VP26B_MOUSE
ID VP26B_MOUSE Reviewed; 336 AA.
AC Q8C0E2; Q3TN45; Q8K2V3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Vacuolar protein sorting-associated protein 26B;
DE AltName: Full=Vesicle protein sorting 26B;
GN Name=Vps26b;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Brain, Mammary tumor, and Olfactory epithelium;
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH VPS35.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-319, 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 [5]
RP FUNCTION, AND 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [7]
RP FUNCTION, SUBUNIT, INTERACTION WITH TBC1D5 AND GOLPH3, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
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 [8]
RP FUNCTION, INTERACTION WITH SNX27, AND MUTAGENESIS OF ASP-42 AND LEU-152.
RX PubMed=25136126; DOI=10.1073/pnas.1410552111;
RA Gallon M., Clairfeuille T., Steinberg F., Mas C., Ghai R., Sessions R.B.,
RA Teasdale R.D., Collins B.M., Cullen P.J.;
RT "A unique PDZ domain and arrestin-like fold interaction reveals mechanistic
RT details of endocytic recycling by SNX27-retromer.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E3604-E3613(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 7-336, SUBUNIT, MUTAGENESIS OF
RP LEU-197; ARG-199; 233-ILE-MET-234; 240-ARG--GLU-242; PRO-245 AND ARG-247,
RP AND SUBCELLULAR LOCATION.
RX PubMed=18088321; DOI=10.1111/j.1600-0854.2007.00688.x;
RA Collins B.M., Norwood S.J., Kerr M.C., Mahony D., Seaman M.N.,
RA Teasdale R.D., Owen D.J.;
RT "Structure of Vps26B and mapping of its interaction with the retromer
RT protein complex.";
RL Traffic 9:366-379(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 7-336, AND 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).
CC -!- FUNCTION: Acts as component of the retromer cargo-selective complex
CC (CSC) (PubMed:21040701, PubMed:21920005). The CSC is believed to be the
CC core functional component of retromer or respective retromer complex
CC variants acting to prevent missorting of selected transmembrane cargo
CC proteins into the lysosomal degradation pathway. The recruitment of the
CC CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR
CC retromer mediates retrograde transport of cargo proteins from endosomes
CC to the trans-Golgi network (TGN) and is involved in endosome-to-plasma
CC membrane transport for cargo protein recycling. The SNX3-retromer
CC mediates the retrograde transport of WLS distinct from the SNX-BAR
CC retromer pathway. The SNX27-retromer is believed to be involved in
CC endosome-to-plasma membrane trafficking and recycling of a broad
CC spectrum of cargo proteins. The CSC seems to act as recruitment hub for
CC other proteins, such as the WASH complex and TBC1D5 (By similarity).
CC May be involved in retrograde transport of SORT1 but not of IGF2R
CC (PubMed:21040701). Acts redundantly with VSP26A in SNX-27 mediated
CC endocytic recycling of SLC2A1/GLUT1 (PubMed:25136126).
CC {ECO:0000250|UniProtKB:O75436, ECO:0000269|PubMed:21040701,
CC ECO:0000269|PubMed:21920005, ECO:0000269|PubMed:25136126}.
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
CC (PubMed:21040701, PubMed:21920005, PubMed:18088321, PubMed:20875039).
CC The CSC has a highly elongated structure with VPS26 and VPS29 binding
CC independently at opposite distal ends of VPS35 as central platform
CC (Probable). The CSC is believed to associate with variable sorting
CC nexins to form functionally distinct retromer complex variants. The
CC originally described SNX-BAR retromer is a pentamer containing the CSC
CC and a heterodimeric membrane-deforming subcomplex formed between SNX1
CC or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the
CC respective CSC and SNX-BAR subcomplexes associate with low affinity.
CC The CSC associates with SNX3 to form a SNX3-retromer complex. The CSC
CC associates with SNX27, the WASH complex and the SNX-BAR subcomplex to
CC form the SNX27-retromer complex (By similarity). Interacts with VPS29,
CC VPS35, TBC1D5, GOLPH3, SNX27 (PubMed:16190980, PubMed:21040701,
CC PubMed:21920005, PubMed:25136126). {ECO:0000250|UniProtKB:O75436,
CC ECO:0000269|PubMed:16190980, ECO:0000269|PubMed:18088321,
CC ECO:0000269|PubMed:20875039, ECO:0000269|PubMed:21040701,
CC ECO:0000269|PubMed:21920005, ECO:0000269|PubMed:25136126,
CC ECO:0000303|PubMed:20875039}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16190980}. Membrane
CC {ECO:0000269|PubMed:16190980}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16190980}. Early endosome
CC {ECO:0000269|PubMed:21920005}. Late endosome
CC {ECO:0000269|PubMed:21920005}. Note=Endosomal localization is reported
CC controversially. Does not localize to endosomes (PubMed:16190980).
CC Localizes to early and late endosomal structures (PubMed:21920005,
CC PubMed:18088321). {ECO:0000269|PubMed:16190980,
CC ECO:0000269|PubMed:18088321, ECO:0000269|PubMed:21920005}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C0E2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0E2-2; Sequence=VSP_019927;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in developing embryo and
CC adult. Highly expressed in brain. {ECO:0000269|PubMed:16190980,
CC ECO:0000269|PubMed:21920005}.
CC -!- SIMILARITY: Belongs to the VPS26 family. {ECO:0000305}.
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DR EMBL; AK031589; BAC27465.1; -; mRNA.
DR EMBL; AK150929; BAE29967.1; -; mRNA.
DR EMBL; AK155578; BAE33333.1; -; mRNA.
DR EMBL; AK165539; BAE38244.1; -; mRNA.
DR EMBL; AK171154; BAE42279.1; -; mRNA.
DR EMBL; BC029758; AAH29758.1; -; mRNA.
DR EMBL; BC049180; AAH49180.1; -; mRNA.
DR EMBL; BC052721; AAH52721.1; -; mRNA.
DR EMBL; BC062972; AAH62972.1; -; mRNA.
DR CCDS; CCDS22938.1; -. [Q8C0E2-1]
DR RefSeq; NP_821170.1; NM_178027.4. [Q8C0E2-1]
DR PDB; 2R51; X-ray; 2.10 A; A=7-336.
DR PDB; 3LH8; X-ray; 2.60 A; A/B=7-336.
DR PDB; 3LH9; X-ray; 2.40 A; A/B=7-336.
DR PDB; 3LHA; X-ray; 2.80 A; A/B=7-336.
DR PDBsum; 2R51; -.
DR PDBsum; 3LH8; -.
DR PDBsum; 3LH9; -.
DR PDBsum; 3LHA; -.
DR AlphaFoldDB; Q8C0E2; -.
DR SMR; Q8C0E2; -.
DR BioGRID; 213223; 10.
DR IntAct; Q8C0E2; 6.
DR MINT; Q8C0E2; -.
DR STRING; 10090.ENSMUSP00000034470; -.
DR iPTMnet; Q8C0E2; -.
DR PhosphoSitePlus; Q8C0E2; -.
DR SwissPalm; Q8C0E2; -.
DR EPD; Q8C0E2; -.
DR jPOST; Q8C0E2; -.
DR MaxQB; Q8C0E2; -.
DR PaxDb; Q8C0E2; -.
DR PeptideAtlas; Q8C0E2; -.
DR PRIDE; Q8C0E2; -.
DR ProteomicsDB; 297577; -. [Q8C0E2-1]
DR ProteomicsDB; 297578; -. [Q8C0E2-2]
DR Antibodypedia; 33166; 128 antibodies from 26 providers.
DR DNASU; 69091; -.
DR Ensembl; ENSMUST00000034470; ENSMUSP00000034470; ENSMUSG00000031988. [Q8C0E2-1]
DR GeneID; 69091; -.
DR KEGG; mmu:69091; -.
DR UCSC; uc009oqd.2; mouse. [Q8C0E2-1]
DR UCSC; uc009oqf.2; mouse. [Q8C0E2-2]
DR CTD; 112936; -.
DR MGI; MGI:1917656; Vps26b.
DR VEuPathDB; HostDB:ENSMUSG00000031988; -.
DR eggNOG; KOG3063; Eukaryota.
DR GeneTree; ENSGT00950000183064; -.
DR HOGENOM; CLU_031077_0_0_1; -.
DR InParanoid; Q8C0E2; -.
DR OMA; LWVHSYR; -.
DR OrthoDB; 987411at2759; -.
DR PhylomeDB; Q8C0E2; -.
DR TreeFam; TF300907; -.
DR BioGRID-ORCS; 69091; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Vps26b; mouse.
DR EvolutionaryTrace; Q8C0E2; -.
DR PRO; PR:Q8C0E2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8C0E2; protein.
DR Bgee; ENSMUSG00000031988; Expressed in ascending aorta and 259 other tissues.
DR Genevisible; Q8C0E2; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0030904; C:retromer complex; IDA:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR Gene3D; 2.60.40.640; -; 2.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR028934; Vps26-related.
DR PANTHER; PTHR12233; PTHR12233; 1.
DR Pfam; PF03643; Vps26; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Endosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..336
FT /note="Vacuolar protein sorting-associated protein 26B"
FT /id="PRO_0000247090"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT VAR_SEQ 243..336
FT /note="SIPIRLFLAGYELTPTMRDINKKFSVRYYLNLVLIDEEERRYFKQQEVVLWR
FT KGDIVRKSMSHQAAIASQRFEGTTSLGEVRTPGQLSDNNSRQ -> PPGLGPLSLCSQT
FT TCSVSALGKGSNFEVKSLFYFIYLFIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019927"
FT MUTAGEN 42
FT /note="D->A: Disrupts interaction with SNX27."
FT /evidence="ECO:0000269|PubMed:25136126"
FT MUTAGEN 152
FT /note="L->A: Disrupts interaction with SNX27."
FT /evidence="ECO:0000269|PubMed:25136126"
FT MUTAGEN 197
FT /note="L->S: No endosomal localization; no effect on
FT interaction with VPS35:VPS29 dimer; when associated with E-
FT 199."
FT /evidence="ECO:0000269|PubMed:18088321"
FT MUTAGEN 199
FT /note="R->E: No endosomal localization; no effect on
FT interaction with VPS35:VPS29 dimer; when associated with S-
FT 197."
FT /evidence="ECO:0000269|PubMed:18088321"
FT MUTAGEN 233..234
FT /note="IM->DN: Disrupts interaction with VPS35:VPS29 dimer;
FT no endosomal localization."
FT /evidence="ECO:0000269|PubMed:18088321"
FT MUTAGEN 240..242
FT /note="RGE->SAS: No endosomal localization; no effect on
FT interaction with VPS35:VPS29 dimer."
FT /evidence="ECO:0000269|PubMed:18088321"
FT MUTAGEN 245
FT /note="P->S: Disrupts interaction with VPS35:VPS29 dimer;
FT no endosomal localization; when associated with S-247."
FT /evidence="ECO:0000269|PubMed:18088321"
FT MUTAGEN 247
FT /note="R->S: Disrupts interaction with VPS35:VPS29 dimer;
FT no endosomal localization; when associated with S-245."
FT /evidence="ECO:0000269|PubMed:18088321"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:2R51"
FT TURN 17..21
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3LH8"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 66..76
FT /evidence="ECO:0007829|PDB:2R51"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 122..134
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:2R51"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 202..217
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 220..236
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:2R51"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:2R51"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 266..278
FT /evidence="ECO:0007829|PDB:2R51"
FT STRAND 283..293
FT /evidence="ECO:0007829|PDB:2R51"
SQ SEQUENCE 336 AA; 39125 MW; AD5395AF30900018 CRC64;
MSFFGFGQSV EVEILLNDAE SRKRAEHKTE DGKKEKYFLF YDGETVSGKV SLSLKNPNKR
LEHQGIKIEF IGQIELYYDR GNHHEFVSLV KDLARPGEIT QSQAFDFEFT HVEKPYESYT
GQNVKLRYFL RATISRRLND VVKEMDIVVH TLSTYPELNS SIKMEVGIED CLHIEFEYNK
SKYHLKDVIV GKIYFLLVRI KIKHMEIDII KRETTGTGPN VYHENDTIAK YEIMDGAPVR
GESIPIRLFL AGYELTPTMR DINKKFSVRY YLNLVLIDEE ERRYFKQQEV VLWRKGDIVR
KSMSHQAAIA SQRFEGTTSL GEVRTPGQLS DNNSRQ
