UBP2L_MOUSE
ID UBP2L_MOUSE Reviewed; 1107 AA.
AC Q80X50; Q8BIT6; Q8BIW4; Q8BJ01; Q8CIG7; Q8K102; Q9CRT6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ubiquitin-associated protein 2-like {ECO:0000305};
GN Name=Ubap2l {ECO:0000312|MGI:MGI:1921633};
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 2 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND VARIANT
RP SER-374.
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Brain, Eye, Mammary gland, 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND IDENTIFICATION BY
RP 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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625 AND SER-629, AND
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; SER-487; SER-497 AND
RP SER-879, AND 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 [8]
RP FUNCTION.
RX PubMed=25185265; DOI=10.1182/blood-2014-01-548651;
RA Bordeleau M.E., Aucagne R., Chagraoui J., Girard S., Mayotte N.,
RA Bonneil E., Thibault P., Pabst C., Bergeron A., Barabe F., Hebert J.,
RA Sauvageau M., Boutonnet C., Meloche S., Sauvageau G.;
RT "UBAP2L is a novel BMI1-interacting protein essential for hematopoietic
RT stem cell activity.";
RL Blood 124:2362-2369(2014).
RN [9]
RP STRUCTURE BY NMR OF 19-109.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-015, a UBA domain from mouse cDNA.";
RL Submitted (SEP-2005) to the PDB data bank.
CC -!- FUNCTION: Plays an important role in the activity of long-term
CC repopulating hematopoietic stem cells (LT-HSCs) (PubMed:25185265).
CC {ECO:0000269|PubMed:25185265}.
CC -!- SUBUNIT: Interacts with BMI1. Part of a complex consisting of UBAP2L,
CC BMI1 and RNF2. {ECO:0000250|UniProtKB:Q14157}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q80X50-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80X50-2; Sequence=VSP_019418, VSP_019421;
CC Name=3;
CC IsoId=Q80X50-3; Sequence=VSP_019419, VSP_019422;
CC Name=4;
CC IsoId=Q80X50-4; Sequence=VSP_019423;
CC Name=5;
CC IsoId=Q80X50-5; Sequence=VSP_019420;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37777.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK014274; BAB29236.1; -; mRNA.
DR EMBL; AK048286; BAC33295.1; -; mRNA.
DR EMBL; AK079895; BAC37777.1; ALT_FRAME; mRNA.
DR EMBL; AK088702; BAC40514.1; -; mRNA.
DR EMBL; BC023906; AAH23906.1; -; mRNA.
DR EMBL; BC029075; AAH29075.1; -; mRNA.
DR EMBL; BC050910; AAH50910.1; -; mRNA.
DR CCDS; CCDS38498.1; -. [Q80X50-4]
DR CCDS; CCDS50965.1; -. [Q80X50-2]
DR CCDS; CCDS50966.1; -. [Q80X50-5]
DR CCDS; CCDS79960.1; -. [Q80X50-1]
DR RefSeq; NP_001159455.1; NM_001165983.1. [Q80X50-5]
DR RefSeq; NP_001159456.1; NM_001165984.1. [Q80X50-1]
DR RefSeq; NP_001159457.1; NM_001165985.1. [Q80X50-2]
DR RefSeq; NP_001159458.1; NM_001165986.1. [Q80X50-2]
DR RefSeq; NP_082751.1; NM_028475.2. [Q80X50-4]
DR RefSeq; XP_006502235.1; XM_006502172.2. [Q80X50-5]
DR PDB; 1WJ7; NMR; -; A=19-109.
DR PDBsum; 1WJ7; -.
DR AlphaFoldDB; Q80X50; -.
DR SMR; Q80X50; -.
DR BioGRID; 216707; 24.
DR IntAct; Q80X50; 7.
DR MINT; Q80X50; -.
DR STRING; 10090.ENSMUSP00000066138; -.
DR iPTMnet; Q80X50; -.
DR PhosphoSitePlus; Q80X50; -.
DR SwissPalm; Q80X50; -.
DR EPD; Q80X50; -.
DR jPOST; Q80X50; -.
DR MaxQB; Q80X50; -.
DR PaxDb; Q80X50; -.
DR PeptideAtlas; Q80X50; -.
DR PRIDE; Q80X50; -.
DR ProteomicsDB; 298101; -. [Q80X50-1]
DR ProteomicsDB; 298102; -. [Q80X50-2]
DR ProteomicsDB; 298103; -. [Q80X50-3]
DR ProteomicsDB; 298104; -. [Q80X50-4]
DR ProteomicsDB; 298105; -. [Q80X50-5]
DR Antibodypedia; 34148; 203 antibodies from 25 providers.
DR Ensembl; ENSMUST00000029553; ENSMUSP00000029553; ENSMUSG00000042520. [Q80X50-4]
DR Ensembl; ENSMUST00000064639; ENSMUSP00000066138; ENSMUSG00000042520. [Q80X50-5]
DR Ensembl; ENSMUST00000195995; ENSMUSP00000143638; ENSMUSG00000042520. [Q80X50-2]
DR Ensembl; ENSMUST00000196843; ENSMUSP00000143459; ENSMUSG00000042520. [Q80X50-1]
DR Ensembl; ENSMUST00000199834; ENSMUSP00000143254; ENSMUSG00000042520. [Q80X50-2]
DR GeneID; 74383; -.
DR KEGG; mmu:74383; -.
DR UCSC; uc008qal.2; mouse. [Q80X50-4]
DR UCSC; uc008qam.2; mouse. [Q80X50-3]
DR UCSC; uc008qao.2; mouse. [Q80X50-1]
DR UCSC; uc008qap.2; mouse. [Q80X50-5]
DR UCSC; uc008qas.2; mouse. [Q80X50-2]
DR CTD; 9898; -.
DR MGI; MGI:1921633; Ubap2l.
DR VEuPathDB; HostDB:ENSMUSG00000042520; -.
DR eggNOG; ENOG502QPRH; Eukaryota.
DR GeneTree; ENSGT00390000003453; -.
DR InParanoid; Q80X50; -.
DR OMA; PPYNIAG; -.
DR OrthoDB; 234795at2759; -.
DR PhylomeDB; Q80X50; -.
DR TreeFam; TF328468; -.
DR BioGRID-ORCS; 74383; 9 hits in 72 CRISPR screens.
DR ChiTaRS; Ubap2l; mouse.
DR EvolutionaryTrace; Q80X50; -.
DR PRO; PR:Q80X50; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q80X50; protein.
DR Bgee; ENSMUSG00000042520; Expressed in embryonic post-anal tail and 261 other tissues.
DR ExpressionAtlas; Q80X50; baseline and differential.
DR Genevisible; Q80X50; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031519; C:PcG protein complex; ISO:MGI.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:MGI.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI.
DR GO; GO:0034063; P:stress granule assembly; ISS:UniProtKB.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR022166; UBAP2/Lig.
DR Pfam; PF12478; DUF3697; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1107
FT /note="Ubiquitin-associated protein 2-like"
FT /id="PRO_0000240665"
FT DOMAIN 49..89
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 187
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 190
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 487
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14157"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 150
FT /note="F -> CMHGALSKPAVV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019418"
FT VAR_SEQ 235..255
FT /note="RLDFIGVEGSNYPRKFETAPG -> S (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019419"
FT VAR_SEQ 255
FT /note="G -> GMIHPG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019420"
FT VAR_SEQ 989..1107
FT /note="VSVTSSNTGVPDISGSVYSKTQQSFEKQGFHSGTPAASFNLPSALGSGGPIN
FT PATAAAYPPAPFMHILTPHQQPHSQILHHHLQQDGQTGSGQRSQTSSIPQKPQTNKSAY
FT NSYSWGAN -> RKYPPPYKHFWTAES (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019421"
FT VAR_SEQ 1077..1107
FT /note="TGSGQRSQTSSIPQKPQTNKSAYNSYSWGAN -> DILTLVDDQLGE (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019422"
FT VAR_SEQ 1077..1107
FT /note="TGSGQRSQTSSIPQKPQTNKSAYNSYSWGAN -> LPYLQMILCCQRQQEEQ
FT DILTLVDDQLGE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019423"
FT VARIANT 374
FT /note="G -> S (in strain: FVB/N)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT CONFLICT 303
FT /note="D -> G (in Ref. 1; BAC33295)"
FT /evidence="ECO:0000305"
FT CONFLICT 1010
FT /note="Missing (in Ref. 2; AAH23906)"
FT /evidence="ECO:0000305"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:1WJ7"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:1WJ7"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:1WJ7"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:1WJ7"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:1WJ7"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:1WJ7"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1WJ7"
SQ SEQUENCE 1107 AA; 116799 MW; F4A4FB502B619C51 CRC64;
MMTSVGTNRA RGNWEQPQNQ NQTQHKQRPQ ATAEQIRLAQ MISDHNDADF EEKVKQLIDI
TGKNQDECVI ALHDCNGDVN RAINVLLEGN PDTHSWEMVG KKKGVSGQKD GGQTESNEEG
KENRDRDRDY SRRRGGPPRR GRGASRGREF RGQENGLDGT KSGGPSGRGT DRGRRGRGRG
RGSSGRRGGR FSAQGMGTFN PADYAEPANT DDNYGNSSGN TWNNTGHFEP DDGTRLDFIG
VEGSNYPRKF ETAPGAWRTA TEEWGTEDWN EDLSETKIFT ASNVSSVPLP AENVTITAGQ
RIDLAVLLGK TPSSMENDSS NLDPSQAPSL AQPLVFSNSK QNAISQPASG STFSHHSMVS
MLGKGFGDVG EAKGGSTTGS QFLEQFKTAQ ALAQLAAQHS QSGSTTTSSW DMGSTTQSPS
LVQYDLKSAN DSTVHSPFTK RQAFTPSSTM MEVFLQEKPP AVATSTAAPP PPSSPLPSKS
TSAPQMSPGS SDNQSSSPQP AQQKLKQQKK KTSLTSKIPA LAVEMPGSAD ISGLNLQFGA
LQFGSEPVLS DYESTPTTSA SSSQAPSSLY TSTASESSST VSSNQSQESG YQSGPIQSTT
YTSQNNAQGP LYEQRSTQTR RYPSSISSSP QKDLTQAKNG FSSVQATQLQ TTQSVEGATG
SAVKSESPST SSIPSLNETV PAASLLTTAN QHSSSLSGLS HTEEIPNTTT TQHSSALSTQ
QNTLSSSTSS GRTSTSTLLH TSVESEANLH SSSSTFSTTS STVSAPPPVV SVSSSLNSGS
SLGLSLGSNS TVTASTRSSV ATTSGKAPPN LPPGVPPLLP NPYIMAPGLL HAYPPQVYGY
DDLQMLQTRF PLDYYSIPFP TPTTPLTGRD GSLASNPYSG DLTKFGRGDA SSPAPATTLA
QPQQNQTQTH HTTQQTFLNP ALPPGYSYTS LPYYTGVPGL PSTFQYGPAV FPVAPTSSKQ
HGVNVSVNAS ATPFQQPSGY GSHGYNTGVS VTSSNTGVPD ISGSVYSKTQ QSFEKQGFHS
GTPAASFNLP SALGSGGPIN PATAAAYPPA PFMHILTPHQ QPHSQILHHH LQQDGQTGSG
QRSQTSSIPQ KPQTNKSAYN SYSWGAN
