ID VPS35_MOUSE Reviewed; 796 AA. AC Q9EQH3; Q61123; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 176. DE RecName: Full=Vacuolar protein sorting-associated protein 35; DE AltName: Full=Maternal-embryonic 3; DE AltName: Full=Vesicle protein sorting 35; GN Name=Vps35; Synonyms=Mem3; 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]. RC TISSUE=Embryo, and Embryonic carcinoma; RX PubMed=8678978; DOI=10.1007/s003359900174; RA Hwang S.-Y., Benjamin L.E., Oh B., Rothstein J.L., Ackerman S.L., RA Beddington R.S.P., Solter D., Knowles B.B.; RT "Genetic mapping and embryonic expression of a novel, maternally RT transcribed gene Mem3."; RL Mamm. Genome 7:586-590(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11112353; DOI=10.1006/geno.2000.6380; RA Zhang P., Yu L., Gao J., Fu Q., Dai F., Zhao Y., Zheng L., Zhao S.; RT "Cloning and characterization of human VPS35 and mouse Vps35 and mapping of RT VPS35 to human chromosome 16q13-q21."; RL Genomics 70:253-257(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC 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 [4] RP PROTEIN SEQUENCE OF 91-107; 218-226; 297-305; 313-323; 372-382; 404-417 AND RP 574-582, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Brain; RA Lubec G., Kang S.U.; RL Submitted (APR-2007) to UniProtKB. RN [5] RP INTERACTION WITH VPS26B. RX PubMed=16190980; DOI=10.1111/j.1600-0854.2005.00328.x; RA Kerr M.C., Bennetts J.S., Simpson F., Thomas E.C., Flegg C., Gleeson P.A., RA Wicking C., Teasdale R.D.; RT "A novel mammalian retromer component, Vps26B."; RL Traffic 6:991-1001(2005). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-791, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Mast cell; RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864; RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., RA Kawakami T., Salomon A.R.; RT "Quantitative time-resolved phosphoproteomic analysis of mast cell RT signaling."; RL J. Immunol. 179:5864-5876(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-791, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [8] RP SUBUNIT. RX PubMed=21040701; DOI=10.1016/j.bbrc.2010.10.121; RA Kim E., Lee Y., Lee H.J., Kim J.S., Song B.S., Huh J.W., Lee S.R., RA Kim S.U., Kim S.H., Hong Y., Shim I., Chang K.T.; RT "Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin RT trafficking."; RL Biochem. Biophys. Res. Commun. 403:167-171(2010). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, 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 expression."; RL Cell 143:1174-1189(2010). RN [10] RP SUBUNIT. RX PubMed=20875039; DOI=10.1111/j.1600-0854.2010.01124.x; RA Norwood S.J., Shaw D.J., Cowieson N.P., Owen D.J., Teasdale R.D., RA Collins B.M.; RT "Assembly and solution structure of the core retromer protein complex."; RL Traffic 12:56-71(2011). RN [11] RP SUBUNIT. RX PubMed=21920005; DOI=10.1111/j.1600-0854.2011.01284.x; RA Bugarcic A., Zhe Y., Kerr M.C., Griffin J., Collins B.M., Teasdale R.D.; RT "Vps26A and Vps26B subunits define distinct retromer complexes."; RL Traffic 12:1759-1773(2011). RN [12] RP INTERACTION WITH LRRK2. RX PubMed=23395371; DOI=10.1016/j.neuron.2012.11.033; RA MacLeod D.A., Rhinn H., Kuwahara T., Zolin A., Di Paolo G., McCabe B.D., RA MacCabe B.D., Marder K.S., Honig L.S., Clark L.N., Small S.A., RA Abeliovich A.; RT "RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and RT Parkinson's disease risk."; RL Neuron 77:425-439(2013). RN [13] RP INTERACTION WITH SORCS2, AND TISSUE SPECIFICITY. RX PubMed=28469074; DOI=10.1172/jci.insight.88995; RA Ma Q., Yang J., Milner T.A., Vonsattel J.G., Palko M.E., Tessarollo L., RA Hempstead B.L.; RT "SorCS2-mediated NR2A trafficking regulates motor deficits in Huntington's RT disease."; RL JCI Insight 2:0-0(2017). CC -!- FUNCTION: Acts as a component of the retromer cargo-selective complex CC (CSC). The CSC is believed to be the core functional component of CC retromer or respective retromer complex variants acting to prevent CC missorting of selected transmembrane cargo proteins into the lysosomal CC degradation pathway. The recruitment of the CSC to the endosomal CC membrane involves RAB7A and SNX3. The CSC seems to associate with the CC cytoplasmic domain of cargo proteins predominantly via VPS35; however, CC these interactions seem to be of low affinity and retromer SNX proteins CC may also contribute to cargo selectivity thus questioning the classical CC function of the CSC. The SNX-BAR retromer mediates retrograde transport CC of cargo proteins from endosomes to the trans-Golgi network (TGN) and CC is involved in endosome-to-plasma membrane transport for cargo protein CC recycling. The SNX3-retromer mediates the retrograde transport of WLS CC distinct from the SNX-BAR retromer pathway. The SNX27-retromer is CC believed to be involved in endosome-to-plasma membrane trafficking and CC recycling of a broad spectrum of cargo proteins. The CSC seems to act CC as recruitment hub for other proteins, such as the WASH complex and CC TBC1D5 (Probable). Required for retrograde transport of lysosomal CC enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of CC the polymeric immunoglobulin receptor (pIgR-pIgA). Required for CC endosomal localization of WASHC2 and mediates the association of the CC CSC with the WASH complex (By similarity). CC {ECO:0000250|UniProtKB:Q96QK1}. CC -!- SUBUNIT: Component of the heterotrimeric retromer cargo-selective CC complex (CSC), also described as vacuolar protein sorting subcomplex CC (VPS) formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35. The CSC has CC a highly elongated structure with VPS26 and VPS29 binding independently CC at opposite distal ends of VPS35 as central platform (PubMed:21040701, CC PubMed:20875039, PubMed:21920005). The CSC is believed to associate CC with variable sorting nexins to form functionally distinct retromer CC complex variants. The originally described retromer complex (also CC called SNX-BAR retromer) is a pentamer containing the CSC and a CC heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 CC and SNX5 or SNX6 (also called SNX-BAR subcomplex); the affinity between CC the respective CSC and SNX-BAR subcomplexes is low. The CSC associates CC with SNX3 to form a SNX3-retromer complex. The CSC associates with CC SNX27, the WASH complex and the SNX-BAR subcomplex to form the SNX27- CC retromer complex (Probable). Interacts with VPS26A, VPS29, VPS26B and CC LRRK2 (PubMed:16190980, PubMed:21040701, PubMed:20875039, CC PubMed:21920005, PubMed:23395371). Interacts with SNX1, SNX2, IGF2R, CC SNX3, GOLPH3, SLC11A2, WASHC2, FKBP15, WASHC1, EHD1. Interacts with CC MAGEL2; leading to recruitment of the TRIM27:MAGEL2 E3 ubiquitin ligase CC complex retromer-containing endosomes (By similarity). Interacts with CC SORCS2 (PubMed:28469074). {ECO:0000250|UniProtKB:Q96QK1, CC ECO:0000269|PubMed:16190980, ECO:0000269|PubMed:20875039, CC ECO:0000269|PubMed:21040701, ECO:0000269|PubMed:21920005, CC ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:28469074}. CC -!- INTERACTION: CC Q9EQH3; O88307: Sorl1; NbExp=2; IntAct=EBI-775825, EBI-7540114; CC Q9EQH3; Q6PHU5: Sort1; NbExp=3; IntAct=EBI-775825, EBI-6985663; CC Q9EQH3; P40336-1: Vps26a; NbExp=2; IntAct=EBI-775825, EBI-15553779; CC Q9EQH3; Q9QZ88: Vps29; NbExp=5; IntAct=EBI-775825, EBI-8334188; CC Q9EQH3; Q9QZ88-1: Vps29; NbExp=3; IntAct=EBI-775825, EBI-15553808; CC Q9EQH3; Q5T1M5: FKBP15; Xeno; NbExp=3; IntAct=EBI-775825, EBI-5235934; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. Endosome CC {ECO:0000250|UniProtKB:Q96QK1}. Early endosome {ECO:0000305}. Late CC endosome {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Detected in striatum (at protein level) CC (PubMed:28469074). Ubiquitous. Highly expressed in fat tissue, testis, CC brain, kidney, thymus, liver and pancreas, and at lower levels in CC heart, intestine and skeletal muscle. Detected in oocytes, pre- CC implantation embryos and at 6.5-12.5 dpc. CC {ECO:0000269|PubMed:28469074}. CC -!- SIMILARITY: Belongs to the VPS35 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB18153.1; Type=Frameshift; Evidence={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; U47024; AAB18153.1; ALT_FRAME; mRNA. DR EMBL; AF226323; AAG40621.1; -; mRNA. DR EMBL; BC005469; AAH05469.1; -; mRNA. DR EMBL; BC006637; AAH06637.1; -; mRNA. DR CCDS; CCDS40421.1; -. DR RefSeq; NP_075373.1; NM_022997.4. DR PDB; 6VAB; EM; 4.90 A; B/D=1-796. DR PDB; 6VAC; EM; 5.70 A; A=1-796. DR PDB; 7U6F; EM; 4.90 A; D1=1-796. DR PDBsum; 6VAB; -. DR PDBsum; 6VAC; -. DR PDBsum; 7U6F; -. DR AlphaFoldDB; Q9EQH3; -. DR EMDB; EMD-21135; -. DR EMDB; EMD-21136; -. DR EMDB; EMD-24963; -. DR EMDB; EMD-24964; -. DR EMDB; EMD-26340; -. DR EMDB; EMD-26341; -. DR EMDB; EMD-26342; -. DR EMDB; EMD-26343; -. DR EMDB; EMD-26345; -. DR SMR; Q9EQH3; -. DR BioGRID; 211137; 32. DR CORUM; Q9EQH3; -. DR DIP; DIP-32210N; -. DR IntAct; Q9EQH3; 33. DR MINT; Q9EQH3; -. DR STRING; 10090.ENSMUSP00000034131; -. DR GlyGen; Q9EQH3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9EQH3; -. DR PhosphoSitePlus; Q9EQH3; -. DR SwissPalm; Q9EQH3; -. DR EPD; Q9EQH3; -. DR jPOST; Q9EQH3; -. DR MaxQB; Q9EQH3; -. DR PaxDb; 10090-ENSMUSP00000034131; -. DR ProteomicsDB; 297815; -. DR Pumba; Q9EQH3; -. DR Antibodypedia; 28023; 368 antibodies from 41 providers. DR DNASU; 65114; -. DR Ensembl; ENSMUST00000034131.10; ENSMUSP00000034131.9; ENSMUSG00000031696.10. DR GeneID; 65114; -. DR KEGG; mmu:65114; -. DR UCSC; uc009mpo.1; mouse. DR AGR; MGI:1890467; -. DR CTD; 55737; -. DR MGI; MGI:1890467; Vps35. DR VEuPathDB; HostDB:ENSMUSG00000031696; -. DR eggNOG; KOG1107; Eukaryota. DR GeneTree; ENSGT00390000007315; -. DR HOGENOM; CLU_005836_1_0_1; -. DR InParanoid; Q9EQH3; -. DR OMA; YIRSREY; -. DR OrthoDB; 5475912at2759; -. DR PhylomeDB; Q9EQH3; -. DR TreeFam; TF105659; -. DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking. DR BioGRID-ORCS; 65114; 32 hits in 80 CRISPR screens. DR ChiTaRS; Vps35; mouse. DR PRO; PR:Q9EQH3; -. DR Proteomes; UP000000589; Chromosome 8. DR RNAct; Q9EQH3; Protein. DR Bgee; ENSMUSG00000031696; Expressed in medial ganglionic eminence and 259 other cell types or tissues. DR ExpressionAtlas; Q9EQH3; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0098691; C:dopaminergic synapse; IDA:SynGO. DR GO; GO:0005769; C:early endosome; ISO:MGI. DR GO; GO:0005768; C:endosome; IDA:MGI. DR GO; GO:0010008; C:endosome membrane; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO. DR GO; GO:0005770; C:late endosome; IBA:GO_Central. DR GO; GO:0005764; C:lysosome; ISO:MGI. DR GO; GO:0016020; C:membrane; ISA:MGI. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0099073; C:mitochondrion-derived vesicle; ISO:MGI. DR GO; GO:0043005; C:neuron projection; IMP:ParkinsonsUK-UCL. DR GO; GO:0043025; C:neuronal cell body; IMP:ParkinsonsUK-UCL. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:ParkinsonsUK-UCL. DR GO; GO:0098794; C:postsynapse; IDA:SynGO. DR GO; GO:0014069; C:postsynaptic density; IDA:MGI. DR GO; GO:0098793; C:presynapse; IDA:SynGO. DR GO; GO:0030904; C:retromer complex; IDA:UniProtKB. DR GO; GO:0030906; C:retromer, cargo-selective complex; ISO:MGI. DR GO; GO:0045202; C:synapse; IDA:MGI. DR GO; GO:0097422; C:tubular endosome; ISS:UniProtKB. DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0007040; P:lysosome organization; IMP:ParkinsonsUK-UCL. DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:MGI. DR GO; GO:0099074; P:mitochondrion to lysosome vesicle-mediated transport; ISO:MGI. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL. DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI. DR GO; GO:1902823; P:negative regulation of late endosome to lysosome transport; ISO:MGI. DR GO; GO:1905166; P:negative regulation of lysosomal protein catabolic process; IMP:ParkinsonsUK-UCL. DR GO; GO:0032463; P:negative regulation of protein homooligomerization; IMP:ParkinsonsUK-UCL. DR GO; GO:1903828; P:negative regulation of protein localization; IMP:ParkinsonsUK-UCL. DR GO; GO:0099639; P:neurotransmitter receptor transport, endosome to plasma membrane; IMP:ParkinsonsUK-UCL. DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IDA:SynGO. DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL. DR GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; IMP:ParkinsonsUK-UCL. DR GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ParkinsonsUK-UCL. DR GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:ARUK-UCL. DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI. DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI. DR GO; GO:1904377; P:positive regulation of protein localization to cell periphery; ISO:MGI. DR GO; GO:0061357; P:positive regulation of Wnt protein secretion; IMP:ParkinsonsUK-UCL. DR GO; GO:0031648; P:protein destabilization; IMP:ParkinsonsUK-UCL. DR GO; GO:0036010; P:protein localization to endosome; ISS:UniProtKB. DR GO; GO:0033365; P:protein localization to organelle; IMP:ParkinsonsUK-UCL. DR GO; GO:1902950; P:regulation of dendritic spine maintenance; ISO:MGI. DR GO; GO:0010821; P:regulation of mitochondrion organization; ISO:MGI. DR GO; GO:0150052; P:regulation of postsynapse assembly; IDA:SynGO. DR GO; GO:0051246; P:regulation of protein metabolic process; ISO:MGI. DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI. DR GO; GO:0090128; P:regulation of synapse maturation; IDA:SynGO. DR GO; GO:2000331; P:regulation of terminal button organization; ISO:MGI. DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB. DR GO; GO:0045056; P:transcytosis; ISS:UniProtKB. DR GO; GO:0006624; P:vacuolar protein processing; ISA:MGI. DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO. DR GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:ARUK-UCL. DR Gene3D; 1.25.40.660; Vacuolar protein sorting-associated protein 35, helical subcomplex Vps35-C; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR005378; Vps35. DR InterPro; IPR042491; Vps35_C. DR PANTHER; PTHR11099:SF0; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 35; 1. DR PANTHER; PTHR11099; VACUOLAR SORTING PROTEIN 35; 1. DR Pfam; PF03635; Vps35; 1. DR PIRSF; PIRSF009375; Retromer_Vps35; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q9EQH3; MM. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Endosome; Membrane; KW Phosphoprotein; Protein transport; Reference proteome; Transport. FT CHAIN 1..796 FT /note="Vacuolar protein sorting-associated protein 35" FT /id="PRO_0000065897" FT REGION 25..44 FT /note="Interaction with SNX3" FT /evidence="ECO:0000250|UniProtKB:Q96QK1" FT REGION 205..215 FT /note="Interaction with SNX3" FT /evidence="ECO:0000250|UniProtKB:Q96QK1" FT REGION 438..796 FT /note="Interaction with SLC11A2" FT /evidence="ECO:0000250|UniProtKB:Q96QK1" FT REGION 500..693 FT /note="Interaction with IGF2R cytoplasmic domain" FT /evidence="ECO:0000250|UniProtKB:Q96QK1" FT REGION 776..796 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96QK1" FT MOD_RES 783 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 791 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660, FT ECO:0007744|PubMed:19131326" SQ SEQUENCE 796 AA; 91713 MW; 2ABD338111D641CC CRC64; MPTTQQSPQD EQEKLLDEAI QAVKVQSFQM KRCLDKNKLM DALKHASNML GELRTSMLSP KSYYELYMAI SDELHYLEVY LTDEFAKGRK VADLYELVQY AGNIIPRLYL LITVGVVYVK SFPQSRKDIL KDLVEMCRGV QHPLRGLFLR NYLLQCTRNI LPDEGEPTDE ETTGDISDSM DFVLLNFAEM NKLWVRMQHQ GHSRDREKRE RERQELRILV GTNLVRLSQL EGVNVERYKQ IVLTGILEQV VNCRDALAQE YLMECIIQVF PDEFHLQTLN PFLRACAELH QNVNVKNIII ALIDRLALFA HREDGPGIPA EIKLFDIFSQ QVATVIQSRQ DMPSEDVVSL QVSLINLAMK CYPDRVDYVD KVLETTVEIF NKLNLEHIAT SSAVSKELTR LLKIPVDTYN NILTVLKLKH FHPLFEYFDY ESRKSMSCYV LSNVLDYNTE IVSQDQVDSI MNLVSTLIQD QPDQPVEDPD PEDFADEQSL VGRFIHLLRS DDPDQQYLIL NTARKHFGAG GNQRIRFTLP PLVFAAYQLA FRYKENSQMD DKWEKKCQKI FSFAHQTISA LIKAELAELP LRLFLQGALA AGEIGFENHE TVAYEFMSQA FSLYEDEISD SKAQLAAITL IIGTFERMKC FSEENHEPLR TQCALAASKL LKKPDQGRAV STCAHLFWSG RNTDKNGEEL HGGKRVMECL KKALKIANQC MDPSLQVQLF IEILNRYIYF YEKENDAVTI QVLNQLIQKI REDLPNLESS EETEQINKHF HNTLEHLRSR RESPESEGPI YEGLIL //