ID CTNA2_MOUSE Reviewed; 953 AA. AC Q61301; Q3TY37; Q61300; Q6AXD1; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-SEP-2015, entry version 134. DE RecName: Full=Catenin alpha-2; DE AltName: Full=Alpha N-catenin; GN Name=Ctnna2; Synonyms=Catna2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND RP DEVELOPMENTAL STAGE. RX PubMed=8174789; DOI=10.1006/dbio.1994.1124; RA Uchida N., Shimamura K., Miyatani S., Copeland N.G., Gilbert D.J., RA Jenkins N.A., Takeichi M.; RT "Mouse alpha N-catenin: two isoforms, specific expression in the RT nervous system, and chromosomal localization of the gene."; RL Dev. Biol. 163:75-85(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC STRAIN=C57BL/6J; TISSUE=Visual cortex; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC STRAIN=C57BL/6; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=12089526; DOI=10.1038/ng908; RA Park C., Falls W., Finger J.H., Longo-Guess C.M., Ackerman S.L.; RT "Deletion in Catna2, encoding alpha N-catenin, causes cerebellar and RT hippocampal lamination defects and impaired startle modulation."; RL Nat. Genet. 31:279-284(2002). RN [5] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=12123610; DOI=10.1016/S0896-6273(02)00748-1; RA Togashi H., Abe K., Mizoguchi A., Takaoka K., Chisaka O., Takeichi M.; RT "Cadherin regulates dendritic spine morphogenesis."; RL Neuron 35:77-89(2002). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640 AND SER-901, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [7] RP DISRUPTION PHENOTYPE, AND FUNCTION. RX PubMed=15034585; DOI=10.1038/nn1212; RA Abe K., Chisaka O., Van Roy F., Takeichi M.; RT "Stability of dendritic spines and synaptic contacts is controlled by RT alpha N-catenin."; RL Nat. Neurosci. 7:357-363(2004). RN [8] RP DEVELOPMENTAL STAGE. RX PubMed=16185771; DOI=10.1016/j.devbrainres.2005.08.004; RA Ajioka I., Nakajima K.; RT "Switching of alpha-catenin from alphaE-catenin in the cortical RT ventricular zone to alphaN-catenin II in the intermediate zone."; RL Brain Res. Dev. Brain Res. 160:106-111(2005). RN [9] RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION. RX PubMed=16457793; DOI=10.1016/j.brainres.2005.12.057; RA Stocker A.M., Chenn A.; RT "Differential expression of alpha-E-catenin and alpha-N-catenin in the RT developing cerebral cortex."; RL Brain Res. 1073:151-158(2006). RN [10] RP DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION. RX PubMed=16691566; DOI=10.1002/dvdy.20841; RA Uemura M., Takeichi M.; RT "Alpha N-catenin deficiency causes defects in axon migration and RT nuclear organization in restricted regions of the mouse brain."; RL Dev. Dyn. 235:2559-2566(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., RA Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in RT naive and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632; SER-640; SER-651; RP SER-901 AND SER-939, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Brain, and Testis; 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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: May function as a linker between cadherin adhesion CC receptors and the cytoskeleton to regulate cell-cell adhesion and CC differentiation in the nervous system. Regulates morphological CC plasticity of synapses and cerebellar and hippocampal lamination CC during development. Functions in the control of startle CC modulation. {ECO:0000269|PubMed:12089526, CC ECO:0000269|PubMed:12123610, ECO:0000269|PubMed:15034585}. CC -!- SUBUNIT: Interacts with ZNF639. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, CC cytoskeleton {ECO:0000250}. Cell junction, adherens junction. Cell CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; CC Cytoplasmic side {ECO:0000250}. Cell projection, axon. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=alpha N-catenin II; CC IsoId=Q61301-1; Sequence=Displayed; CC Name=2; Synonyms=alpha N-catenin I; CC IsoId=Q61301-2; Sequence=VSP_006734; CC Name=3; CC IsoId=Q61301-3; Sequence=VSP_038010, VSP_006734; CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in the nervous CC system. {ECO:0000269|PubMed:8174789}. CC -!- DEVELOPMENTAL STAGE: The ratio of the two isoforms changes during CC development; isoform 1 is more abundant than isoform 2 in earlier CC embryonic stages, whereas isoform 2 is predominant in the adult CC stage. Expressed in the ventricular zone and in neurons of the CC developing cortical plate (at protein level). Expressed in CC migrating neurons of the external granule cell layer at E13.5 CC while expression appears in the Purkinje cell layer at E17.5 (at CC protein level). Expressed postnatally in Purkinje cells and CC hippocampus (at protein level). {ECO:0000269|PubMed:12089526, CC ECO:0000269|PubMed:16185771, ECO:0000269|PubMed:16457793, CC ECO:0000269|PubMed:8174789}. CC -!- DISRUPTION PHENOTYPE: Mice generally die within 24 hours after CC birth. They display altered Purkinje cells migration, unstable CC synaptic junctions, defective ventricular architecture, impaired CC axon migration, reduced number of neurons in specific nuclei, and CC disordered laminar formation. {ECO:0000269|PubMed:12089526, CC ECO:0000269|PubMed:12123610, ECO:0000269|PubMed:15034585, CC ECO:0000269|PubMed:16691566}. CC -!- MISCELLANEOUS: The cdf (cerebellar deficient folia) mice are CC viable but are ataxic and have cerebellar hypoplasia associated CC with abnormal lobulation of the cerebellum. They also display CC defects in Purkinje cells positioning and in packing density and CC lamination. Fear conditioning and prepulse inhibition of the CC startle response are altered in cdf mice. Those phenotypes are CC associated with alteration of the Ctnna2 gene which results in the CC C-terminal truncation of the protein and are rescued by expression CC of a Ctnna2 transgene (isoform 2). CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family. CC {ECO:0000305}. 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; D25282; BAA04970.1; -; mRNA. DR EMBL; D25281; BAA04969.1; -; mRNA. DR EMBL; AK158916; BAE34726.1; -; mRNA. DR EMBL; BC079648; AAH79648.1; -; mRNA. DR CCDS; CCDS20250.1; -. [Q61301-1] DR CCDS; CCDS39521.1; -. [Q61301-2] DR PIR; I49499; I49499. DR PIR; I49500; I49500. DR RefSeq; NP_001103234.1; NM_001109764.1. [Q61301-1] DR RefSeq; NP_033949.2; NM_009819.2. [Q61301-1] DR RefSeq; NP_663785.2; NM_145732.2. [Q61301-2] DR RefSeq; XP_011239496.1; XM_011241194.1. [Q61301-3] DR UniGene; Mm.34637; -. DR PDB; 4K1O; X-ray; 2.60 A; A=651-953. DR PDB; 4ONS; X-ray; 2.80 A; A/C=18-264. DR PDB; 4P9T; X-ray; 2.50 A; A/B/C/D=13-261. DR PDBsum; 4K1O; -. DR PDBsum; 4ONS; -. DR PDBsum; 4P9T; -. DR ProteinModelPortal; Q61301; -. DR SMR; Q61301; 18-924. DR BioGrid; 198511; 1. DR DIP; DIP-31971N; -. DR IntAct; Q61301; 3. DR MINT; MINT-4092530; -. DR STRING; 10090.ENSMUSP00000124376; -. DR PhosphoSite; Q61301; -. DR MaxQB; Q61301; -. DR PaxDb; Q61301; -. DR PRIDE; Q61301; -. DR Ensembl; ENSMUST00000075340; ENSMUSP00000074809; ENSMUSG00000063063. [Q61301-2] DR Ensembl; ENSMUST00000159626; ENSMUSP00000124376; ENSMUSG00000063063. [Q61301-1] DR Ensembl; ENSMUST00000161846; ENSMUSP00000123714; ENSMUSG00000063063. [Q61301-3] DR GeneID; 12386; -. DR KEGG; mmu:12386; -. DR UCSC; uc009cjq.2; mouse. [Q61301-1] DR UCSC; uc012enl.1; mouse. [Q61301-2] DR CTD; 1496; -. DR MGI; MGI:88275; Ctnna2. DR eggNOG; NOG240050; -. DR GeneTree; ENSGT00550000074411; -. DR HOGENOM; HOG000280724; -. DR HOVERGEN; HBG000069; -. DR InParanoid; Q61301; -. DR KO; K05691; -. DR OrthoDB; EOG7HQN7B; -. DR PhylomeDB; Q61301; -. DR TreeFam; TF313686; -. DR Reactome; R-MMU-375170; CDO in myogenesis. DR ChiTaRS; Ctnna2; mouse. DR NextBio; 281100; -. DR PRO; PR:Q61301; -. DR Proteomes; UP000000589; Chromosome 6. DR Bgee; Q61301; -. DR CleanEx; MM_CTNNA2; -. DR ExpressionAtlas; Q61301; baseline and differential. DR Genevisible; Q61301; MM. DR GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro. DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB. DR GO; GO:0030424; C:axon; IMP:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI. DR GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0030027; C:lamellipodium; IDA:MGI. DR GO; GO:0097481; C:neuronal postsynaptic density; IDA:MGI. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0007409; P:axonogenesis; IMP:UniProtKB. DR GO; GO:0048854; P:brain morphogenesis; IMP:UniProtKB. DR GO; GO:0048813; P:dendrite morphogenesis; IMP:UniProtKB. DR GO; GO:0060134; P:prepulse inhibition; IMP:UniProtKB. DR GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:UniProtKB. DR GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:UniProtKB. DR GO; GO:0016337; P:single organismal cell-cell adhesion; ISS:UniProtKB. DR InterPro; IPR001033; Alpha_catenin. DR InterPro; IPR030046; CTNNA2. DR InterPro; IPR006077; Vinculin/catenin. DR InterPro; IPR000633; Vinculin_CS. DR PANTHER; PTHR18914; PTHR18914; 1. DR PANTHER; PTHR18914:SF23; PTHR18914:SF23; 1. DR Pfam; PF01044; Vinculin; 2. DR PRINTS; PR00805; ALPHACATENIN. DR SUPFAM; SSF47220; SSF47220; 5. DR PROSITE; PS00663; VINCULIN_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell junction; KW Cell membrane; Cell projection; Complete proteome; Cytoplasm; KW Cytoskeleton; Developmental protein; Differentiation; Membrane; KW Phosphoprotein; Reference proteome. FT CHAIN 1 953 Catenin alpha-2. FT /FTId=PRO_0000064264. FT MOD_RES 632 632 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 640 640 Phosphoserine. FT {ECO:0000244|PubMed:15345747, FT ECO:0000244|PubMed:16452087, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 651 651 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 901 901 Phosphoserine. FT {ECO:0000244|PubMed:15345747, FT ECO:0000244|PubMed:21183079}. FT MOD_RES 939 939 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT VAR_SEQ 1 1 M -> MTDIHSSYTYTGSM (in isoform 3). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_038010. FT VAR_SEQ 811 858 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:8174789}. FT /FTId=VSP_006734. FT CONFLICT 103 103 M -> K (in Ref. 1; BAA04970/BAA04969). FT {ECO:0000305}. FT CONFLICT 331 331 I -> M (in Ref. 1; BAA04970/BAA04969). FT {ECO:0000305}. FT CONFLICT 349 349 Y -> D (in Ref. 1; BAA04970/BAA04969). FT {ECO:0000305}. FT CONFLICT 558 558 M -> I (in Ref. 3; AAH79648). FT {ECO:0000305}. FT CONFLICT 618 618 D -> Y (in Ref. 1; BAA04970/BAA04969). FT {ECO:0000305}. FT CONFLICT 648 648 Missing (in Ref. 3; AAH79648). FT {ECO:0000305}. FT CONFLICT 660 660 D -> R (in Ref. 1; BAA04970/BAA04969). FT {ECO:0000305}. FT CONFLICT 817 817 F -> S (in Ref. 1; BAA04970). FT {ECO:0000305}. FT CONFLICT 862 862 A -> S (in Ref. 1; BAA04970/BAA04969). FT {ECO:0000305}. FT CONFLICT 911 911 P -> S (in Ref. 2; BAE34726). FT {ECO:0000305}. FT HELIX 22 39 {ECO:0000244|PDB:4P9T}. FT HELIX 55 81 {ECO:0000244|PDB:4P9T}. FT STRAND 83 85 {ECO:0000244|PDB:4P9T}. FT HELIX 86 112 {ECO:0000244|PDB:4P9T}. FT HELIX 117 165 {ECO:0000244|PDB:4P9T}. FT HELIX 169 196 {ECO:0000244|PDB:4P9T}. FT HELIX 200 229 {ECO:0000244|PDB:4P9T}. FT HELIX 234 258 {ECO:0000244|PDB:4P9T}. FT HELIX 668 673 {ECO:0000244|PDB:4K1O}. FT HELIX 677 702 {ECO:0000244|PDB:4K1O}. FT HELIX 710 729 {ECO:0000244|PDB:4K1O}. FT HELIX 738 763 {ECO:0000244|PDB:4K1O}. FT HELIX 769 791 {ECO:0000244|PDB:4K1O}. FT STRAND 798 802 {ECO:0000244|PDB:4K1O}. FT STRAND 805 809 {ECO:0000244|PDB:4K1O}. FT HELIX 859 894 {ECO:0000244|PDB:4K1O}. SQ SEQUENCE 953 AA; 105286 MW; 52DC5230A4A4A159 CRC64; MTSATSPIIL KWDPKSLEIR TLTVERLLEP LVTQVTTLVN TSNKGPSGKK KGRSKKAHVL AASVEQATQN FLEKGEQIAK ESQDLKEELV AAVEDVRKQG ETMRIASSEF ADDPCSSVKR GTMVRAARAL LSAVTRLLIL ADMADVMRLL SHLKIVEEAL EAVKNATNEQ DLANRFKEFG KEMVKLNYVA ARRQQELKDP HCRDEMAAAR GALKKNATML YTASQAFLRH PDVAATRANR DYVFKQVQEA IAGISSAAQA TSPTDEAKGH TGIGELAAAL NEFDNKIILD PMTFSEARFR PSLEERLESI ISGAALMADS SCTRDDRRER IVAECNAVRQ ALQDLLSEYM NNTGRKEKGD PLNIAIDKMT KKTRDLRRQL RKAVMDHISD SFLETNVPLL VLIEAAKSGN EKEVKEYAQV FREHANKLVE VANLACSISN NEEGVKLVRM AATQIDSLCP QVINAALTLA ARPQSKVAQD NMDVFKDQWE KQVRVLTEAV DDITSVDDFL SVSENHILED VNKCVIALQE GDVDTLDRTA GAIRGRAARV IHIINAEMEN YEAGVYTEKV LEATKLLSET VMPRFAEQVE VAIEALSANV PQPFEENEFI DASRLVYDGV RDIRKAVLMI RTPEELEDDS DFEQEDYDVR SRTSVQTEDD QLIAGQSARA IMAQLPQEEK AKIAEQVEIF HQEKSKLDAE VAKWDDSGND IIVLAKQMCM IMMEMTDFTR GKGPLKNTSD VINAAKKIAE AGSRMDKLAR AVADQCPDSA CKQDLLAYLQ RIALYCHQLN ICSKVKAEVQ NLGGELIVSG TGVQSTFTTF YEVDCDVIDG GRASQLSTHL PTCAEGAPIG SGSSDSSMLD SATSLIQAAK NLMNAVVLTV KASYVASTKY QKVYGTAAVN SPVVSWKMKA PEKKPLVKRE KPEEFQTRVR RGSQKKHISP VQALSEFKAM DSF //