PRCC_HUMAN
ID PRCC_HUMAN Reviewed; 491 AA.
AC Q92733; A8K1F7; O00665; O00724; Q5SZ06;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Proline-rich protein PRCC;
DE AltName: Full=Papillary renal cell carcinoma translocation-associated gene protein;
GN Name=PRCC; Synonyms=TPRC;
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], AND CHROMOSOMAL TRANSLOCATION WITH TFE3.
RC TISSUE=Monocyte;
RX PubMed=8872474; DOI=10.1093/hmg/5.9.1333;
RA Sidhar S.K., Clark J., Gill S., Hamoudi R., Crew A.J., Gwilliam R.,
RA Ross M., Linehan W.M., Birdsall S., Shipley J., Cooper C.S.;
RT "The t(X;1)(p11.2;q21.2) translocation in papillary renal cell carcinoma
RT fuses a novel gene PRCC to the TFE3 transcription factor gene.";
RL Hum. Mol. Genet. 5:1333-1338(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHROMOSOMAL TRANSLOCATION WITH TFE3.
RX PubMed=8986805; DOI=10.1073/pnas.93.26.15294;
RA Weterman M.A.J., Wilbrink M., Geurts van Kessel A.;
RT "Fusion of the transcription factor TFE3 gene to a novel gene, PRCC, in
RT t(X;1)(p11;q21)-positive papillary renal cell carcinomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:15294-15298(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-136.
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [7]
RP FUNCTION, INTERACTION WITH MAD2L2, AND SUBCELLULAR LOCATION.
RX PubMed=11717438; DOI=10.1073/pnas.241304198;
RA Weterman M.A., van Groningen J.J., Tertoolen L., van Kessel A.G.;
RT "Impairment of MAD2B-PRCC interaction in mitotic checkpoint defective
RT t(X;1)-positive renal cell carcinomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13808-13813(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159 AND SER-267, AND
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-114; SER-157;
RP SER-159; SER-212; THR-239 AND SER-241, AND IDENTIFICATION BY MASS
RP 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND SER-159, AND
RP IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159 AND SER-241, AND
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-157 AND SER-159, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May regulate cell cycle progression through interaction with
CC MAD2L2. {ECO:0000269|PubMed:11717438}.
CC -!- SUBUNIT: Interacts with MAD2L2; the interaction is direct.
CC {ECO:0000269|PubMed:11717438}.
CC -!- INTERACTION:
CC Q92733; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-4397741, EBI-748420;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11717438}.
CC -!- TISSUE SPECIFICITY: Ubiquitous in fetal and adult tissues.
CC -!- DISEASE: Note=A chromosomal aberration involving PRCC is found in
CC patients with papillary renal cell carcinoma. Translocation
CC t(X;1)(p11.2;q21.2) with TFE3. {ECO:0000269|PubMed:8872474,
CC ECO:0000269|PubMed:8986805}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PRCCID69.html";
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DR EMBL; X97124; CAA65791.1; -; mRNA.
DR EMBL; X99720; CAA68060.1; -; Genomic_DNA.
DR EMBL; AK289872; BAF82561.1; -; mRNA.
DR EMBL; AL590666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52909.1; -; Genomic_DNA.
DR EMBL; BC004913; AAH04913.1; -; mRNA.
DR CCDS; CCDS1157.1; -.
DR RefSeq; NP_005964.3; NM_005973.4.
DR AlphaFoldDB; Q92733; -.
DR SMR; Q92733; -.
DR BioGRID; 111537; 87.
DR IntAct; Q92733; 38.
DR MINT; Q92733; -.
DR STRING; 9606.ENSP00000271526; -.
DR GlyGen; Q92733; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92733; -.
DR PhosphoSitePlus; Q92733; -.
DR BioMuta; PRCC; -.
DR DMDM; 2498802; -.
DR EPD; Q92733; -.
DR jPOST; Q92733; -.
DR MassIVE; Q92733; -.
DR MaxQB; Q92733; -.
DR PaxDb; Q92733; -.
DR PeptideAtlas; Q92733; -.
DR PRIDE; Q92733; -.
DR ProteomicsDB; 75429; -.
DR Antibodypedia; 4485; 83 antibodies from 19 providers.
DR DNASU; 5546; -.
DR Ensembl; ENST00000271526.9; ENSP00000271526.4; ENSG00000143294.15.
DR GeneID; 5546; -.
DR KEGG; hsa:5546; -.
DR MANE-Select; ENST00000271526.9; ENSP00000271526.4; NM_005973.5; NP_005964.3.
DR UCSC; uc001fqa.4; human.
DR CTD; 5546; -.
DR DisGeNET; 5546; -.
DR GeneCards; PRCC; -.
DR HGNC; HGNC:9343; PRCC.
DR HPA; ENSG00000143294; Low tissue specificity.
DR MalaCards; PRCC; -.
DR MIM; 179755; gene.
DR neXtProt; NX_Q92733; -.
DR OpenTargets; ENSG00000143294; -.
DR Orphanet; 319308; MiT family translocation renal cell carcinoma.
DR PharmGKB; PA33704; -.
DR VEuPathDB; HostDB:ENSG00000143294; -.
DR eggNOG; KOG3903; Eukaryota.
DR GeneTree; ENSGT00390000009042; -.
DR HOGENOM; CLU_032704_0_0_1; -.
DR InParanoid; Q92733; -.
DR OMA; WAPKPGE; -.
DR OrthoDB; 817156at2759; -.
DR PhylomeDB; Q92733; -.
DR TreeFam; TF318780; -.
DR PathwayCommons; Q92733; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q92733; -.
DR SIGNOR; Q92733; -.
DR BioGRID-ORCS; 5546; 142 hits in 1080 CRISPR screens.
DR ChiTaRS; PRCC; human.
DR GeneWiki; PRCC_(gene); -.
DR GenomeRNAi; 5546; -.
DR Pharos; Q92733; Tbio.
DR PRO; PR:Q92733; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q92733; protein.
DR Bgee; ENSG00000143294; Expressed in cortical plate and 194 other tissues.
DR ExpressionAtlas; Q92733; baseline and differential.
DR Genevisible; Q92733; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR InterPro; IPR018800; PRCC.
DR PANTHER; PTHR13621; PTHR13621; 1.
DR Pfam; PF10253; PRCC; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chromosomal rearrangement; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome.
FT CHAIN 1..491
FT /note="Proline-rich protein PRCC"
FT /id="PRO_0000058568"
FT REGION 1..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..100
FT /note="Mediates interaction with MAD2L2"
FT /evidence="ECO:0000269|PubMed:11717438"
FT REGION 260..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..98
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 239
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 136
FT /note="P -> S (in dbSNP:rs11264542)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_024341"
SQ SEQUENCE 491 AA; 52418 MW; F99CFD9D42725D57 CRC64;
MSLVAYASSD ESEPDEAEPE PEEEEAVAPT SGPALGGLFA SLPAPKGPAL LPPPPQMLAP
AFPPPLLLPP PTGDPRLQPP PPLPFGLGGF PPPPGVSPAE AAGVGEGLGL GLPSPRGPGL
NLPPPIGGAG PPLGLPKPKK RKEPVKIAAP ELHKGDSDSE EDEPTKKKTI LQGSSEGTGL
SALLPQPKNL TVKETNRLLL PHAFSRKPSD GSPDTKPSRL ASKTKTSSLA PVVGTTTTTP
SPSAIKAAAK SAALQVTKQI TQEEDDSDEE VAPENFFSLP EKAEPPGVEP YPYPIPTVPE
ELPPGTEPEP AFQDDAANAP LEFKMAAGSS GAPWMPKPGD DYSYNQFSTY GDANAAGAYY
QDYYSGGYYP AQDPALVPPQ EIAPDASFID DEAFKRLQGK RNRGREEINF VEIKGDDQLS
GAQQWMTKSL TEEKTMKSFS KKKGEQPTGQ QRRKHQITYL IHQAKERELE LKNTWSENKL
SRRQTQAKYG F
