ID RNF38_HUMAN Reviewed; 515 AA. AC Q9H0F5; A6PVP9; B1AM81; B1AM82; B3KSG4; E7EVL3; Q7LB33; Q8N0Y0; Q9H748; DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 4. DT 24-JAN-2024, entry version 175. DE RecName: Full=E3 ubiquitin-protein ligase RNF38 {ECO:0000305}; DE EC=2.3.2.27; DE AltName: Full=RING finger protein 38; DE AltName: Full=RING-type E3 ubiquitin transferase RNF38 {ECO:0000305}; GN Name=RNF38 {ECO:0000312|HGNC:HGNC:18052}; 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] (ISOFORM 3), TISSUE SPECIFICITY, AND VARIANT RP THR-206. RX PubMed=12074600; DOI=10.1016/s0006-291x(02)00584-3; RA Eisenberg I., Hochner H., Levi T., Yelin R., Kahan T., RA Mitrani-Rosenbaum S.; RT "Cloning and characterization of a novel human gene RNF38 encoding a RT conserved putative protein with a RING finger domain."; RL Biochem. Biophys. Res. Commun. 294:1169-1176(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5). RC TISSUE=Colon, and Testis; 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=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 [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] (ISOFORM 2). RC TISSUE=Brain; 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, NUCLEAR LOCALIZATION SIGNAL, AND SUBCELLULAR LOCATION. RX PubMed=23973461; DOI=10.1016/j.bbrc.2013.08.031; RA Sheren J.E., Kassenbrock C.K.; RT "RNF38 encodes a nuclear ubiquitin protein ligase that modifies p53."; RL Biochem. Biophys. Res. Commun. 440:473-478(2013). RN [8] RP STRUCTURE BY NMR OF 445-506. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of RING finger in RING finger protein 38."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase able to ubiquitinate CC p53/TP53 which promotes its relocalization to discrete foci associated CC with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme. CC {ECO:0000269|PubMed:23973461}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- INTERACTION: CC Q9H0F5; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2341200, EBI-3867333; CC Q9H0F5; Q5T749: KPRP; NbExp=3; IntAct=EBI-2341200, EBI-10981970; CC Q9H0F5; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-2341200, EBI-10171774; CC Q9H0F5; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-2341200, EBI-1052037; CC Q9H0F5; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-2341200, EBI-1048945; CC Q9H0F5; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-2341200, EBI-18395721; CC Q9H0F5; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-2341200, EBI-11962084; CC Q9H0F5; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-2341200, EBI-18394498; CC Q9H0F5; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-2341200, EBI-10261141; CC Q9H0F5; Q14847-2: LASP1; NbExp=3; IntAct=EBI-2341200, EBI-9088686; CC Q9H0F5; Q8TDS5: OXER1; NbExp=3; IntAct=EBI-2341200, EBI-12813389; CC Q9H0F5; Q9H0X6: RNF208; NbExp=3; IntAct=EBI-2341200, EBI-751555; CC Q9H0F5-2; P54253: ATXN1; NbExp=6; IntAct=EBI-25866807, EBI-930964; CC Q9H0F5-2; P48643: CCT5; NbExp=3; IntAct=EBI-25866807, EBI-355710; CC Q9H0F5-2; P42858: HTT; NbExp=21; IntAct=EBI-25866807, EBI-466029; CC Q9H0F5-2; O76024: WFS1; NbExp=3; IntAct=EBI-25866807, EBI-720609; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23973461}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9H0F5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H0F5-2; Sequence=VSP_012243; CC Name=3; CC IsoId=Q9H0F5-3; Sequence=VSP_037337; CC Name=4; CC IsoId=Q9H0F5-4; Sequence=VSP_053846, VSP_053847; CC Name=5; CC IsoId=Q9H0F5-5; Sequence=VSP_053845; CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis. CC {ECO:0000269|PubMed:12074600}. 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; AF394047; AAM73697.1; -; mRNA. DR EMBL; AL136817; CAB66751.3; -; mRNA. DR EMBL; AK024996; BAB15050.1; -; mRNA. DR EMBL; AK093480; BAG52726.1; -; mRNA. DR EMBL; AL161792; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL354935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58305.1; -; Genomic_DNA. DR EMBL; BC033786; AAH33786.2; -; mRNA. DR CCDS; CCDS6603.1; -. [Q9H0F5-1] DR CCDS; CCDS6604.1; -. [Q9H0F5-2] DR RefSeq; NP_073618.3; NM_022781.4. [Q9H0F5-1] DR RefSeq; NP_919309.1; NM_194328.2. [Q9H0F5-3] DR RefSeq; NP_919310.1; NM_194329.2. [Q9H0F5-2] DR RefSeq; NP_919311.1; NM_194330.2. [Q9H0F5-3] DR RefSeq; NP_919313.1; NM_194332.2. [Q9H0F5-3] DR RefSeq; XP_005251423.1; XM_005251366.3. [Q9H0F5-3] DR RefSeq; XP_005251424.1; XM_005251367.3. [Q9H0F5-3] DR RefSeq; XP_005251425.1; XM_005251368.3. DR RefSeq; XP_006716784.1; XM_006716721.3. [Q9H0F5-3] DR RefSeq; XP_011516014.1; XM_011517712.2. [Q9H0F5-3] DR RefSeq; XP_011516015.1; XM_011517713.2. [Q9H0F5-3] DR RefSeq; XP_016869784.1; XM_017014295.1. DR PDB; 1X4J; NMR; -; A=445-506. DR PDB; 4V3K; X-ray; 2.04 A; C/F=439-515. DR PDB; 4V3L; X-ray; 1.53 A; C=439-515. DR PDB; 7OJX; X-ray; 2.40 A; A=439-515. DR PDBsum; 1X4J; -. DR PDBsum; 4V3K; -. DR PDBsum; 4V3L; -. DR PDBsum; 7OJX; -. DR AlphaFoldDB; Q9H0F5; -. DR SMR; Q9H0F5; -. DR BioGRID; 127416; 101. DR IntAct; Q9H0F5; 32. DR MINT; Q9H0F5; -. DR STRING; 9606.ENSP00000259605; -. DR iPTMnet; Q9H0F5; -. DR PhosphoSitePlus; Q9H0F5; -. DR BioMuta; RNF38; -. DR DMDM; 56749664; -. DR MassIVE; Q9H0F5; -. DR PaxDb; 9606-ENSP00000259605; -. DR PeptideAtlas; Q9H0F5; -. DR ProteomicsDB; 3188; -. DR ProteomicsDB; 80269; -. [Q9H0F5-1] DR ProteomicsDB; 80270; -. [Q9H0F5-2] DR ProteomicsDB; 80271; -. [Q9H0F5-3] DR ProteomicsDB; 81080; -. DR Antibodypedia; 2887; 94 antibodies from 21 providers. DR DNASU; 152006; -. DR Ensembl; ENST00000259605.11; ENSP00000259605.6; ENSG00000137075.18. [Q9H0F5-1] DR Ensembl; ENST00000350199.8; ENSP00000343947.4; ENSG00000137075.18. [Q9H0F5-3] DR Ensembl; ENST00000353739.8; ENSP00000335239.5; ENSG00000137075.18. [Q9H0F5-2] DR Ensembl; ENST00000357058.7; ENSP00000349566.3; ENSG00000137075.18. [Q9H0F5-3] DR Ensembl; ENST00000377877.4; ENSP00000367109.3; ENSG00000137075.18. [Q9H0F5-4] DR Ensembl; ENST00000377885.6; ENSP00000367117.2; ENSG00000137075.18. [Q9H0F5-3] DR Ensembl; ENST00000611646.4; ENSP00000483536.1; ENSG00000137075.18. [Q9H0F5-4] DR GeneID; 152006; -. DR KEGG; hsa:152006; -. DR MANE-Select; ENST00000259605.11; ENSP00000259605.6; NM_022781.5; NP_073618.3. DR UCSC; uc003zzh.5; human. [Q9H0F5-1] DR AGR; HGNC:18052; -. DR CTD; 152006; -. DR DisGeNET; 152006; -. DR GeneCards; RNF38; -. DR HGNC; HGNC:18052; RNF38. DR HPA; ENSG00000137075; Low tissue specificity. DR MIM; 612488; gene. DR neXtProt; NX_Q9H0F5; -. DR OpenTargets; ENSG00000137075; -. DR PharmGKB; PA34438; -. DR VEuPathDB; HostDB:ENSG00000137075; -. DR eggNOG; KOG0800; Eukaryota. DR GeneTree; ENSGT00940000156228; -. DR HOGENOM; CLU_024578_0_0_1; -. DR InParanoid; Q9H0F5; -. DR OMA; LGAHSNH; -. DR OrthoDB; 5474929at2759; -. DR PhylomeDB; Q9H0F5; -. DR TreeFam; TF325756; -. DR PathwayCommons; Q9H0F5; -. DR SignaLink; Q9H0F5; -. DR SIGNOR; Q9H0F5; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 152006; 10 hits in 1193 CRISPR screens. DR ChiTaRS; RNF38; human. DR EvolutionaryTrace; Q9H0F5; -. DR GeneWiki; RNF38; -. DR GenomeRNAi; 152006; -. DR Pharos; Q9H0F5; Tbio. DR PRO; PR:Q9H0F5; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9H0F5; Protein. DR Bgee; ENSG00000137075; Expressed in sperm and 209 other cell types or tissues. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0036126; C:sperm flagellum; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase. DR GO; GO:0008584; P:male gonad development; IEA:Ensembl. DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase. DR CDD; cd16679; RING-H2_RNF38; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR46171:SF1; E3 UBIQUITIN-PROTEIN LIGASE RNF38; 1. DR PANTHER; PTHR46171; GH10160P; 1. DR Pfam; PF13639; zf-RING_2; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q9H0F5; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Metal-binding; Nucleus; KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc; KW Zinc-finger. FT CHAIN 1..515 FT /note="E3 ubiquitin-protein ligase RNF38" FT /id="PRO_0000056078" FT ZN_FING 463..504 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT REGION 73..141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 57..71 FT /note="Bipartite nuclear localization signal 1" FT MOTIF 115..131 FT /note="Bipartite nuclear localization signal 2" FT COMPBIAS 87..113 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..183 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053845" FT VAR_SEQ 1..83 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12074600" FT /id="VSP_037337" FT VAR_SEQ 1..44 FT /note="MACKISPGANSASLPGHPNKVICERVRLQSLFPLLPSDQNTTVQ -> MQHT FT CTQQKKVTYKHIARFSPRNRLCQADAVFNNNLAGFQLQSP (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053846" FT VAR_SEQ 5..54 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_012243" FT VAR_SEQ 45..120 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_053847" FT VARIANT 206 FT /note="A -> T (in dbSNP:rs183475137)" FT /evidence="ECO:0000269|PubMed:12074600" FT /id="VAR_055400" FT CONFLICT 308 FT /note="I -> K (in Ref. 2; CAB66751)" FT /evidence="ECO:0000305" FT CONFLICT 421 FT /note="E -> G (in Ref. 3; BAG52726)" FT /evidence="ECO:0000305" FT HELIX 441..445 FT /evidence="ECO:0007829|PDB:4V3K" FT STRAND 448..450 FT /evidence="ECO:0007829|PDB:4V3L" FT STRAND 453..455 FT /evidence="ECO:0007829|PDB:1X4J" FT STRAND 457..459 FT /evidence="ECO:0007829|PDB:4V3L" FT TURN 464..467 FT /evidence="ECO:0007829|PDB:4V3L" FT STRAND 475..478 FT /evidence="ECO:0007829|PDB:4V3L" FT TURN 480..482 FT /evidence="ECO:0007829|PDB:1X4J" FT STRAND 484..486 FT /evidence="ECO:0007829|PDB:4V3L" FT HELIX 487..496 FT /evidence="ECO:0007829|PDB:4V3L" FT TURN 501..503 FT /evidence="ECO:0007829|PDB:4V3L" SQ SEQUENCE 515 AA; 57595 MW; ABFE9486CA732AFA CRC64; MACKISPGAN SASLPGHPNK VICERVRLQS LFPLLPSDQN TTVQEDAHFK AFFQSEDSPS PKRQRLSHSV FDYTSASPAP SPPMRPWEMT SNRQPPSVRP SQHHFSGERC NTPARNRRSP PVRRQRGRRD RLSRHNSISQ DENYHHLPYA QQQAIEEPRA FHPPNVSPRL LHPAAHPPQQ NAVMVDIHDQ LHQGTVPVSY TVTTVAPHGI PLCTGQHIPA CSTQQVPGCS VVFSGQHLPV CSVPPPMLQA CSVQHLPVPY AAFPPLISSD PFLIHPPHLS PHHPPHLPPP GQFVPFQTQQ SRSPLQRIEN EVELLGEHLP VGGFTYPPSA HPPTLPPSAP LQFLTHDPLH QEVSFGVPYP PFMPRRLTGR SRYRSQQPIP PPPYHPSLLP YVLSMLPVPP AVGPTFSFEL DVEDGEVENY EALLNLAERL GEAKPRGLTK ADIEQLPSYR FNPNNHQSEQ TLCVVCMCDF ESRQLLRVLP CNHEFHAKCV DKWLKANRTC PICRADASEV HRDSE //