K1522_MOUSE
ID K1522_MOUSE Reviewed; 1013 AA.
AC A2A7S8; A2A7S9; Q3U356; Q3U437; Q3V3N0; Q6ZPN9; Q8K0K8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Uncharacterized protein KIAA1522;
GN Name=Kiaa1522;
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] (ISOFORM 4).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
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] OF 817-1013.
RC STRAIN=FVB/N; TISSUE=Colon;
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 IDENTIFICATION 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., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108, 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 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-610 AND SER-909,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 (ISOFORM 2), 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-213; SER-325;
RP SER-328; SER-402; SER-407; THR-529; SER-543; SER-838; SER-842; SER-909;
RP SER-952 AND SER-959, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17
RP (ISOFORM 2), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, and Pancreas;
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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-318, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A2A7S8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2A7S8-2; Sequence=VSP_029460;
CC Name=3;
CC IsoId=A2A7S8-3; Sequence=VSP_029459;
CC Name=4;
CC IsoId=A2A7S8-4; Sequence=VSP_029461;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98192.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129382; BAC98192.1; ALT_INIT; mRNA.
DR EMBL; AK038020; BAE20526.1; -; mRNA.
DR EMBL; AK154456; BAE32598.1; -; mRNA.
DR EMBL; AK154932; BAE32933.1; -; mRNA.
DR EMBL; AL606977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031163; AAH31163.1; -; mRNA.
DR CCDS; CCDS18686.1; -. [A2A7S8-2]
DR CCDS; CCDS71474.1; -. [A2A7S8-1]
DR CCDS; CCDS71475.1; -. [A2A7S8-4]
DR RefSeq; NP_001028361.1; NM_001033189.3. [A2A7S8-2]
DR RefSeq; NP_001272794.1; NM_001285865.1. [A2A7S8-4]
DR RefSeq; NP_001272795.1; NM_001285866.1. [A2A7S8-1]
DR RefSeq; NP_001272796.1; NM_001285867.1. [A2A7S8-3]
DR AlphaFoldDB; A2A7S8; -.
DR BioGRID; 220616; 1.
DR IntAct; A2A7S8; 1.
DR MINT; A2A7S8; -.
DR STRING; 10090.ENSMUSP00000062395; -.
DR iPTMnet; A2A7S8; -.
DR PhosphoSitePlus; A2A7S8; -.
DR jPOST; A2A7S8; -.
DR MaxQB; A2A7S8; -.
DR PaxDb; A2A7S8; -.
DR PRIDE; A2A7S8; -.
DR ProteomicsDB; 268924; -. [A2A7S8-1]
DR ProteomicsDB; 268925; -. [A2A7S8-2]
DR ProteomicsDB; 268926; -. [A2A7S8-3]
DR ProteomicsDB; 268927; -. [A2A7S8-4]
DR Antibodypedia; 31358; 45 antibodies from 13 providers.
DR Ensembl; ENSMUST00000052602; ENSMUSP00000062395; ENSMUSG00000050390. [A2A7S8-2]
DR Ensembl; ENSMUST00000097873; ENSMUSP00000095483; ENSMUSG00000050390. [A2A7S8-4]
DR Ensembl; ENSMUST00000106051; ENSMUSP00000101666; ENSMUSG00000050390. [A2A7S8-1]
DR GeneID; 97130; -.
DR KEGG; mmu:97130; -.
DR UCSC; uc008uwl.2; mouse. [A2A7S8-1]
DR UCSC; uc008uwm.2; mouse. [A2A7S8-4]
DR UCSC; uc008uwn.1; mouse. [A2A7S8-2]
DR CTD; 97130; -.
DR MGI; MGI:2140651; C77080.
DR VEuPathDB; HostDB:ENSMUSG00000050390; -.
DR eggNOG; ENOG502QV6M; Eukaryota.
DR GeneTree; ENSGT00950000182963; -.
DR HOGENOM; CLU_004158_0_0_1; -.
DR InParanoid; A2A7S8; -.
DR OMA; KEPVGCN; -.
DR OrthoDB; 315746at2759; -.
DR PhylomeDB; A2A7S8; -.
DR TreeFam; TF333323; -.
DR BioGRID-ORCS; 97130; 1 hit in 71 CRISPR screens.
DR ChiTaRS; C77080; mouse.
DR PRO; PR:A2A7S8; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; A2A7S8; protein.
DR Bgee; ENSMUSG00000050390; Expressed in lacrimal gland and 165 other tissues.
DR ExpressionAtlas; A2A7S8; baseline and differential.
DR Genevisible; A2A7S8; MM.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
PE 1: Evidence at protein level;
KW Alternative splicing; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..1013
FT /note="Uncharacterized protein KIAA1522"
FT /id="PRO_0000311247"
FT REGION 20..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 330..1013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..613
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..718
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..964
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 108
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 160
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 318
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 529
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 591
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 848
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P206"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 952
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 959
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..113
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029459"
FT VAR_SEQ 1..18
FT /note="MVVFLGRHLPALLEVFKK -> MAARAPPAAPAADEPGSPGGPPRRKKSRSG
FT LRRAFSWLRGKRRKKKAAGAEGAESTASRAKKADDKAKRAKGKSR (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029460"
FT VAR_SEQ 1..18
FT /note="MVVFLGRHLPALLEVFKK -> MGNSHHKRKAPSGPRTRSFWRFGRSAKRPA
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_029461"
FT CONFLICT 221
FT /note="T -> P (in Ref. 2; BAE20526)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="I -> L (in Ref. 2; BAE20526)"
FT /evidence="ECO:0000305"
FT MOD_RES A2A7S8-2:17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1013 AA; 104842 MW; 0E7A98C1A1D4382F CRC64;
MVVFLGRHLP ALLEVFKKGS AKAESDNRQG AGPSQGPGSV GDELQDNVFF PSGRPPHLEE
LHTQAQEGLR SLQHQERQKL SKGGWDHGDT QSIQSSQTGP DEDTISIYSQ KSYMTESSTA
EDALSVRSEM IQRRGSTFRP HDSFPKSGKS GRRRRERRST VLGLPQHVQK ELGLRNNREA
PGTPQPPGSR DAVRIPTVDG RPGLALGTGV RVSLQALEAE TEAGTDAEAV IQRHIDRVYH
DDTLVGRSTG ARPPPLTRPM SLAVPGLTGG AGSPEPLSPA MSISPQATYL SKLIPHAVLP
PTVDVVALGR SSLRTLSRCS LLSASPASVR SLGRFSSASS PRPRSRNASS SSDNWSHSQS
SETIVSDGST LSSKGGSEGQ PEGSVASNNV APPPPGGSGR GSPSGGSTAE TSDTASIRSS
GQLSGRSVSL RKMKRPPPPP RRTYSLHQRG SAVPDGPLGL PPKPERKQQP QLPRPPTAGG
SSGVGAVSCP PSSAGTWGSG LSPGGSRRPP RSPERTLSPS SGYSSQSGTP TLPPKGLAVA
PASPGKAQPP KPDRVTSLRS PGASVSSSLT SLCSSSSDPT PLDRSGPQMS TPLSDRFVIP
PHPKVPAPFS PPPSKSKSSN QAAPVLAAPA VAPGQVSTID TSPASPSMPQ TTLTPAQESP
VASKDESPPP SPPPSYHPPP PPTKKPEVLE EAPPPPEAAV EILPDPSWPP PPPPAPEEQD
LSMADFPPPE EVFFNAGPEL GPLESCSSEA AVPPAASLSQ TPPPAPPPSS GSEPLARLPQ
KDSVGKHSGA PREDSGTPLV TPSLLQMVRL RSVGASTGIP NPSPGSSAPQ KPLRRALSGR
ASPVTAPSSG LHAAVRLKAS SLAASESPAS ALPTGIPEAE PRSPQSPASK ASFIFSKGTK
KLQLERPVSP EAQADLQRNL VAELRSISEH RPPPQAQKKP SKAPPPVARK PSVGVPPPSP
SLPRTESLTA PSTNGLPHAE DRTNGELAEN GGVQLAATEK MGSPGSDPQK KLV
