AGRE5_MOUSE
ID AGRE5_MOUSE Reviewed; 818 AA.
AC Q9Z0M6; Q923A1; Q9CVI5; Q9JLQ8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 2.
DT 25-MAY-2022, entry version 177.
DE RecName: Full=Adhesion G protein-coupled receptor E5 {ECO:0000312|MGI:MGI:1347095};
DE AltName: Full=Leukocyte antigen CD97 {ECO:0000250|UniProtKB:P48960};
DE AltName: CD_antigen=CD97;
DE Contains:
DE RecName: Full=Adhesion G protein-coupled receptor E5 subunit alpha;
DE Contains:
DE RecName: Full=Adhesion G protein-coupled receptor E5 subunit beta;
DE Flags: Precursor;
GN Name=Adgre5 {ECO:0000312|MGI:MGI:1347095};
GN Synonyms=Cd97 {ECO:0000312|MGI:MGI:1347095};
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] (ISOFORMS 1; 2 AND 3).
RX PubMed=10744645; DOI=10.1093/intimm/12.4.439;
RA Hamann J., van Zventer C., Bijl A., Molenaar C., Tesselaar K.,
RA van Lier R.A.W.;
RT "Molecular cloning and characterization of mouse CD97.";
RL Int. Immunol. 12:439-448(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INTERACTION WITH DAF, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=10540231; DOI=10.1046/j.1365-2567.1999.00859.x;
RA Qian Y.-M., Haino M., Kelly K., Song W.-C.;
RT "Structural characterization of mouse CD97 and study of its specific
RT interaction with the murine decay-accelerating factor (DAF, CD55).";
RL Immunology 98:303-311(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 607-818.
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
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 [5]
RP FUNCTION.
RX PubMed=14707087; DOI=10.4049/jimmunol.172.2.1125;
RA Leemans J.C., te Velde A.A., Florquin S., Bennink R.J., de Bruin K.,
RA van Lier R.A.W., van der Poll T., Hamann J.;
RT "The epidermal growth factor-seven transmembrane (EGF-TM7) receptor CD97 is
RT required for neutrophil migration and host defense.";
RL J. Immunol. 172:1125-1131(2004).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299; ASN-395 AND ASN-461.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299 AND ASN-395.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-814, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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: Receptor potentially involved in both adhesion and signaling
CC processes early after leukocyte activation. Plays an essential role in
CC leukocyte migration. {ECO:0000269|PubMed:14707087}.
CC -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC region (alpha subunit) non-covalently linked to a seven-transmembrane
CC moiety (beta subunit). Interacts with complement decay-accelerating
CC factor (DAF). The largest isoform (isoform 1) do not interact with DAF.
CC Interacts also with chondroitin sulfate (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10540231};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Adhesion G protein-coupled receptor E5 subunit
CC alpha]: Secreted, extracellular space {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=EGF(1,2,X,3,4);
CC IsoId=Q9Z0M6-1; Sequence=Displayed;
CC Name=2; Synonyms=EGF(1,2,4);
CC IsoId=Q9Z0M6-2; Sequence=VSP_009413;
CC Name=3; Synonyms=EGF(1,2,3,4);
CC IsoId=Q9Z0M6-3; Sequence=VSP_009414;
CC -!- TISSUE SPECIFICITY: Although predominantly expressed by cells of the
CC immune system, expressed ubiquitously with particularly high levels of
CC expression in the lung and the thymus gland. In the spleen, expression
CC is detected on most myeloid cells and variable portions of T-cells, B-
CC cells and NK cells. In the bone marrow, expressed in nearly all myeloid
CC cells, whereas little if any expression is found on erythroid cells.
CC -!- INDUCTION: Up-regulated during lymphocyte activation.
CC -!- DOMAIN: The first two EGF domains mediate the interaction with DAF. A
CC third tandemly arranged EGF domain is necessary for the structural
CC integrity of the binding region (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Binding to chondroitin sulfate is mediated by the fourth EGF
CC domain. {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular alpha
CC subunit and a seven-transmembrane subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000305}.
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DR EMBL; Y18365; CAB38246.1; -; mRNA.
DR EMBL; AF146344; AAF67800.1; -; mRNA.
DR EMBL; BC006676; AAH06676.1; -; mRNA.
DR EMBL; AK008101; BAB25461.1; -; mRNA.
DR CCDS; CCDS22461.1; -. [Q9Z0M6-1]
DR CCDS; CCDS52610.1; -. [Q9Z0M6-2]
DR CCDS; CCDS52611.1; -. [Q9Z0M6-3]
DR RefSeq; NP_001156501.1; NM_001163029.1.
DR AlphaFoldDB; Q9Z0M6; -.
DR BioGRID; 204924; 13.
DR STRING; 10090.ENSMUSP00000075240; -.
DR MEROPS; P02.033; -.
DR GlyGen; Q9Z0M6; 7 sites.
DR iPTMnet; Q9Z0M6; -.
DR PhosphoSitePlus; Q9Z0M6; -.
DR CPTAC; non-CPTAC-3898; -.
DR EPD; Q9Z0M6; -.
DR MaxQB; Q9Z0M6; -.
DR PaxDb; Q9Z0M6; -.
DR PRIDE; Q9Z0M6; -.
DR ProteomicsDB; 265634; -. [Q9Z0M6-1]
DR ProteomicsDB; 265635; -. [Q9Z0M6-2]
DR ProteomicsDB; 265636; -. [Q9Z0M6-3]
DR DNASU; 26364; -.
DR GeneID; 26364; -.
DR KEGG; mmu:26364; -.
DR CTD; 976; -.
DR MGI; MGI:1347095; Adgre5.
DR eggNOG; KOG4193; Eukaryota.
DR InParanoid; Q9Z0M6; -.
DR PhylomeDB; Q9Z0M6; -.
DR Reactome; R-MMU-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 26364; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q9Z0M6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z0M6; protein.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; TAS:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0031256; C:leading edge membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0035374; F:chondroitin sulfate binding; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR Gene3D; 2.60.220.50; -; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR003056; GPCR_2_ADGRE2_ADGRE5.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR000203; GPS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF01825; GPS; 1.
DR PRINTS; PR01278; CD97PROTEIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00303; GPS; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Disulfide bond; EGF-like domain; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Secreted;
KW Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..818
FT /note="Adhesion G protein-coupled receptor E5"
FT /id="PRO_0000012869"
FT CHAIN 24..513
FT /note="Adhesion G protein-coupled receptor E5 subunit
FT alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000435126"
FT CHAIN 514..818
FT /note="Adhesion G protein-coupled receptor E5 subunit beta"
FT /evidence="ECO:0000250"
FT /id="PRO_0000435127"
FT TOPO_DOM 24..533
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 563..583
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 584..602
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..623
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..658
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 659..679
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..700
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 701..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 745..752
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..773
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 774..818
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..68
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 69..119
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 165..213
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 214..261
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 479..524
FT /note="GPS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00098"
FT REGION 799..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 513..514
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 798
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48960"
FT MOD_RES 808
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48960"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48960"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 35..47
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 49..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 73..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 80..95
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 97..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 169..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 176..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 193..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 218..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 225..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 242..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 120..213
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10540231,
FT ECO:0000303|PubMed:10744645, ECO:0000303|PubMed:15489334"
FT /id="VSP_009413"
FT VAR_SEQ 120..164
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10540231,
FT ECO:0000303|PubMed:10744645"
FT /id="VSP_009414"
FT CONFLICT 3
FT /note="G -> S (in Ref. 1; CAB38246)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="S -> I (in Ref. 1; CAB38246)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="Q -> E (in Ref. 3; AAH06676)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="F -> S (in Ref. 2; AAF67800)"
FT /evidence="ECO:0000305"
FT CONFLICT 599
FT /note="M -> V (in Ref. 3; AAH06676)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="A -> S (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 796
FT /note="F -> I (in Ref. 4; BAB25461)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 818 AA; 90413 MW; E59A292F2CF626C2 CRC64;
MRGVRCPGLL VVCILLSLSG AGTQKAESKN CAKWCPINSK CVSNRSCVCK PGFSSEKELI
TNPAESCEDI NECLLPGFSC GDFAMCKNSE GSYTCVCNLG YKLLSGAESF VNESENTCQA
SVNTGTTPVP SRIHTVTTAP GNLPEQTTTV HQTQMGDSEE RTPKDVNECI SGQNHCHQST
HCINKLGGYS CICRQGWKPV PGSPNGPVST VCEDVDECSS GQHQCHNSTV CKNTVGSYKC
HCRPGWKPTS GSLRGPDTIC QEPPFPTWTL LPTAHSQTLL RFSVEVQNLL RDFNPATVNY
TIQKLIEAVD KLLEDPMETQ TQQVAAQLLS NLEQSLRTLA QFLPKGPFTY TSPSNTELSL
MVKEQDNKDV TTVHHGQTWM ELDWAVTAGA KISENGSSVA GILSSPNMEK LLGNTPLNLE
QRRASLEDFY GSPIPSVSLK LLSNINSVFL TNTNTEKLAS NVTFKFDFTS VESIEPRHEL
ICAFWKAHNG NGYWDTDGCS MNGTGFCHCN HLTSFAILMA QYHVQDPRLE LITKVGLLLS
LICLLLCILT FLLVKPIQSS RTMVHLHLCI CLFLGSIIFL VGVENEGGEV GLRCRLVAMM
LHFCFLAAFC WMALEGVELY FLVVRVFQGQ GLSTWQRCLI GYGVPLLIVA ISMAVVKMDG
YGHATYCWLD FRKQGFLWSF SGPVAFIIFC NAAIFVITVW KLTKKFSEIN PNMKKLRKAR
VLTITAIAQL LVLGCTWGFG LFLFNPHSTW LSYIFTLLNC LQGLFLYVML CLLNKKVREE
YWKWACMVTG SKYTEFNSST TGTGTSQTRA LRSSESGM
