F117B_HUMAN
ID F117B_HUMAN Reviewed; 589 AA.
AC Q6P1L5; Q53QZ5; Q585T9; Q8N8W1; Q96Q34;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein FAM117B;
DE AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 13 protein;
GN Name=FAM117B; Synonyms=ALS2CR13;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-589 (ISOFORM 2).
RX PubMed=11586298; DOI=10.1038/ng1001-166;
RA Hadano S., Hand C.K., Osuga H., Yanagisawa Y., Otomo A., Devon R.S.,
RA Miyamoto N., Showguchi-Miyata J., Okada Y., Singaraja R., Figlewicz D.A.,
RA Kwiatkowski T., Hosler B.A., Sagie T., Skaug J., Nasir J., Brown R.H. Jr.,
RA Scherer S.W., Rouleau G.A., Hayden M.R., Ikeda J.-E.;
RT "A gene encoding a putative GTPase regulator is mutated in familial
RT amyotrophic lateral sclerosis 2.";
RL Nat. Genet. 29:166-173(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-589 (ISOFORM 1).
RC TISSUE=Kidney;
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 MRNA] OF 196-589 (ISOFORM 1).
RC TISSUE=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 IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION BY 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-210; SER-220; SER-273
RP AND SER-457, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
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 -!- INTERACTION:
CC Q6P1L5; O95994: AGR2; NbExp=3; IntAct=EBI-3893327, EBI-712648;
CC Q6P1L5; P24539: ATP5PB; NbExp=3; IntAct=EBI-3893327, EBI-1044810;
CC Q6P1L5; P46379-2: BAG6; NbExp=3; IntAct=EBI-3893327, EBI-10988864;
CC Q6P1L5; Q8N9N5: BANP; NbExp=3; IntAct=EBI-3893327, EBI-744695;
CC Q6P1L5; Q8N9N5-2: BANP; NbExp=4; IntAct=EBI-3893327, EBI-11524452;
CC Q6P1L5; O75190: DNAJB6; NbExp=3; IntAct=EBI-3893327, EBI-1053164;
CC Q6P1L5; Q01658: DR1; NbExp=3; IntAct=EBI-3893327, EBI-750300;
CC Q6P1L5; P63167: DYNLL1; NbExp=11; IntAct=EBI-3893327, EBI-349105;
CC Q6P1L5; Q96FJ2: DYNLL2; NbExp=7; IntAct=EBI-3893327, EBI-742371;
CC Q6P1L5; P21333-2: FLNA; NbExp=3; IntAct=EBI-3893327, EBI-9641086;
CC Q6P1L5; P78333: GPC5; NbExp=3; IntAct=EBI-3893327, EBI-2558325;
CC Q6P1L5; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-3893327, EBI-1054873;
CC Q6P1L5; P04792: HSPB1; NbExp=3; IntAct=EBI-3893327, EBI-352682;
CC Q6P1L5; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-3893327, EBI-6398041;
CC Q6P1L5; Q14145: KEAP1; NbExp=6; IntAct=EBI-3893327, EBI-751001;
CC Q6P1L5; O60333-2: KIF1B; NbExp=3; IntAct=EBI-3893327, EBI-10975473;
CC Q6P1L5; O14901: KLF11; NbExp=3; IntAct=EBI-3893327, EBI-948266;
CC Q6P1L5; P31153: MAT2A; NbExp=3; IntAct=EBI-3893327, EBI-1050743;
CC Q6P1L5; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-3893327, EBI-473160;
CC Q6P1L5; O60260-5: PRKN; NbExp=3; IntAct=EBI-3893327, EBI-21251460;
CC Q6P1L5; P60891: PRPS1; NbExp=3; IntAct=EBI-3893327, EBI-749195;
CC Q6P1L5; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-3893327, EBI-396669;
CC Q6P1L5; Q13148: TARDBP; NbExp=6; IntAct=EBI-3893327, EBI-372899;
CC Q6P1L5; O76024: WFS1; NbExp=3; IntAct=EBI-3893327, EBI-720609;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P1L5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1L5-2; Sequence=VSP_027729, VSP_027730;
CC -!- MISCELLANEOUS: ALS2CR13 is mapped in the genomic region covering the
CC complete candidate region for Amyotrophic lateral sclerosis 2 (ALS2).
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI06907.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI06908.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAX76518.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB69023.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB69023.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
CC Sequence=BAC04700.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC009960; AAX76518.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC098831; AAY24090.1; -; Genomic_DNA.
DR EMBL; AB053315; BAB69023.1; ALT_SEQ; mRNA.
DR EMBL; AK096090; BAC04700.1; ALT_INIT; mRNA.
DR EMBL; BC065010; AAH65010.1; -; mRNA.
DR EMBL; BC106906; AAI06907.1; ALT_INIT; mRNA.
DR EMBL; BC106907; AAI06908.1; ALT_INIT; mRNA.
DR CCDS; CCDS33362.2; -. [Q6P1L5-1]
DR RefSeq; NP_775782.2; NM_173511.3. [Q6P1L5-1]
DR AlphaFoldDB; Q6P1L5; -.
DR SMR; Q6P1L5; -.
DR BioGRID; 127329; 38.
DR IntAct; Q6P1L5; 47.
DR MINT; Q6P1L5; -.
DR STRING; 9606.ENSP00000376071; -.
DR GlyGen; Q6P1L5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6P1L5; -.
DR PhosphoSitePlus; Q6P1L5; -.
DR BioMuta; FAM117B; -.
DR DMDM; 158563965; -.
DR EPD; Q6P1L5; -.
DR jPOST; Q6P1L5; -.
DR MassIVE; Q6P1L5; -.
DR MaxQB; Q6P1L5; -.
DR PaxDb; Q6P1L5; -.
DR PeptideAtlas; Q6P1L5; -.
DR PRIDE; Q6P1L5; -.
DR ProteomicsDB; 66843; -. [Q6P1L5-1]
DR ProteomicsDB; 66844; -. [Q6P1L5-2]
DR Antibodypedia; 1012; 142 antibodies from 23 providers.
DR DNASU; 150864; -.
DR Ensembl; ENST00000392238.3; ENSP00000376071.2; ENSG00000138439.12. [Q6P1L5-1]
DR GeneID; 150864; -.
DR KEGG; hsa:150864; -.
DR MANE-Select; ENST00000392238.3; ENSP00000376071.2; NM_173511.4; NP_775782.2.
DR UCSC; uc010zhx.3; human. [Q6P1L5-1]
DR CTD; 150864; -.
DR DisGeNET; 150864; -.
DR GeneCards; FAM117B; -.
DR HGNC; HGNC:14440; FAM117B.
DR HPA; ENSG00000138439; Low tissue specificity.
DR neXtProt; NX_Q6P1L5; -.
DR OpenTargets; ENSG00000138439; -.
DR PharmGKB; PA164719514; -.
DR VEuPathDB; HostDB:ENSG00000138439; -.
DR eggNOG; ENOG502QR2I; Eukaryota.
DR GeneTree; ENSGT00950000183046; -.
DR HOGENOM; CLU_033432_0_0_1; -.
DR InParanoid; Q6P1L5; -.
DR OMA; DKTRQPS; -.
DR PhylomeDB; Q6P1L5; -.
DR TreeFam; TF333159; -.
DR PathwayCommons; Q6P1L5; -.
DR SignaLink; Q6P1L5; -.
DR BioGRID-ORCS; 150864; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; FAM117B; human.
DR GenomeRNAi; 150864; -.
DR Pharos; Q6P1L5; Tdark.
DR PRO; PR:Q6P1L5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6P1L5; protein.
DR Bgee; ENSG00000138439; Expressed in cortical plate and 175 other tissues.
DR Genevisible; Q6P1L5; HS.
DR InterPro; IPR026641; FAM117B.
DR InterPro; IPR026642; Glcci1/FAM117.
DR PANTHER; PTHR14972; PTHR14972; 1.
DR PANTHER; PTHR14972:SF6; PTHR14972:SF6; 1.
DR Pfam; PF15388; FAM117; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome.
FT CHAIN 1..589
FT /note="Protein FAM117B"
FT /id="PRO_0000299533"
FT REGION 1..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..150
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U3E2"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U3E2"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3U3E2"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 283..289
FT /note="IAKLRQQ -> VRKMVLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11586298"
FT /id="VSP_027729"
FT VAR_SEQ 290..589
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11586298"
FT /id="VSP_027730"
FT CONFLICT 168
FT /note="A -> V (in Ref. 3; BAB69023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 61968 MW; 61B47F16D3E06B14 CRC64;
MSQRVRRNGS PTPAGSLGGG AVATAGGPGS RLQPMRATVP FQLKQQQQQQ HGSPTRSGGG
GGGNNNGGCC GGASGPAGGG GGGGPRTASR STSPTRGGGN AAARTSPTVA TQTGASATST
RGTSPTRSAA PGARGSPPRP PPPPPLLGTV SSPSSSPTHL WTGEVSAAPP PARVRHRRRS
PEQSRSSPEK RSPSAPVCKA GDKTRQPSSS PSSIIRRTSS LDTLAAPYLA GHWPRDSHGQ
AAPCMRDKAT QTESAWAEEY SEKKKGSHKR SASWGSTDQL KEIAKLRQQL QRSKHSSRHH
RDKERQSPFH GNHAAINQCQ APVPKSALIP VIPITKSTGS RFRNSVEGLN QEIEIIIKET
GEKEEQLIPQ DIPDGHRAPP PLVQRSSSTR SIDTQTPGGA DRGSNNSSRS QSVSPTSFLT
ISNEGSEESP CSADDLLVDP RDKENGNNSP LPKYATSPKP NNSYMFKREP PEGCERVKVF
EECSPKQLHE IPAFYCPDKN KVNFIPKSGS AFCLVSILKP LLPTPDLTLK GSGHSLTVTT
GMTTTLLQPI AVASLSTNTE QDRVSRGTST VMPSASLLPP PEPIEEAEG
