with SRSF1 and SRSF2. Interacts
CC with U2AF2/U2AF65. {ECO:0000269|PubMed:15146077,
CC ECO:0000269|PubMed:21041408, ECO:0000269|PubMed:9237760}.
CC -!- INTERACTION:
CC Q15696; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-6657923, EBI-2836773;
CC Q15696; P49760: CLK2; NbExp=8; IntAct=EBI-6657923, EBI-750020;
CC Q15696; Q92997: DVL3; NbExp=3; IntAct=EBI-6657923, EBI-739789;
CC Q15696; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-6657923, EBI-9089060;
CC Q15696; Q9Y383: LUC7L2; NbExp=3; IntAct=EBI-6657923, EBI-352851;
CC Q15696; Q6BDI9: REP15; NbExp=3; IntAct=EBI-6657923, EBI-12048237;
CC Q15696; Q9H190: SDCBP2; NbExp=7; IntAct=EBI-6657923, EBI-742426;
CC Q15696; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-6657923, EBI-539478;
CC Q15696; P78362: SRPK2; NbExp=7; IntAct=EBI-6657923, EBI-593303;
CC Q15696; A7MD48: SRRM4; NbExp=3; IntAct=EBI-6657923, EBI-3867173;
CC Q15696; Q13243: SRSF5; NbExp=3; IntAct=EBI-6657923, EBI-720503;
CC Q15696; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-6657923, EBI-2212028;
CC Q15696; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-6657923, EBI-11139477;
CC Q15696; Q8WVP5: TNFAIP8L1; NbExp=3; IntAct=EBI-6657923, EBI-752102;
CC Q15696; Q15696: ZRSR2; NbExp=3; IntAct=EBI-6657923, EBI-6657923;
CC Q15696; Q15695: ZRSR2P1; NbExp=4; IntAct=EBI-6657923, EBI-12270264;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15146077}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9237760}.
CC -!- PTM: Phosphorylated in the RS domain by SRPK1.
CC {ECO:0000269|PubMed:9237760}.
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DR EMBL; D49677; BAA08533.1; -; mRNA.
DR EMBL; AC004106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC113454; AAI13455.1; -; mRNA.
DR EMBL; BC113480; AAI13481.1; -; mRNA.
DR CCDS; CCDS14172.1; -.
DR RefSeq; NP_005080.1; NM_005089.3.
DR AlphaFoldDB; Q15696; -.
DR SMR; Q15696; -.
DR BioGRID; 113865; 73.
DR CORUM; Q15696; -.
DR DIP; DIP-62117N; -.
DR IntAct; Q15696; 51.
DR STRING; 9606.ENSP00000303015; -.
DR iPTMnet; Q15696; -.
DR PhosphoSitePlus; Q15696; -.
DR BioMuta; ZRSR2; -.
DR DMDM; 2833266; -.
DR EPD; Q15696; -.
DR jPOST; Q15696; -.
DR MassIVE; Q15696; -.
DR MaxQB; Q15696; -.
DR PaxDb; Q15696; -.
DR PeptideAtlas; Q15696; -.
DR PRIDE; Q15696; -.
DR ProteomicsDB; 60704; -.
DR Antibodypedia; 8950; 110 antibodies from 22 providers.
DR DNASU; 8233; -.
DR Ensembl; ENST00000307771.8; ENSP00000303015.7; ENSG00000169249.14.
DR GeneID; 8233; -.
DR KEGG; hsa:8233; -.
DR MANE-Select; ENST00000307771.8; ENSP00000303015.7; NM_005089.4; NP_005080.1.
DR UCSC; uc004cxg.5; human.
DR CTD; 8233; -.
DR DisGeNET; 8233; -.
DR GeneCards; ZRSR2; -.
DR HGNC; HGNC:23019; ZRSR2.
DR HPA; ENSG00000169249; Low tissue specificity.
DR MIM; 300028; gene.
DR neXtProt; NX_Q15696; -.
DR OpenTargets; ENSG00000169249; -.
DR PharmGKB; PA162410930; -.
DR VEuPathDB; HostDB:ENSG00000169249; -.
DR eggNOG; KOG2202; Eukaryota.
DR GeneTree; ENSGT00950000183152; -.
DR HOGENOM; CLU_029117_1_0_1; -.
DR InParanoid; Q15696; -.
DR OMA; MDLRIME; -.
DR OrthoDB; 1340384at2759; -.
DR PhylomeDB; Q15696; -.
DR TreeFam; TF324447; -.
DR PathwayCommons; Q15696; -.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; Q15696; -.
DR SIGNOR; Q15696; -.
DR BioGRID-ORCS; 8233; 185 hits in 715 CRISPR screens.
DR ChiTaRS; ZRSR2; human.
DR GeneWiki; ZRSR2; -.
DR GenomeRNAi; 8233; -.
DR Pharos; Q15696; Tbio.
DR PRO; PR:Q15696; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q15696; protein.
DR Bgee; ENSG00000169249; Expressed in sural nerve and 206 other tissues.
DR ExpressionAtlas; Q15696; baseline and differential.
DR Genevisible; Q15696; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0089701; C:U2AF complex; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IC:HGNC-UCL.
DR GO; GO:0000245; P:spliceosomal complex assembly; IMP:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR009145; U2AF_small.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR12620; PTHR12620; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR PRINTS; PR01848; U2AUXFACTOR.
DR SMART; SM00361; RRM_1; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Isopeptide bond; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
KW Spliceosome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..482
FT /note="U2 small nuclear ribonucleoprotein auxiliary factor
FT 35 kDa subunit-related protein 2"
FT /id="PRO_0000082001"
FT DOMAIN 198..304
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 166..194
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 306..333
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..420
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..469
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 45
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 62
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 482 AA; 58045 MW; 1DACC8A6CA4727A6 CRC64;
MAAPEKMTFP EKPSHKKYRA ALKKEKRKKR RQELARLRDS GLSQKEEEED TFIEEQQLEE
EKLLERERQR LHEEWLLREQ KAQEEFRIKK EKEEAAKKRQ EEQERKLKEQ WEEQQRKERE
EEEQKRQEKK EKEEALQKML DQAENELENG TTWQNPEPPV DFRVMEKDRA NCPFYSKTGA
CRFGDRCSRK HNFPTSSPTL LIKSMFTTFG MEQCRRDDYD PDASLEYSEE ETYQQFLDFY
EDVLPEFKNV GKVIQFKVSC NLEPHLRGNV YVQYQSEEEC QAALSLFNGR WYAGRQLQCE
FCPVTRWKMA ICGLFEIQQC PRGKHCNFLH VFRNPNNEFW EANRDIYLSP DRTGSSFGKN
SERRERMGHH DDYYSRLRGR RNPSPDHSYK RNGESERKSS RHRGKKSHKR TSKSRERHNS
RSRGRNRDRS RDRSRGRGSR SRSRSRSRRS RRSRSQSSSR SRSRGRRRSG NRDRTVQSPK
SK
