SNPC4_HUMAN
ID SNPC4_HUMAN Reviewed; 1469 AA.
AC Q5SXM2; Q9Y6P7;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=snRNA-activating protein complex subunit 4;
DE Short=SNAPc subunit 4;
DE AltName: Full=Proximal sequence element-binding transcription factor subunit alpha;
DE Short=PSE-binding factor subunit alpha;
DE Short=PTF subunit alpha;
DE AltName: Full=snRNA-activating protein complex 190 kDa subunit;
DE Short=SNAPc 190 kDa subunit;
GN Name=SNAPC4 {ECO:0000312|EMBL:CAI13935.1, ECO:0000312|HGNC:HGNC:11137};
GN Synonyms=SNAP190 {ECO:0000312|EMBL:AAC02972.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAC02972.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH SNAPC2.
RC TISSUE=Teratocarcinoma {ECO:0000312|EMBL:AAC02972.1};
RX PubMed=9418884; DOI=10.1128/mcb.18.1.368;
RA Wong M.W., Henry R.W., Ma B., Kobayashi R., Klages N., Matthias P.,
RA Strubin M., Hernandez N.;
RT "The large subunit of basal transcription factor SNAPc is a Myb domain
RT protein that interacts with Oct-1.";
RL Mol. Cell. Biol. 18:368-377(1998).
RN [2] {ECO:0000312|EMBL:CAI13935.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3] {ECO:0000305}
RP INTERACTION WITH SNAPC1; SNAPC2 AND SNAPC5, AND MUTAGENESIS OF GLN-94;
RP GLN-115; LEU-1314; LEU-1355; LEU-1362; LEU-1364 AND LEU-1369.
RX PubMed=11056176; DOI=10.1074/jbc.m009301200;
RA Ma B., Hernandez N.;
RT "A map of protein-protein contacts within the small nuclear RNA-activating
RT protein complex SNAPc.";
RL J. Biol. Chem. 276:5027-5035(2001).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH TBP AND BRF2.
RX PubMed=12621023; DOI=10.1074/jbc.m204247200;
RA Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W.;
RT "The small nuclear RNA-activating protein 190 Myb DNA binding domain
RT stimulates TATA box-binding protein-TATA box recognition.";
RL J. Biol. Chem. 278:18649-18657(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1157, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1398 AND SER-1400, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-599; SER-626 AND
RP SER-1224, AND IDENTIFICATION BY 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).
CC -!- FUNCTION: Part of the SNAPc complex required for the transcription of
CC both RNA polymerase II and III small-nuclear RNA genes. Binds to the
CC proximal sequence element (PSE), a non-TATA-box basal promoter element
CC common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA
CC TATA box. {ECO:0000269|PubMed:12621023, ECO:0000269|PubMed:9418884}.
CC -!- SUBUNIT: Part of the SNAPc complex composed of 5 subunits: SNAPC1,
CC SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC4 interacts with SNAPC1,
CC SNAPC2, SNAPC5, BRF2 and TBP. {ECO:0000269|PubMed:11056176,
CC ECO:0000269|PubMed:12621023, ECO:0000269|PubMed:9418884}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF032387; AAC02972.1; -; mRNA.
DR EMBL; AL592301; CAI13935.1; -; Genomic_DNA.
DR CCDS; CCDS6998.1; -.
DR PIR; T09219; T09219.
DR RefSeq; NP_003077.2; NM_003086.3.
DR RefSeq; XP_005266153.1; XM_005266096.2.
DR RefSeq; XP_006717304.1; XM_006717241.2.
DR RefSeq; XP_006717305.1; XM_006717242.3.
DR AlphaFoldDB; Q5SXM2; -.
DR SMR; Q5SXM2; -.
DR BioGRID; 112505; 72.
DR CORUM; Q5SXM2; -.
DR IntAct; Q5SXM2; 23.
DR MINT; Q5SXM2; -.
DR STRING; 9606.ENSP00000298532; -.
DR GlyGen; Q5SXM2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5SXM2; -.
DR PhosphoSitePlus; Q5SXM2; -.
DR BioMuta; SNAPC4; -.
DR DMDM; 74762223; -.
DR EPD; Q5SXM2; -.
DR jPOST; Q5SXM2; -.
DR MassIVE; Q5SXM2; -.
DR MaxQB; Q5SXM2; -.
DR PaxDb; Q5SXM2; -.
DR PeptideAtlas; Q5SXM2; -.
DR PRIDE; Q5SXM2; -.
DR ProteomicsDB; 63996; -.
DR Antibodypedia; 18701; 195 antibodies from 20 providers.
DR DNASU; 6621; -.
DR Ensembl; ENST00000298532.2; ENSP00000298532.2; ENSG00000165684.6.
DR Ensembl; ENST00000637388.2; ENSP00000490037.2; ENSG00000165684.6.
DR Ensembl; ENST00000684778.1; ENSP00000510559.1; ENSG00000165684.6.
DR GeneID; 6621; -.
DR KEGG; hsa:6621; -.
DR MANE-Select; ENST00000684778.1; ENSP00000510559.1; NM_003086.4; NP_003077.2.
DR UCSC; uc004chh.4; human.
DR CTD; 6621; -.
DR DisGeNET; 6621; -.
DR GeneCards; SNAPC4; -.
DR HGNC; HGNC:11137; SNAPC4.
DR HPA; ENSG00000165684; Low tissue specificity.
DR MIM; 602777; gene.
DR neXtProt; NX_Q5SXM2; -.
DR OpenTargets; ENSG00000165684; -.
DR PharmGKB; PA35985; -.
DR VEuPathDB; HostDB:ENSG00000165684; -.
DR eggNOG; KOG0049; Eukaryota.
DR GeneTree; ENSGT00940000160404; -.
DR HOGENOM; CLU_004641_0_0_1; -.
DR InParanoid; Q5SXM2; -.
DR OMA; LWHGTFQ; -.
DR OrthoDB; 219341at2759; -.
DR PhylomeDB; Q5SXM2; -.
DR TreeFam; TF313064; -.
DR PathwayCommons; Q5SXM2; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR SignaLink; Q5SXM2; -.
DR BioGRID-ORCS; 6621; 706 hits in 1101 CRISPR screens.
DR ChiTaRS; SNAPC4; human.
DR GeneWiki; SNAPC4; -.
DR GenomeRNAi; 6621; -.
DR Pharos; Q5SXM2; Tbio.
DR PRO; PR:Q5SXM2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5SXM2; protein.
DR Bgee; ENSG00000165684; Expressed in sural nerve and 161 other tissues.
DR ExpressionAtlas; Q5SXM2; baseline and differential.
DR Genevisible; Q5SXM2; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019185; C:snRNA-activating protein complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-UCL.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:ARUK-UCL.
DR GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0042796; P:snRNA transcription by RNA polymerase III; IDA:UniProtKB.
DR CDD; cd00167; SANT; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR SMART; SM00717; SANT; 5.
DR SUPFAM; SSF46689; SSF46689; 3.
DR PROSITE; PS51294; HTH_MYB; 3.
DR PROSITE; PS50090; MYB_LIKE; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..1469
FT /note="snRNA-activating protein complex subunit 4"
FT /id="PRO_0000197120"
FT DOMAIN 250..288
FT /note="Myb-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DOMAIN 289..343
FT /note="HTH myb-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 344..395
FT /note="Myb-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT DOMAIN 396..451
FT /note="HTH myb-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DOMAIN 452..503
FT /note="HTH myb-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 317..341
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 424..447
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 476..499
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 16..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..133
FT /note="SNAPC5-binding"
FT /evidence="ECO:0000269|PubMed:11056176"
FT REGION 501..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1281..1393
FT /note="SNAPC2-binding"
FT /evidence="ECO:0000269|PubMed:11056176"
FT REGION 1430..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..516
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1157
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 1224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BP86"
FT VARIANT 44
FT /note="D -> N (in dbSNP:rs7031489)"
FT /id="VAR_059455"
FT VARIANT 799
FT /note="H -> Q (in dbSNP:rs3812571)"
FT /id="VAR_050193"
FT VARIANT 1448
FT /note="P -> S (in dbSNP:rs3812561)"
FT /id="VAR_050194"
FT MUTAGEN 94
FT /note="Q->A: Abolishes SNAPC5 binding in the absence of
FT SNAPC1. Minimal effect on SNAPC5 binding in the presence of
FT SNAPC1."
FT /evidence="ECO:0000269|PubMed:11056176"
FT MUTAGEN 94
FT /note="Q->L: Abolishes SNAPC5 binding in the absence of
FT SNAPC1. Minimal effect on SNAPC5 binding in the presence of
FT SNAPC1."
FT /evidence="ECO:0000269|PubMed:11056176"
FT MUTAGEN 115
FT /note="Q->L: Abolishes SNAPC5 binding in the absence of
FT SNAPC1. Minimal effect on SNAPC5 binding in the presence of
FT SNAPC1."
FT /evidence="ECO:0000269|PubMed:11056176"
FT MUTAGEN 1314
FT /note="L->A: Abolishes SNAPC2-binding."
FT /evidence="ECO:0000269|PubMed:11056176"
FT MUTAGEN 1355
FT /note="L->A: Abolishes SNAPC2-binding."
FT /evidence="ECO:0000269|PubMed:11056176"
FT MUTAGEN 1362
FT /note="L->A: Abolishes SNAPC2-binding."
FT /evidence="ECO:0000269|PubMed:11056176"
FT MUTAGEN 1364
FT /note="L->A: Abolishes SNAPC2-binding."
FT /evidence="ECO:0000269|PubMed:11056176"
FT MUTAGEN 1369
FT /note="L->A: Decreased binding to SNAPC2."
FT /evidence="ECO:0000269|PubMed:11056176"
FT CONFLICT 1046
FT /note="A -> G (in Ref. 1; AAC02972)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1469 AA; 159433 MW; 78CBCFB1887E106C CRC64;
MDVDAEREKI TQEIKELERI LDPGSSGSHV EISESSLESD SEADSLPSED LDPADPPISE
EERWGEASND EDDPKDKTLP EDPETCLQLN MVYQEVIQEK LAEANLLLAQ NREQQEELMR
DLAGSKGTKV KDGKSLPPST YMGHFMKPYF KDKVTGVGPP ANEDTREKAA QGIKAFEELL
VTKWKNWEKA LLRKSVVSDR LQRLLQPKLL KLEYLHQKQS KVSSELERQA LEKQGREAEK
EIQDINQLPE EALLGNRLDS HDWEKISNIN FEGSRSAEEI RKFWQNSEHP SINKQEWSRE
EEERLQAIAA AHGHLEWQKI AEELGTSRSA FQCLQKFQQH NKALKRKEWT EEEDRMLTQL
VQEMRVGSHI PYRRIVYYME GRDSMQLIYR WTKSLDPGLK KGYWAPEEDA KLLQAVAKYG
EQDWFKIREE VPGRSDAQCR DRYLRRLHFS LKKGRWNLKE EEQLIELIEK YGVGHWAKIA
SELPHRSGSQ CLSKWKIMMG KKQGLRRRRR RARHSVRWSS TSSSGSSSGS SGGSSSSSSS
SSEEDEPEQA QAGEGDRALL SPQYMVPDMD LWVPARQSTS QPWRGGAGAW LGGPAASLSP
PKGSSASQGG SKEASTTAAA PGEETSPVQV PARAHGPVPR SAQASHSADT RPAGAEKQAL
EGGRRLLTVP VETVLRVLRA NTAARSCTQK EQLRQPPLPT SSPGVSSGDS VARSHVQWLR
HRATQSGQRR WRHALHRRLL NRRLLLAVTP WVGDVVVPCT QASQRPAVVQ TQADGLREQL
QQARLASTPV FTLFTQLFHI DTAGCLEVVR ERKALPPRLP QAGARDPPVH LLQASSSAQS
TPGHLFPNVP AQEASKSASH KGSRRLASSR VERTLPQASL LASTGPRPKP KTVSELLQEK
RLQEARAREA TRGPVVLPSQ LLVSSSVILQ PPLPHTPHGR PAPGPTVLNV PLSGPGAPAA
AKPGTSGSWQ EAGTSAKDKR LSTMQALPLA PVFSEAEGTA PAASQAPALG PGQISVSCPE
SGLGQSQAPA ASRKQGLPEA PPFLPAAPSP TPLPVQPLSL THIGGPHVAT SVPLPVTWVL
TAQGLLPVPV PAVVSLPRPA GTPGPAGLLA TLLPPLTETR AAQGPRAPAL SSSWQPPANM
NREPEPSCRT DTPAPPTHAL SQSPAEADGS VAFVPGEAQV AREIPEPRTS SHADPPEAEP
PWSGRLPAFG GVIPATEPRG TPGSPSGTQE PRGPLGLEKL PLRQPGPEKG ALDLEKPPLP
QPGPEKGALD LGLLSQEGEA ATQQWLGGQR GVRVPLLGSR LPYQPPALCS LRALSGLLLH
KKALEHKATS LVVGGEAERP AGALQASLGL VRGQLQDNPA YLLLRARFLA AFTLPALLAT
LAPQGVRTTL SVPSRVGSES EDEDLLSELE LADRDGQPGC TTATCPIQGA PDSGKCSASS
CLDTSNDPDD LDVLRTRHAR HTRKRRRLV
