RUSC2_HUMAN
ID RUSC2_HUMAN Reviewed; 1516 AA.
AC Q8N2Y8; A2RU62; A7E2A9; O15080; Q5W134; Q641Q6; Q6P1W7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=AP-4 complex accessory subunit RUSC2 {ECO:0000305};
DE AltName: Full=Interacting protein of Rab1 {ECO:0000303|PubMed:15796781};
DE Short=Iporin {ECO:0000303|PubMed:15796781};
DE AltName: Full=RUN and SH3 domain-containing protein 2;
GN Name=RUSC2 {ECO:0000303|PubMed:27612186, ECO:0000312|HGNC:HGNC:23625};
GN Synonyms=KIAA0375 {ECO:0000303|PubMed:9205841};
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 [LARGE SCALE MRNA], AND VARIANT ALA-73.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-73.
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-73.
RC TISSUE=PNS, and Skin;
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 [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH RAB1A; RAB1B
RP AND GOLGA2.
RX PubMed=15796781; DOI=10.1186/1471-2121-6-15;
RA Bayer M., Fischer J., Kremerskothen J., Ossendorf E., Matanis T.,
RA Konczal M., Weide T., Barnekow A.;
RT "Identification and characterization of Iporin as a novel interaction
RT partner for rab1.";
RL BMC Cell Biol. 6:15-15(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536; SER-656; SER-1368 AND
RP SER-1380, AND 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536; SER-543; SER-559 AND
RP SER-781, 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).
RN [10]
RP INVOLVEMENT IN MRT61, AND VARIANTS MRT61 866-ARG--ASN-1516 DEL AND
RP 1318-ARG--ASN-1516 DEL.
RX PubMed=27612186; DOI=10.1111/dmcn.13250;
RA Alwadei A.H., Benini R., Mahmoud A., Alasmari A., Kamsteeg E.J.,
RA Alfadhel M.;
RT "Loss-of-function mutation in RUSC2 causes intellectual disability and
RT secondary microcephaly.";
RL Dev. Med. Child. Neurol. 58:1317-1322(2016).
RN [11]
RP FUNCTION, AND IDENTIFICATION IN THE AP-4 COMPLEX.
RX PubMed=30262884; DOI=10.1038/s41467-018-06172-7;
RA Davies A.K., Itzhak D.N., Edgar J.R., Archuleta T.L., Hirst J.,
RA Jackson L.P., Robinson M.S., Borner G.H.H.;
RT "AP-4 vesicles contribute to spatial control of autophagy via RUSC-
RT dependent peripheral delivery of ATG9A.";
RL Nat. Commun. 9:3958-3958(2018).
CC -!- FUNCTION: Associates with the adapter-like complex 4 (AP-4) and may
CC therefore play a role in vesicular trafficking of proteins at the
CC trans-Golgi network. {ECO:0000269|PubMed:30262884}.
CC -!- SUBUNIT: Associated component of the adapter-like complex 4 (AP-4)
CC (PubMed:30262884). Interacts with active RAB1A and RAB1B, and with
CC GOLGA2. {ECO:0000269|PubMed:15796781, ECO:0000269|PubMed:30262884}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15796781}.
CC Note=Cytosolic punctate distribution. Also observed in the perinuclear
CC region. {ECO:0000269|PubMed:15796781}.
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in brain and
CC testis. {ECO:0000269|PubMed:15796781}.
CC -!- DOMAIN: The RUN domain is required for the interaction with RAB1A and
CC RAB1B. {ECO:0000269|PubMed:15796781}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 61
CC (MRT61) [MIM:617773]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRT61
CC patients manifest delayed psychomotor development, moderate to severe
CC intellectual disability, and variable dysmorphic facial features.
CC Refractory seizures and brain abnormalities are present in severely
CC affected patients. {ECO:0000269|PubMed:27612186}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20830.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB002373; BAA20830.2; ALT_INIT; mRNA.
DR EMBL; AL133476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58377.1; -; Genomic_DNA.
DR EMBL; BC029647; AAH29647.1; -; mRNA.
DR EMBL; BC064843; AAH64843.1; -; mRNA.
DR EMBL; BC082245; AAH82245.1; -; mRNA.
DR EMBL; BC132766; AAI32767.1; -; mRNA.
DR EMBL; BC132770; AAI32771.1; -; mRNA.
DR EMBL; BC146654; AAI46655.1; -; mRNA.
DR EMBL; BC150262; AAI50263.1; -; mRNA.
DR CCDS; CCDS35008.1; -.
DR RefSeq; NP_001129471.1; NM_001135999.1.
DR RefSeq; NP_055621.1; NM_014806.4.
DR PDB; 6IF2; X-ray; 2.40 A; A=983-1181.
DR PDBsum; 6IF2; -.
DR AlphaFoldDB; Q8N2Y8; -.
DR SMR; Q8N2Y8; -.
DR BioGRID; 115187; 26.
DR ELM; Q8N2Y8; -.
DR IntAct; Q8N2Y8; 31.
DR MINT; Q8N2Y8; -.
DR STRING; 9606.ENSP00000393922; -.
DR iPTMnet; Q8N2Y8; -.
DR PhosphoSitePlus; Q8N2Y8; -.
DR BioMuta; RUSC2; -.
DR DMDM; 317373513; -.
DR EPD; Q8N2Y8; -.
DR jPOST; Q8N2Y8; -.
DR MassIVE; Q8N2Y8; -.
DR MaxQB; Q8N2Y8; -.
DR PaxDb; Q8N2Y8; -.
DR PeptideAtlas; Q8N2Y8; -.
DR PRIDE; Q8N2Y8; -.
DR ProteomicsDB; 71741; -.
DR Antibodypedia; 11549; 138 antibodies from 22 providers.
DR DNASU; 9853; -.
DR Ensembl; ENST00000361226.8; ENSP00000355177.3; ENSG00000198853.12.
DR Ensembl; ENST00000455600.1; ENSP00000393922.1; ENSG00000198853.12.
DR GeneID; 9853; -.
DR KEGG; hsa:9853; -.
DR MANE-Select; ENST00000361226.8; ENSP00000355177.3; NM_014806.5; NP_055621.2.
DR UCSC; uc003zww.4; human.
DR CTD; 9853; -.
DR DisGeNET; 9853; -.
DR GeneCards; RUSC2; -.
DR HGNC; HGNC:23625; RUSC2.
DR HPA; ENSG00000198853; Low tissue specificity.
DR MalaCards; RUSC2; -.
DR MIM; 611053; gene.
DR MIM; 617773; phenotype.
DR neXtProt; NX_Q8N2Y8; -.
DR OpenTargets; ENSG00000198853; -.
DR PharmGKB; PA134956488; -.
DR VEuPathDB; HostDB:ENSG00000198853; -.
DR eggNOG; ENOG502QR1I; Eukaryota.
DR GeneTree; ENSGT00900000141033; -.
DR HOGENOM; CLU_004141_0_0_1; -.
DR InParanoid; Q8N2Y8; -.
DR OMA; TSHFHCK; -.
DR OrthoDB; 373320at2759; -.
DR PhylomeDB; Q8N2Y8; -.
DR TreeFam; TF332235; -.
DR PathwayCommons; Q8N2Y8; -.
DR SignaLink; Q8N2Y8; -.
DR BioGRID-ORCS; 9853; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; RUSC2; human.
DR GenomeRNAi; 9853; -.
DR Pharos; Q8N2Y8; Tbio.
DR PRO; PR:Q8N2Y8; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8N2Y8; protein.
DR Bgee; ENSG00000198853; Expressed in cortical plate and 161 other tissues.
DR Genevisible; Q8N2Y8; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR Gene3D; 1.20.58.900; -; 1.
DR InterPro; IPR004012; Run_dom.
DR InterPro; IPR037213; Run_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF02759; RUN; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00593; RUN; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50826; RUN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; Intellectual disability;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..1516
FT /note="AP-4 complex accessory subunit RUSC2"
FT /id="PRO_0000097534"
FT DOMAIN 1031..1175
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 1447..1506
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 33..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1422..1449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1251
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 73
FT /note="T -> A (in dbSNP:rs1535422)"
FT /evidence="ECO:0000269|PubMed:15164053,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9205841"
FT /id="VAR_034653"
FT VARIANT 654
FT /note="P -> L (in dbSNP:rs3750427)"
FT /id="VAR_034654"
FT VARIANT 866..1516
FT /note="Missing (in MRT61; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27612186"
FT /id="VAR_080461"
FT VARIANT 1318..1516
FT /note="Missing (in MRT61; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27612186"
FT /id="VAR_080462"
FT HELIX 990..1010
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1017..1023
FT /evidence="ECO:0007829|PDB:6IF2"
FT TURN 1026..1028
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1030..1038
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1040..1049
FT /evidence="ECO:0007829|PDB:6IF2"
FT STRAND 1054..1058
FT /evidence="ECO:0007829|PDB:6IF2"
FT TURN 1059..1061
FT /evidence="ECO:0007829|PDB:6IF2"
FT STRAND 1062..1065
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1068..1074
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1083..1094
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1101..1114
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1118..1126
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1129..1135
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1141..1147
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1150..1160
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1161..1165
FT /evidence="ECO:0007829|PDB:6IF2"
FT HELIX 1174..1177
FT /evidence="ECO:0007829|PDB:6IF2"
SQ SEQUENCE 1516 AA; 161225 MW; E96E1180A1E18CF8 CRC64;
MDSPPKLTGE TLIVHHIPLV HCQVPDRQCC GGAGGGGGST RPNPFCPPEL GITQPDQDLG
QADSLLFSSL HSTPGGTARS IDSTKSRSRD GRGPGAPKRH NPFLLQEGVG EPGLGDLYDD
SIGDSATQQS FHLHGTGQPN FHLSSFQLPP SGPRVGRPWG TTRSRAGVVE GQEQEPVMTL
DTQQCGTSHC CRPELEAETM ELDECGGPGG SGSGGGASDT SGFSFDQEWK LSSDESPRNP
GCSGSGDQHC RCSSTSSQSE AADQSMGYVS DSSCNSSDGV LVTFSTLYNK MHGTPRANLN
SAPQSCSDSS FCSHSDPGAF YLDLQPSPFE SKMSYESHHP ESGGREGGYG CPHASSPELD
ANCNSYRPHC EPCPAVADLT ACFQSQARLV VATQNYYKLV TCDLSSQSSP SPAGSSITSC
SEEHTKISPP PGPGPDPGPS QPSEYYLFQK PEVQPEEQEA VSSSTQAAAA VGPTVLEGQV
YTNTSPPNLS TGRQRSRSYD RSLQRSPPVR LGSLERMLSC PVRLSEGPAA MAGPGSPPRR
VTSFAELAKG RKKTGGSGSP PLRVSVGDSS QEFSPIQEAQ QDRGAPLDEG TCCSHSLPPM
PLGPGMDLLG PDPSPPWSTQ VCQGPHSSEM PPAGLRATGQ GPLAQLMDPG PALPGSPANS
HTQRDARARA DGGGTESRPV LRYSKEQRPT TLPIQPFVFQ HHFPKQLAKA RALHSLSQLY
SLSGCSRTQQ PAPLAAPAAQ VSVPAPSGEP QASTPRATGR GARKAGSEPE TSRPSPLGSY
SPIRSVGPFG PSTDSSASTS CSPPPEQPTA TESLPPWSHS CPSAVRPATS QQPQKEDQKI
LTLTEYRLHG TGSLPPLGSW RSGLSRAESL ARGGGEGSMA TRPSNANHLS PQALKWREYR
RKNPLGPPGL SGSLDRRSQE ARLARRNPIF EFPGSLSAAS HLNCRLNGQA VKPLPLTCPD
FQDPFSLTEK PPAEFCLSPD GSSEAISIDL LQKKGLVKAV NIAVDLIVAH FGTSRDPGVK
AKLGNSSVSP NVGHLVLKYL CPAVRAVLED GLKAFVLDVI IGQRKNMPWS VVEASTQLGP
STKVLHGLYN KVSQFPELTS HTMRFNAFIL GLLNIRSLEF WFNHLYNHED IIQTHYQPWG
FLSAAHTVCP GLFEELLLLL QPLALLPFSL DLLFQHRLLQ SGQQQRQHKE LLRVSQDLLL
SAHSTLQLAR ARGQEGPGDV DRAAQGERVK GVGASEGGEE EEEEEETEEV AEAAGGSGRA
RWARGGQAGW WYQLMQSSQV YIDGSIEGSR FPRGSSNSSS EKKKGAGGGG PPQAPPPREG
VVEGAEACPA SEEALGRERG WPFWMGSPPD SVLAELRRSR EREGPAASPA ENEEGASEPS
PGGIKWGHLF GSRKAQREAR PTNRLPSDWL SLDKSMFQLV AQTVGSRREP EPKESLQEPH
SPALPSSPPC EVQALCHHLA TGPGQLSFHK GDILRVLGRA GGDWLRCSRG PDSGLVPLAY
VTLTPTPSPT PGSSQN
