ID ZN363_MOUSE Reviewed; 261 AA. AC Q9CR50; Q920H0; DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 172. DE RecName: Full=RING finger and CHY zinc finger domain-containing protein 1; DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q96PM5}; DE AltName: Full=Androgen receptor N-terminal-interacting protein; DE AltName: Full=CH-rich-interacting match with PLAG1; DE AltName: Full=E3 ubiquitin-protein ligase Pirh2; DE AltName: Full=RING-type E3 ubiquitin transferase RCHY1; DE AltName: Full=Zinc finger protein 363; GN Name=Rchy1; Synonyms=Arnip, Chimp, Zfp363, Znf363; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Beitel L.K., Lumbroso R., Panet-Raymond V., de Tourreil A.S., Pinsky L., RA Trifiro M.A.; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Braem C.V., Kas K.; RT "Identification of PLAG1 interacting proteins."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RA Wu H.-S., Chou C.-M., Leu J.-H., Huang C.-J.; RT "A novel mouse zinc-finger protein."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Colon, and Egg; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary tumor; 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 [6] RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=12654245; DOI=10.1016/s0092-8674(03)00193-4; RA Leng R.P., Lin Y., Ma W., Wu H., Lemmers B., Chung S., Parant J.M., RA Lozano G., Hakem R., Benchimol S.; RT "Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation."; RL Cell 112:779-791(2003). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Pancreas; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [8] RP STRUCTURE BY NMR OF 9-186. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the CHY zinc finger domain and of the RING domain of RT the RING finger and CHY zinc finger domain-containing protein 1 from Mus RT musculus."; RL Submitted (AUG-2007) to the PDB data bank. CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of CC target proteins, including p53/TP53, TP73, HDAC1 and CDKN1B (By CC similarity). Mediates ubiquitination and degradation of p53/TP53; CC preferentially acts on tetrameric p53/TP53 (By similarity). Catalyzes CC monoubiquitinates the translesion DNA polymerase POLH CC (PubMed:12654245). Involved in the ribosome-associated quality control CC (RQC) pathway, which mediates the extraction of incompletely CC synthesized nascent chains from stalled ribosomes: RCHY1 acts CC downstream of NEMF and recognizes CAT tails associated with stalled CC nascent chains, leading to their ubiquitination and degradation (By CC similarity). {ECO:0000250|UniProtKB:Q96PM5, CC ECO:0000269|PubMed:12654245}. 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; Evidence={ECO:0000250|UniProtKB:Q96PM5}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000250|UniProtKB:Q96PM5}. CC -!- SUBUNIT: Monomer and homodimer. Interacts with AR, MDM2, KAT5, PLAG1, CC PLAGL2, COPE, UBE2D2 and GORAB/NTKLBP1. {ECO:0000250|UniProtKB:Q96PM5}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96PM5}. Nucleus CC speckle {ECO:0000250|UniProtKB:Q96PM5}. Cytoplasm CC {ECO:0000250|UniProtKB:Q96PM5}. CC -!- TISSUE SPECIFICITY: Detected in testis, liver, kidney and heart. CC {ECO:0000269|PubMed:12654245}. CC -!- INDUCTION: Up-regulated upon p53/TP53 activation. CC {ECO:0000269|PubMed:12654245}. CC -!- PTM: Subject to ubiquitination and proteasomal degradation. Interaction CC with PLAGL2 or KAT5 enhances protein stability. CC {ECO:0000250|UniProtKB:Q96PM5}. 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; AF071222; AAL75940.1; -; mRNA. DR EMBL; AF276959; AAK96899.1; -; mRNA. DR EMBL; AF305423; AAL09355.1; -; mRNA. DR EMBL; AK018364; BAB31179.1; -; mRNA. DR EMBL; AK018488; BAB31236.1; -; mRNA. DR EMBL; AK078397; BAC37254.1; -; mRNA. DR EMBL; BC057143; AAH57143.1; -; mRNA. DR CCDS; CCDS19424.1; -. DR RefSeq; NP_001258726.1; NM_001271797.1. DR RefSeq; NP_080833.1; NM_026557.4. DR PDB; 2DKT; NMR; -; A=9-138. DR PDB; 2ECM; NMR; -; A=145-186. DR PDBsum; 2DKT; -. DR PDBsum; 2ECM; -. DR AlphaFoldDB; Q9CR50; -. DR BMRB; Q9CR50; -. DR SMR; Q9CR50; -. DR BioGRID; 212655; 5. DR STRING; 10090.ENSMUSP00000031345; -. DR PhosphoSitePlus; Q9CR50; -. DR EPD; Q9CR50; -. DR MaxQB; Q9CR50; -. DR PaxDb; 10090-ENSMUSP00000031345; -. DR PeptideAtlas; Q9CR50; -. DR ProteomicsDB; 302081; -. DR Pumba; Q9CR50; -. DR Antibodypedia; 24650; 233 antibodies from 33 providers. DR Ensembl; ENSMUST00000031345.15; ENSMUSP00000031345.9; ENSMUSG00000029397.16. DR GeneID; 68098; -. DR KEGG; mmu:68098; -. DR UCSC; uc008yby.2; mouse. DR AGR; MGI:1915348; -. DR MGI; MGI:1915348; Rchy1. DR VEuPathDB; HostDB:ENSMUSG00000029397; -. DR eggNOG; KOG1940; Eukaryota. DR GeneTree; ENSGT00390000008853; -. DR HOGENOM; CLU_013368_1_0_1; -. DR InParanoid; Q9CR50; -. DR OMA; KLYPCRL; -. DR OrthoDB; 325136at2759; -. DR PhylomeDB; Q9CR50; -. DR TreeFam; TF323762; -. DR Reactome; R-MMU-110320; Translesion Synthesis by POLH. DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 68098; 0 hits in 78 CRISPR screens. DR ChiTaRS; Rchy1; mouse. DR EvolutionaryTrace; Q9CR50; -. DR PRO; PR:Q9CR50; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q9CR50; Protein. DR Bgee; ENSMUSG00000029397; Expressed in interventricular septum and 250 other cell types or tissues. DR ExpressionAtlas; Q9CR50; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB. DR GO; GO:0002039; F:p53 binding; ISO:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI. DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISO:MGI. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB. DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB. DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR CDD; cd16464; RING-H2_Pirh2-like; 1. DR Gene3D; 2.20.28.10; -; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR039512; RCHY1_zinc-ribbon. DR InterPro; IPR008913; Znf_CHY. DR InterPro; IPR037274; Znf_CHY_sf. DR InterPro; IPR017921; Znf_CTCHY. DR InterPro; IPR037275; Znf_CTCHY_sf. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR21319; RING FINGER AND CHY ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1. DR PANTHER; PTHR21319:SF20; RING FINGER AND CHY ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF05495; zf-CHY; 1. DR Pfam; PF13639; zf-RING_2; 1. DR Pfam; PF14599; zinc_ribbon_6; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF161219; CHY zinc finger-like; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF161245; Zinc hairpin stack; 1. DR PROSITE; PS51266; ZF_CHY; 1. DR PROSITE; PS51270; ZF_CTCHY; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR Genevisible; Q9CR50; MM. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Metal-binding; Nucleus; Reference proteome; KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..261 FT /note="RING finger and CHY zinc finger domain-containing FT protein 1" FT /id="PRO_0000056313" FT ZN_FING 13..80 FT /note="CHY-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT ZN_FING 82..144 FT /note="CTCHY-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT ZN_FING 145..189 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 22 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 43 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 44 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 50 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 75 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00601" FT BINDING 87 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT BINDING 90 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT BINDING 101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT BINDING 102 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT BINDING 108 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT BINDING 118 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT BINDING 122 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT BINDING 125 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT BINDING 134 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT BINDING 136 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00965" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 26..31 FT /evidence="ECO:0007829|PDB:2DKT" FT TURN 32..35 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 36..40 FT /evidence="ECO:0007829|PDB:2DKT" FT HELIX 41..46 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 96..102 FT /evidence="ECO:0007829|PDB:2DKT" FT TURN 103..106 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 107..111 FT /evidence="ECO:0007829|PDB:2DKT" FT HELIX 113..115 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:2DKT" FT TURN 120..123 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:2DKT" FT HELIX 128..130 FT /evidence="ECO:0007829|PDB:2DKT" FT STRAND 131..134 FT /evidence="ECO:0007829|PDB:2DKT" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:2ECM" FT TURN 154..156 FT /evidence="ECO:0007829|PDB:2ECM" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:2ECM" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:2ECM" FT HELIX 172..179 FT /evidence="ECO:0007829|PDB:2ECM" SQ SEQUENCE 261 AA; 30014 MW; 219AE48A421CC10D CRC64; MAATAREDGV RNLAQGPRGC EHYDRACLLK APCCDKLYTC RLCHDTNEDH QLDRFKVKEV QCINCEKLQH AQQTCEDCST LFGEYYCSIC HLFDKDKRQY HCESCGICRI GPKEDFFHCL KCNLCLTTNL RGKHKCIENV SRQNCPICLE DIHTSRVVAH VLPCGHLLHR TCYEEMLKEG YRCPLCMHSA LDMTRYWRQL DTEVAQTPMP SEYQNVTVDI LCNDCNGRST VQFHILGMKC KLCDSYNTAQ AGGRRVPVDQ Q //