ID GBRAP_MOUSE Reviewed; 117 AA. AC Q9DCD6; B1AR49; Q9QUI7; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2004, sequence version 2. DT 27-MAR-2024, entry version 166. DE RecName: Full=Gamma-aminobutyric acid receptor-associated protein {ECO:0000305}; DE AltName: Full=GABA(A) receptor-associated protein; DE Flags: Precursor; GN Name=Gabarap {ECO:0000312|MGI:MGI:1861742}; 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], SUBCELLULAR LOCATION, AND INTERACTION WITH RP BETA-TUBULIN. RX PubMed=10899939; DOI=10.1046/j.1471-4159.2000.0750644.x; RA Wang H., Olsen R.W.; RT "Binding of the GABA(A) receptor-associated protein (GABARAP) to RT microtubules and microfilaments suggests involvement of the cytoskeleton in RT GABARAPGABA(A) receptor interaction."; RL J. Neurochem. 75:644-655(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver, and 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 [5] RP INTERACTION WITH ATG7. RX PubMed=11890701; DOI=10.1006/bbrc.2002.6645; RA Tanida I., Tanida-Miyake E., Nishitani T., Komatsu M., Yamazaki H., RA Ueno T., Kominami E.; RT "Murine Apg12p has a substrate preference for murine Apg7p over three Apg8p RT homologs."; RL Biochem. Biophys. Res. Commun. 292:256-262(2002). RN [6] RP CLEAVAGE BY ATG4B, AND SUBCELLULAR LOCATION. RX PubMed=14530254; DOI=10.1074/jbc.m308762200; RA Hemelaar J., Lelyveld V.S., Kessler B.M., Ploegh H.L.; RT "A single protease, Apg4B, is specific for the autophagy-related ubiquitin- RT like proteins GATE-16, MAP1-LC3, GABARAP, and Apg8L."; RL J. Biol. Chem. 278:51841-51850(2003). RN [7] RP INTERACTION WITH GPHN. RX PubMed=10900017; DOI=10.1073/pnas.97.15.8594; RA Kneussel M., Haverkamp S., Fuhrmann J.C., Wang H., Waessle H., Olsen R.W., RA Betz H.; RT "The gamma-aminobutyric acid type A receptor (GABAAR)-associated protein RT GABARAP interacts with gephyrin but is not involved in receptor anchoring RT at the synapse."; RL Proc. Natl. Acad. Sci. U.S.A. 97:8594-8599(2000). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Pancreas, 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 [9] RP INTERACTION WITH TBC1D25. RX PubMed=21383079; DOI=10.1083/jcb.201008107; RA Itoh T., Kanno E., Uemura T., Waguri S., Fukuda M.; RT "OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal RT maturation."; RL J. Cell Biol. 192:839-853(2011). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=24089209; DOI=10.1038/nature12639; RA Pampliega O., Orhon I., Patel B., Sridhar S., Diaz-Carretero A., Beau I., RA Codogno P., Satir B.H., Satir P., Cuervo A.M.; RT "Functional interaction between autophagy and ciliogenesis."; RL Nature 502:194-200(2013). RN [11] RP LIPIDATION, AND DELIPIDATION. RX PubMed=33795848; DOI=10.1038/s41418-021-00776-1; RA Tamargo-Gomez I., Martinez-Garcia G.G., Suarez M.F., Rey V., Fueyo A., RA Codina-Martinez H., Bretones G., Caravia X.M., Morel E., Dupont N., RA Cabo R., Tomas-Zapico C., Souquere S., Pierron G., Codogno P., RA Lopez-Otin C., Fernandez A.F., Marino G.; RT "ATG4D is the main ATG8 delipidating enzyme in mammalian cells and protects RT against cerebellar neurodegeneration."; RL Cell Death Differ. 28:2651-2672(2021). RN [12] {ECO:0007744|PDB:7FB5} RP X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) IN COMPLEX WITH HUMAN RETREG1. RX PubMed=34854256; DOI=10.1002/2211-5463.13340; RA Zhao J., Li Z., Li J.; RT "The crystal structure of the FAM134B-GABARAP complex provides mechanistic RT insights into the selective binding of FAM134 to the GABARAP subfamily."; RL FEBS Open Bio 12:320-331(2022). CC -!- FUNCTION: Ubiquitin-like modifier that plays a role in intracellular CC transport of GABA(A) receptors and its interaction with the CC cytoskeleton. Involved in autophagy: while LC3s are involved in CC elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is CC essential for a later stage in autophagosome maturation. Through its CC interaction with the reticulophagy receptor TEX264, participates in the CC remodeling of subdomains of the endoplasmic reticulum into CC autophagosomes upon nutrient stress, which then fuse with lysosomes for CC endoplasmic reticulum turnover. Also required for the local activation CC of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex, regulating CC ubiquitination and degradation of TIAM1, a guanyl-nucleotide exchange CC factor (GEF) that activates RAC1 and downstream signal transduction. CC Thereby, regulates different biological processes including the CC organization of the cytoskeleton, cell migration and proliferation. CC Involved in apoptosis. {ECO:0000250|UniProtKB:O95166}. CC -!- SUBUNIT: Interacts with GPHN (PubMed:10900017). Interacts with NSF (By CC similarity). Interacts with ATG7 (PubMed:11890701). Interacts with ATG3 CC and ATG13 (By similarity). Interacts with alpha-tubulin (By CC similarity). Interacts with beta-tubulin (PubMed:10899939). Interacts CC with GABRG2 (By similarity). Interacts with RB1CC1 (By similarity). CC Interacts with ULK1 (By similarity). Interacts with CALR (By CC similarity). Interacts with DDX47 (By similarity). Interacts with CC TP53INP1 and TP53INP2 (By similarity). Interacts with TBC1D5 (By CC similarity). Interacts with TBC1D25 (PubMed:21383079). Directly CC interacts with SQSTM1 (By similarity). Interacts with MAPK15 (By CC similarity). Interacts with TECPR2 (By similarity). Interacts with PCM1 CC (By similarity). Interacts with TRIM5 and TRIM21 (By similarity). CC Interacts with MEFV (By similarity). Interacts with KIF21B (By CC similarity). Interacts with WDFY3; this interaction is required for CC WDFY3 recruitment to MAP1LC3B-positive p62/SQSTM1 bodies (By CC similarity). Interacts with FLCN; interaction regulates autophagy (By CC similarity). Interacts with UBA5 (By similarity). Interacts with KBTBD6 CC and KBTBD7; the interaction is direct and required for the CC ubiquitination of TIAM1 (By similarity). Interacts with reticulophagy CC regulators RETREG1, RETREG2 and RETREG3 (By similarity). Interacts with CC Irgm1 (By similarity). Interacts with STX17 (By similarity). Interacts CC with CT55; this interaction may be important for GABARAP protein CC stability (By similarity). Interacts with DNM2 (By similarity). CC {ECO:0000250|UniProtKB:O95166, ECO:0000250|UniProtKB:P60517, CC ECO:0000269|PubMed:10899939, ECO:0000269|PubMed:10900017, CC ECO:0000269|PubMed:11890701, ECO:0000269|PubMed:21383079}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane CC {ECO:0000269|PubMed:14530254}. Endomembrane system CC {ECO:0000250|UniProtKB:P60517}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:10899939}. Golgi apparatus membrane CC {ECO:0000250|UniProtKB:P60517}. Cytoplasmic vesicle CC {ECO:0000250|UniProtKB:P60517}. Note=Largely associated with CC intracellular membrane structures including the Golgi apparatus and CC postsynaptic cisternae. Colocalizes with microtubules CC (PubMed:10899939). Localizes also to discrete punctae along the ciliary CC axoneme (PubMed:24089209). {ECO:0000269|PubMed:10899939, CC ECO:0000269|PubMed:14530254, ECO:0000269|PubMed:24089209}. CC -!- PTM: The precursor molecule is cleaved by ATG4 (ATG4A, ATG4B, ATG4C or CC ATG4D) to expose the glycine at the C-terminus and form the cytosolic CC form, GABARAP-I (PubMed:14530254). The processed form is then activated CC by APG7L/ATG7, transferred to ATG3 and conjugated to CC phosphatidylethanolamine (PE) phospholipid to form the membrane-bound CC form, GABARAP-II (By similarity). During non-canonical autophagy, the CC processed form is conjugated to phosphatidylserine (PS) phospholipid CC (By similarity). ATG4 proteins also mediate the delipidation of PE- CC conjugated forms (PubMed:33795848). In addition, ATG4B and ATG4D CC mediate delipidation of ATG8 proteins conjugated to PS during non- CC canonical autophagy (By similarity). ATG4B constitutes the major CC protein for proteolytic activation (By similarity). ATG4D is the main CC enzyme for delipidation activity (PubMed:33795848). CC {ECO:0000250|UniProtKB:O95166, ECO:0000269|PubMed:14530254, CC ECO:0000269|PubMed:33795848}. CC -!- SIMILARITY: Belongs to the ATG8 family. {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; AF161587; AAD47642.1; -; mRNA. DR EMBL; AK002879; BAB22426.1; -; mRNA. DR EMBL; AK011731; BAB27806.1; -; mRNA. DR EMBL; AL596185; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002126; AAH02126.1; -; mRNA. DR EMBL; BC024621; AAH24621.1; -; mRNA. DR EMBL; BC030350; AAH30350.1; -; mRNA. DR CCDS; CCDS24928.1; -. DR RefSeq; NP_062723.1; NM_019749.4. DR PDB; 5YIR; X-ray; 2.75 A; A/B/D=1-117. DR PDB; 6A9X; X-ray; 2.20 A; D=1-117. DR PDB; 7FB5; X-ray; 2.84 A; A=1-117. DR PDBsum; 5YIR; -. DR PDBsum; 6A9X; -. DR PDBsum; 7FB5; -. DR AlphaFoldDB; Q9DCD6; -. DR BMRB; Q9DCD6; -. DR SMR; Q9DCD6; -. DR BioGRID; 208012; 17. DR ELM; Q9DCD6; -. DR IntAct; Q9DCD6; 2. DR MINT; Q9DCD6; -. DR STRING; 10090.ENSMUSP00000018711; -. DR iPTMnet; Q9DCD6; -. DR PhosphoSitePlus; Q9DCD6; -. DR EPD; Q9DCD6; -. DR MaxQB; Q9DCD6; -. DR PaxDb; 10090-ENSMUSP00000018711; -. DR PeptideAtlas; Q9DCD6; -. DR ProteomicsDB; 266780; -. DR Pumba; Q9DCD6; -. DR Antibodypedia; 11841; 760 antibodies from 37 providers. DR DNASU; 56486; -. DR Ensembl; ENSMUST00000018711.15; ENSMUSP00000018711.9; ENSMUSG00000018567.15. DR GeneID; 56486; -. DR KEGG; mmu:56486; -. DR UCSC; uc007jtg.2; mouse. DR AGR; MGI:1861742; -. DR CTD; 11337; -. DR MGI; MGI:1861742; Gabarap. DR VEuPathDB; HostDB:ENSMUSG00000018567; -. DR eggNOG; KOG1654; Eukaryota. DR GeneTree; ENSGT00940000157496; -. DR HOGENOM; CLU_119276_0_0_1; -. DR InParanoid; Q9DCD6; -. DR OMA; AVYQEHK; -. DR OrthoDB; 652940at2759; -. DR PhylomeDB; Q9DCD6; -. DR TreeFam; TF314556; -. DR Reactome; R-MMU-1632852; Macroautophagy. DR Reactome; R-MMU-8854214; TBC/RABGAPs. DR BioGRID-ORCS; 56486; 2 hits in 77 CRISPR screens. DR ChiTaRS; Gabarap; mouse. DR PRO; PR:Q9DCD6; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q9DCD6; Protein. DR Bgee; ENSMUSG00000018567; Expressed in molar tooth and 272 other cell types or tissues. DR ExpressionAtlas; Q9DCD6; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI. DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB. DR GO; GO:0000421; C:autophagosome membrane; ISO:MGI. DR GO; GO:0005930; C:axoneme; IDA:UniProtKB. DR GO; GO:0044297; C:cell body; ISO:MGI. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; IDA:MGI. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005875; C:microtubule associated complex; IDA:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:MGI. DR GO; GO:0097225; C:sperm midpiece; IDA:MGI. DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI. DR GO; GO:0050811; F:GABA receptor binding; ISO:MGI. DR GO; GO:0008017; F:microtubule binding; IDA:MGI. DR GO; GO:0008429; F:phosphatidylethanolamine binding; ISO:MGI. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB. DR GO; GO:0016236; P:macroautophagy; IBA:GO_Central. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:MGI. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR GO; GO:1902524; P:positive regulation of protein K48-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0035020; P:regulation of Rac protein signal transduction; ISS:UniProtKB. DR CDD; cd17232; Ubl_ATG8_GABARAP; 1. DR InterPro; IPR004241; Atg8-like. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10969:SF20; GAMMA-AMINOBUTYRIC ACID RECEPTOR-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR10969; MICROTUBULE-ASSOCIATED PROTEINS 1A/1B LIGHT CHAIN 3-RELATED; 1. DR Pfam; PF02991; ATG8; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR Genevisible; Q9DCD6; MM. PE 1: Evidence at protein level; KW 3D-structure; Apoptosis; Autophagy; Cytoplasm; Cytoplasmic vesicle; KW Cytoskeleton; Golgi apparatus; Lipoprotein; Membrane; Microtubule; KW Protein transport; Reference proteome; Transport. FT CHAIN 1..116 FT /note="Gamma-aminobutyric acid receptor-associated protein" FT /id="PRO_0000212364" FT PROPEP 117 FT /note="Removed in mature form" FT /evidence="ECO:0000269|PubMed:14530254" FT /id="PRO_0000423066" FT REGION 1..22 FT /note="Interaction with beta-tubulin" FT /evidence="ECO:0000269|PubMed:10899939" FT REGION 36..117 FT /note="Interaction with GPHN" FT /evidence="ECO:0000269|PubMed:10900017" FT REGION 36..68 FT /note="Interaction with GABRG2" FT /evidence="ECO:0000250|UniProtKB:O95166" FT REGION 48..50 FT /note="Interaction with LIR (LC3 nteracting Region) motif FT of ATG3" FT /evidence="ECO:0000250|UniProtKB:O95166" FT SITE 17 FT /note="Interaction with LIR (LC3 nteracting Region) motif FT of ATG3" FT /evidence="ECO:0000250|UniProtKB:O95166" FT SITE 28 FT /note="Interaction with LIR (LC3 nteracting Region) motif FT of ATG3" FT /evidence="ECO:0000250|UniProtKB:O95166" FT SITE 116..117 FT /note="Cleavage; by ATG4B" FT /evidence="ECO:0000269|PubMed:14530254" FT LIPID 116 FT /note="Phosphatidylethanolamine amidated glycine; FT alternate" FT /evidence="ECO:0000250|UniProtKB:O95166" FT LIPID 116 FT /note="Phosphatidylserine amidated glycine; alternate" FT /evidence="ECO:0000250|UniProtKB:O95166" FT CONFLICT 12 FT /note="E -> D (in Ref. 2; BAB22426)" FT /evidence="ECO:0000305" FT HELIX 4..8 FT /evidence="ECO:0007829|PDB:6A9X" FT HELIX 11..24 FT /evidence="ECO:0007829|PDB:6A9X" FT STRAND 28..35 FT /evidence="ECO:0007829|PDB:6A9X" FT STRAND 47..52 FT /evidence="ECO:0007829|PDB:6A9X" FT HELIX 57..68 FT /evidence="ECO:0007829|PDB:6A9X" FT STRAND 77..83 FT /evidence="ECO:0007829|PDB:6A9X" FT HELIX 91..98 FT /evidence="ECO:0007829|PDB:6A9X" FT STRAND 105..114 FT /evidence="ECO:0007829|PDB:6A9X" SQ SEQUENCE 117 AA; 13918 MW; BC0B84B8A51C1E32 CRC64; MKFVYKEEHP FEKRRSEGEK IRKKYPDRVP VIVEKAPKAR IGDLDKKKYL VPSDLTVGQF YFLIRKRIHL RAEDALFFFV NNVIPPTSAT MGQLYQEHHE EDFFLYIAYS DESVYGL //