SHRM2_MOUSE
ID SHRM2_MOUSE Reviewed; 1481 AA.
AC A2ALU4; Q2EY23; Q8C7N1; Q8CCR2; Q8CDZ0;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein Shroom2;
DE AltName: Full=Protein Apxl;
GN Name=Shroom2; Synonyms=Apxl;
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] (ISOFORM 1), DEVELOPMENTAL STAGE, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH F-ACTIN, AND FUNCTION.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=16684770; DOI=10.1074/jbc.m512463200;
RA Dietz M.L., Bernaciak T.M., Vendetti F., Kielec J.M., Hildebrand J.D.;
RT "Differential actin-dependent localization modulates the evolutionarily
RT conserved activity of Shroom family proteins.";
RL J. Biol. Chem. 281:20542-20554(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Head, Hippocampus, and Olfactory bulb;
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 NOMENCLATURE.
RX PubMed=16615870; DOI=10.1186/1471-2121-7-18;
RA Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P., Schiaffino M.V.,
RA Smith P., Staub O., Hildebrand J.D., Wallingford J.B.;
RT "A new standard nomenclature for proteins related to Apx and Shroom.";
RL BMC Cell Biol. 7:18-18(2006).
RN [5]
RP FUNCTION.
RX PubMed=16987870; DOI=10.1242/dev.02563;
RA Fairbank P.D., Lee C., Ellis A., Hildebrand J.D., Gross J.M.,
RA Wallingford J.B.;
RT "Shroom2 (APXL) regulates melanosome biogenesis and localization in the
RT retinal pigment epithelium.";
RL Development 133:4109-4118(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236 AND SER-960, AND
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-318; SER-330;
RP SER-935; SER-959; SER-960; SER-962; THR-963 AND SER-1165, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
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).
CC -!- FUNCTION: May be involved in endothelial cell morphology changes during
CC cell spreading. In the retinal pigment epithelium, may regulate the
CC biogenesis of melanosomes and promote their association with the apical
CC cell surface by inducing gamma-tubulin redistribution.
CC {ECO:0000269|PubMed:16684770, ECO:0000269|PubMed:16987870}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000269|PubMed:16684770}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:16684770}. Cell junction, tight junction
CC {ECO:0000269|PubMed:16684770}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16684770}. Note=Associates with cortical F-actin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2ALU4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2ALU4-2; Sequence=VSP_024964;
CC -!- TISSUE SPECIFICITY: Present in kidney tubules and in the vasculature of
CC many tissues (at protein level). {ECO:0000269|PubMed:16684770}.
CC -!- DEVELOPMENTAL STAGE: Present in the vasculature and in multiple
CC epithelial populations at 10.5 dpc. Present in the cell junctions of
CC the retinal pigmented epithelium at 15.5 dpc (at protein level).
CC {ECO:0000269|PubMed:16684770}.
CC -!- DOMAIN: The ASD1 domain mediates F-actin binding.
CC -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD19518.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC26404.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC27781.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ358971; ABD19518.1; ALT_FRAME; mRNA.
DR EMBL; AK029338; BAC26404.1; ALT_INIT; mRNA.
DR EMBL; AK032256; BAC27781.1; ALT_INIT; mRNA.
DR EMBL; AK049850; BAC33957.1; -; mRNA.
DR EMBL; AL805960; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL807777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS72455.1; -. [A2ALU4-1]
DR RefSeq; NP_001277613.1; NM_001290684.1. [A2ALU4-1]
DR RefSeq; NP_001277614.1; NM_001290685.1.
DR RefSeq; NP_001277615.1; NM_001290686.1. [A2ALU4-2]
DR RefSeq; NP_001277616.1; NM_001290687.1. [A2ALU4-2]
DR RefSeq; NP_766029.2; NM_172441.3.
DR RefSeq; XP_011246074.1; XM_011247772.1.
DR RefSeq; XP_011246075.1; XM_011247773.1.
DR RefSeq; XP_011246076.1; XM_011247774.2. [A2ALU4-2]
DR RefSeq; XP_011246077.1; XM_011247775.2. [A2ALU4-2]
DR RefSeq; XP_011246078.1; XM_011247776.2.
DR RefSeq; XP_011246079.1; XM_011247777.2. [A2ALU4-2]
DR AlphaFoldDB; A2ALU4; -.
DR SMR; A2ALU4; -.
DR BioGRID; 225549; 8.
DR STRING; 10090.ENSMUSP00000098701; -.
DR iPTMnet; A2ALU4; -.
DR PhosphoSitePlus; A2ALU4; -.
DR MaxQB; A2ALU4; -.
DR PaxDb; A2ALU4; -.
DR PeptideAtlas; A2ALU4; -.
DR PRIDE; A2ALU4; -.
DR ProteomicsDB; 257162; -. [A2ALU4-1]
DR ProteomicsDB; 257163; -. [A2ALU4-2]
DR Antibodypedia; 23655; 176 antibodies from 26 providers.
DR Ensembl; ENSMUST00000062317; ENSMUSP00000057500; ENSMUSG00000045180. [A2ALU4-1]
DR GeneID; 110380; -.
DR KEGG; mmu:110380; -.
DR UCSC; uc009uqj.2; mouse. [A2ALU4-2]
DR UCSC; uc009uqm.2; mouse. [A2ALU4-1]
DR CTD; 357; -.
DR MGI; MGI:107194; Shroom2.
DR VEuPathDB; HostDB:ENSMUSG00000045180; -.
DR eggNOG; ENOG502QUU2; Eukaryota.
DR GeneTree; ENSGT00940000155212; -.
DR HOGENOM; CLU_003220_0_0_1; -.
DR InParanoid; A2ALU4; -.
DR OrthoDB; 29607at2759; -.
DR BioGRID-ORCS; 110380; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Shroom2; mouse.
DR PRO; PR:A2ALU4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A2ALU4; protein.
DR Bgee; ENSMUSG00000045180; Expressed in superior colliculus and 213 other tissues.
DR ExpressionAtlas; A2ALU4; baseline and differential.
DR Genevisible; A2ALU4; MM.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0045176; P:apical protein localization; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0043010; P:camera-type eye development; ISS:UniProtKB.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0045217; P:cell-cell junction maintenance; IDA:MGI.
DR GO; GO:0043482; P:cellular pigment accumulation; ISS:UniProtKB.
DR GO; GO:0043583; P:ear development; ISS:UniProtKB.
DR GO; GO:0032401; P:establishment of melanosome localization; ISS:UniProtKB.
DR GO; GO:0008057; P:eye pigment granule organization; ISS:UniProtKB.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; ISS:UniProtKB.
DR GO; GO:0032438; P:melanosome organization; IMP:UniProtKB.
DR GO; GO:0030835; P:negative regulation of actin filament depolymerization; IDA:MGI.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR014800; ASD1_dom.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR027686; Shroom2.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 2.
DR PANTHER; PTHR15012:SF8; PTHR15012:SF8; 2.
DR Pfam; PF08688; ASD1; 1.
DR Pfam; PF08687; ASD2; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51306; ASD1; 1.
DR PROSITE; PS51307; ASD2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Cell membrane;
KW Cytoplasm; Cytoskeleton; Developmental protein; Membrane; Microtubule;
KW Phosphoprotein; Reference proteome; Tight junction.
FT CHAIN 1..1481
FT /note="Protein Shroom2"
FT /id="PRO_0000286063"
FT DOMAIN 26..108
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 705..807
FT /note="ASD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00637"
FT DOMAIN 1185..1476
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 959
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 963
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TP36"
FT MOD_RES 1043
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TP36"
FT MOD_RES 1165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..1035
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024964"
FT CONFLICT 274
FT /note="F -> S (in Ref. 2; ABD19518)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="P -> S (in Ref. 2; ABD19518)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="R -> C (in Ref. 2; ABD19518)"
FT /evidence="ECO:0000305"
FT CONFLICT 1012
FT /note="N -> K (in Ref. 2; BAC27781)"
FT /evidence="ECO:0000305"
FT CONFLICT 1100
FT /note="A -> S (in Ref. 2; ABD19518)"
FT /evidence="ECO:0000305"
FT CONFLICT 1227
FT /note="E -> K (in Ref. 2; ABD19518)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1481 AA; 164703 MW; 3C5C96100263E393 CRC64;
MEGAEPRARP ERLAEAEAPA TDGVRLVEVQ LSGGAPWGFT LKGGREHGEP LVITKIEEGS
KAAAVDKLLA GDEIVAINDV SLSGFRQEAI CLVKGSHKTL KLVVKRKSDP SWRPHSWHAT
KYFDVHPEPA ASLFLNTSGS PSWKSQHQAS SSSHDLSGSW EHTSLQRTSD HFSSMGSIDS
LDHSSQLYPS GHLSSAKSNS SIDHLGGHSK RDSAYGSFST CSSTPDHTLP KADASSTENI
LYKVGLWEAS RPGSSRQSQS TGDPQGLQDR PSCFIPRVPG NSSKSPRPED NVEPKIATHG
RSNFGPVWYV PDKKKAPSPP PLGLPLRSDS FSVAARGHEK ARGPPFSDLA SMQHFITLPH
VQPRGDHRME TTDRQWKLTH LSSGKEIGNV GYQSEGHLDC RWLCSDDRAG RPSGPPGRLQ
FSDVHFLKSY HGSQHQQQCS DESPRAPSSP RELLHITPGG GLQEPPEPSQ DDNPTQVRWP
GSAHQKLDDR GRSHYFPGSL RQPVQGSAQV VIPRGDYWHS DTTPVDLEYP LLRPVGQRTY
LQQHEETPAS HEKEGYHQLN AGIEGCCSGI QEPPRASRTV RTGLQCPSND FKLVDGESGR
ISRQRTPMLH SLTQDGTWRP GNSKDCGNDK PPLFDAQVGK PTRRSDRFAT TLRNEIQMRR
AKLQKSKSTV TLAGDSEAED CAGDWRADVG AVPEGSFPST YKEHLKEAQT RVLKATSFQR
RDLDPTPADQ YSGPSEHRTF DHSASSSLSS FPGEPDSAPR FCETGLAKAP SSGVGVPHVL
RIGGRKRFTA EQKLKSYSEP EKINEVGLSG DHRPHPTVRT PEDTVGTFAD RWKFFEETSK
SLLQKAGHRQ VHCGLPREKA ERPQTGHHEC ESTEPWFQKR SLATSCGEIL SDRKVEKASE
KLNPPRRLGT FAEYQASWKE QKKPLEARSS GRYHSADDIL DAGLDQQQRP QYIHERSRSS
PSTDHYSQEV PVEPNRQAED SGDHKEAILC TLQAEEGCSA PSAQPQDSQH VNEDTTFPQP
ETQLSSKCQH LQTSAMETSR SPSPQFAPQK LTDKPPLLIH EDNSARIERV MDNNTTVKMV
PIKIVHSESQ PEKESRQSLA CPAELPPLPS GLERDQIKTL STSEQCYSRF CVYTRQEVEA
PHRARPPEPR PPSTPAPPVR DSCSSPPSLN YGKAKEKTMD DLKSEELARE IVGKDKSLAD
ILDPSVKIKT TMDLMEGIFP KDEYLLEEAQ QRRKLLPKVP LPRVTEDKKQ DPGMPGVVSL
ATNSTYYSTS APKAELLIKM KDLQEPEEYS AGDLDHDLSV KKQELIDSIS RKLQVLREAR
ESLLEDIQAN NALGDEVEAI VKDVCKPNEF DKFRMFIGDL DKVVNLLLSL SGRLARVENA
LNNLDDNPSP GDRQSLLEKQ RVLTQQHEDA KELKENLDRR ERIVFDILAT YLSEENLADY
EHFVKMKSAL IIEQRELEDK IHLGEEQLKC LFDSLQPERS K
