FKB15_MOUSE
ID FKB15_MOUSE Reviewed; 1216 AA.
AC Q6P9Q6; Q3TSY4; Q5SQG3; Q80TU5;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=FK506-binding protein 15;
DE Short=FKBP-15;
DE AltName: Full=133 kDa FK506-binding protein;
DE Short=133 kDa FKBP;
DE Short=FKBP-133;
DE AltName: Full=WASP and FKBP-like;
DE Short=WAFL;
GN Name=Fkbp15; Synonyms=Fkbp133, Kiaa0674;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=C57BL/6J; 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-704.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 213-1216 (ISOFORM B).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP IDENTIFICATION, ALTERNATIVE SPLICING (ISOFORMS A AND B), FUNCTION,
RP DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16756961; DOI=10.1016/j.bbrc.2006.05.113;
RA Nakajima O., Nakamura F., Yamashita N., Tomita Y., Suto F., Okada T.,
RA Iwamatsu A., Kondo E., Fujisawa H., Takei K., Goshima Y.;
RT "FKBP133: a novel mouse FK506-binding protein homolog alters growth cone
RT morphology.";
RL Biochem. Biophys. Res. Commun. 346:140-149(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1091; THR-1093 AND SER-1159,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-1159, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-310; SER-617;
RP SER-1050; SER-1091; THR-1093; SER-1157; SER-1159 AND SER-1190, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 INTERACTION WITH TBC1D23.
RX PubMed=29084197; DOI=10.1038/ncb3627;
RA Shin J.J.H., Gillingham A.K., Begum F., Chadwick J., Munro S.;
RT "TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at
RT the trans-Golgi.";
RL Nat. Cell Biol. 19:1424-1432(2017).
CC -!- FUNCTION: Involved in the transport of early endosomes at the level of
CC transition between microfilament-based and microtubule-based movement
CC (By similarity). May be involved in the cytoskeletal organization of
CC neuronal growth cones. Seems to be inactive as a PPIase. {ECO:0000250,
CC ECO:0000269|PubMed:16756961}.
CC -!- SUBUNIT: Interacts with WIP and actin (By similarity). Interacts with
CC TBC1D23 (PubMed:29084197). {ECO:0000250|UniProtKB:Q5T1M5,
CC ECO:0000269|PubMed:29084197}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16756961}. Cell
CC projection, axon {ECO:0000269|PubMed:16756961}. Early endosome
CC {ECO:0000269|PubMed:16756961}. Note=Present in axons and neuronal
CC growth cones. {ECO:0000269|PubMed:16756961}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q6P9Q6-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q6P9Q6-2; Sequence=VSP_027759;
CC -!- TISSUE SPECIFICITY: Expressed in brain, with highest levels in the
CC granular cell layer of cerebellum and in the granule cell layer of
CC dentate gyrus. {ECO:0000269|PubMed:16756961}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in the developing nervous
CC system at 18.5 dpc. Present in brain, heart, lung, kidney and thymus at
CC 18.5 dpc (at protein level). {ECO:0000269|PubMed:16756961}.
CC -!- DOMAIN: The PPIase FKBP-type domain seems to be inactive both for
CC FK506-binding and enzymatic activity.
CC -!- DOMAIN: The central coiled-coil region is responsible for association
CC with early endosomes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR EMBL; AL683829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL732548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060651; AAH60651.1; -; mRNA.
DR EMBL; AK161705; BAE36541.1; -; mRNA.
DR EMBL; AK122343; BAC65625.1; -; mRNA.
DR CCDS; CCDS51201.1; -. [Q6P9Q6-1]
DR RefSeq; NP_001038993.1; NM_001045528.1. [Q6P9Q6-1]
DR RefSeq; XP_006538097.1; XM_006538034.3. [Q6P9Q6-2]
DR AlphaFoldDB; Q6P9Q6; -.
DR SMR; Q6P9Q6; -.
DR BioGRID; 237211; 11.
DR IntAct; Q6P9Q6; 2.
DR STRING; 10090.ENSMUSP00000081575; -.
DR iPTMnet; Q6P9Q6; -.
DR PhosphoSitePlus; Q6P9Q6; -.
DR SwissPalm; Q6P9Q6; -.
DR EPD; Q6P9Q6; -.
DR jPOST; Q6P9Q6; -.
DR MaxQB; Q6P9Q6; -.
DR PaxDb; Q6P9Q6; -.
DR PeptideAtlas; Q6P9Q6; -.
DR PRIDE; Q6P9Q6; -.
DR ProteomicsDB; 271893; -. [Q6P9Q6-1]
DR ProteomicsDB; 271894; -. [Q6P9Q6-2]
DR Antibodypedia; 1961; 101 antibodies from 21 providers.
DR Ensembl; ENSMUST00000084527; ENSMUSP00000081575; ENSMUSG00000066151. [Q6P9Q6-1]
DR GeneID; 338355; -.
DR KEGG; mmu:338355; -.
DR UCSC; uc008teh.2; mouse. [Q6P9Q6-1]
DR UCSC; uc008tei.1; mouse. [Q6P9Q6-2]
DR CTD; 23307; -.
DR MGI; MGI:2444782; Fkbp15.
DR VEuPathDB; HostDB:ENSMUSG00000066151; -.
DR eggNOG; KOG0549; Eukaryota.
DR eggNOG; KOG4725; Eukaryota.
DR GeneTree; ENSGT00530000064286; -.
DR HOGENOM; CLU_007194_1_0_1; -.
DR InParanoid; Q6P9Q6; -.
DR OMA; NQHEREK; -.
DR OrthoDB; 936280at2759; -.
DR PhylomeDB; Q6P9Q6; -.
DR TreeFam; TF328592; -.
DR BioGRID-ORCS; 338355; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Fkbp15; mouse.
DR PRO; PR:Q6P9Q6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6P9Q6; protein.
DR Bgee; ENSMUSG00000066151; Expressed in stroma of bone marrow and 259 other tissues.
DR ExpressionAtlas; Q6P9Q6; baseline and differential.
DR Genevisible; Q6P9Q6; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0030426; C:growth cone; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR Pfam; PF00254; FKBP_C; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell projection;
KW Coiled coil; Cytoplasm; Endocytosis; Endosome; Phosphoprotein;
KW Reference proteome; Transport.
FT CHAIN 1..1216
FT /note="FK506-binding protein 15"
FT /id="PRO_0000299557"
FT DOMAIN 196..289
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT REGION 41..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..168
FT /note="Important for function in growth cone organization"
FT REGION 292..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 519..790
FT /evidence="ECO:0000255"
FT COILED 820..865
FT /evidence="ECO:0000255"
FT COMPBIAS 51..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..967
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1216
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1M5"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1M5"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1M5"
FT MOD_RES 91
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1M5"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1M5"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1M5"
FT MOD_RES 1018
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1M5"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1093
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1M5"
FT MOD_RES 1153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1M5"
FT MOD_RES 1157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T1M5"
FT VAR_SEQ 1190..1216
FT /note="SMKGRPPPTPLFGDDDDDDDDDIGWLG -> VRRPQALLSPHTTTWGLFPAG
FT SETRKGVCWWLVSWTLCTGPCGSKLGAQSGQLCKHDGDGQLPLYS (in isoform
FT B)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_027759"
FT CONFLICT 652
FT /note="H -> R (in Ref. 3; BAE36541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1216 AA; 132961 MW; 8F8130D5038122FF CRC64;
MFGAGDEDDT DFLSPSGGAK LASLFGLDQA TMGHGNEFFQ YTAPKQPKKG QGTAAGNQTA
PKPAPATTGT SSVLFATAVH AYRYINGQYA KQGKFGAAVL GNHTSREYRI LLYISQQQPV
TVATIHLNFE LMVRPNNYST FYDDQRQNWS IMFESEKAAV SFNKQVCVAK CNSISSLDAV
LCQDLVAAEG PAVETGDSLE VAYTGWLLQN HVLGQVFDST ANKDKPLRLK LGSGKVVKGL
EDGLLGMKKG GKRLIITPSA CAAGSEGVIG WTQPTDSILV FEVEVRRVKF ARDSGSDGHS
VSSRDSAAPS PIPASDSLSA DPVVTPLPLP LKPGEPGLRS KSNSLSEQLT VNSNPDTVKA
KLISRMAKMG QPMLPILPPQ LDSNDSETED ATVLRGAGQS LVTPSIQPSL QPAHPVLPQM
ASQAPQPSGS GLQTPSAALM QAVSLDSHSA VSGNAQNFQP YAGVQAYAYP QTPSVTSQLQ
PVRPLYPAPL SQAPHFQGSG DMMSFLMTEA RQHNTEIRMA VNKVADKMDH LMTKVEELQK
HSSGNSMLLP SMSVTMETSM IMSNIQRIIQ ENERLKQELL EKSSRIEEQN DKISDLIERN
QRYVEQSNLM MEKRNNSLQT ATENTQARIL HAEQEKAKVT EELAAATAQV SHLQLKMTAH
QKKETELQLQ LTDNLKETDL LRGHVTRLQA DLSELREASE QTQTKFKSEK QSRRQLELKV
TSLEEELTDL RAEKTSLEKN LSERKKKSAQ ERCQAEAEMD EIRKSHQEEL DRLRQLLKKA
RVSTDQAAAE QLTLAQAELQ SQWEAKCEQL LASARDEHLQ QYREVCAQRD AHQQKLALLQ
DECLALQAQI AAFTEQKEHM QRLEKTKSQA PAGRAAADPS EKVKKIMNQV FQSLRGEFEL
EESYDGGTIL RTIMHTIKMV TLQLLNHQEE EEEEEEEEEE EKKPLRPSLE QPGPATPGMP
PAPPSGETQE APEVLPEQVV GETTPLPLQA LPTPENGAQT RKGEPAEAEV PSEIKDSSLP
PQPAGIPAHR VLGPPTSIPP KPPGPVTMDS ESEEMLAADQ RTVQPNGLLG EEHVREVATD
GLLQGNSRRL SLTPDPEKGE PPALDPESQG GEAQPPECKQ AEDVSSSGPR ETLLDTELAS
AAAGTSLRHN QDSQHCSLSG DEEDELFKGA TLKVPRPTAQ PEEEDEDEVS MKGRPPPTPL
FGDDDDDDDD DIGWLG
