ITSN2_MOUSE
ID ITSN2_MOUSE Reviewed; 1659 AA.
AC Q9Z0R6; Q8C9C3; Q9Z0R5;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Intersectin-2;
DE AltName: Full=EH domain and SH3 domain regulator of endocytosis 2;
DE Short=EH and SH3 domains protein 2;
DE AltName: Full=SH3 domain-containing protein 1B;
GN Name=Itsn2; Synonyms=Ese2, Sh3d1B;
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] OF 1-441 (ISOFORM 1/2).
RC STRAIN=C57BL/6J; 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-1659 (ISOFORMS 1 AND 2).
RX PubMed=10064583; DOI=10.1093/emboj/18.5.1159;
RA Sengar A.S., Wang W., Bishay J., Cohen S., Egan S.E.;
RT "The EH and SH3 domain Ese proteins regulate endocytosis by linking to
RT dynamin and Eps15.";
RL EMBO J. 18:1159-1171(1999).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-922, AND IDENTIFICATION BY
RP 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 TYR-554 AND TYR-922, AND
RP IDENTIFICATION BY 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 [5]
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 [6]
RP INTERACTION WITH ANKRD54.
RX PubMed=19064729; DOI=10.1182/blood-2008-04-153452;
RA Samuels A.L., Klinken S.P., Ingley E.;
RT "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that
RT influences erythropoietin-induced differentiation.";
RL Blood 113:3845-3856(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-838; SER-843 AND TYR-922, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; THR-836; SER-838 AND
RP SER-843, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, 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 [10]
RP INTERACTION WITH FCHO2.
RX PubMed=20448150; DOI=10.1126/science.1188462;
RA Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R.,
RA McMahon H.T.;
RT "FCHo proteins are nucleators of clathrin-mediated endocytosis.";
RL Science 328:1281-1284(2010).
CC -!- FUNCTION: Adapter protein that may provide indirect link between the
CC endocytic membrane traffic and the actin assembly machinery. May
CC regulate the formation of clathrin-coated vesicles (CCPs). Seems to be
CC involved in CCPs maturation including invagination or budding. Involved
CC in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor
CC (TFR). Plays a role in dendrite formation by melanocytes.
CC {ECO:0000250|UniProtKB:Q9NZM3}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Belongs to a complex that may contain multimers of ITSN1,
CC ITSN2 and EPS15, and different partners according to the step in the
CC endocytic process. Interacts with ADAM15. Interacts with FASLG (By
CC similarity). Interacts with ANKRD54. Interacts with FCHO2.
CC {ECO:0000250, ECO:0000269|PubMed:19064729,
CC ECO:0000269|PubMed:20448150}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Ese2L, Long;
CC IsoId=Q9Z0R6-1; Sequence=Displayed;
CC Name=2; Synonyms=Ese2, Short;
CC IsoId=Q9Z0R6-2; Sequence=VSP_003896, VSP_003897;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues.
CC -!- DEVELOPMENTAL STAGE: Widely distributed throughout the adult forebrain.
CC Prominent expression was observed in the neocortex, the piriform
CC cortex, the pyramidal cell layers of hippocampus, the dentate gyrus, in
CC several nuclei of the thalamus and hypothalamus and in the amygdala.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31264.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK042449; BAC31264.1; ALT_INIT; mRNA.
DR EMBL; AF132479; AAD19747.1; -; mRNA.
DR EMBL; AF132480; AAD19748.1; -; mRNA.
DR AlphaFoldDB; Q9Z0R6; -.
DR SMR; Q9Z0R6; -.
DR IntAct; Q9Z0R6; 13.
DR STRING; 10090.ENSMUSP00000052758; -.
DR iPTMnet; Q9Z0R6; -.
DR PhosphoSitePlus; Q9Z0R6; -.
DR EPD; Q9Z0R6; -.
DR jPOST; Q9Z0R6; -.
DR MaxQB; Q9Z0R6; -.
DR PaxDb; Q9Z0R6; -.
DR PeptideAtlas; Q9Z0R6; -.
DR PRIDE; Q9Z0R6; -.
DR ProteomicsDB; 269019; -. [Q9Z0R6-1]
DR ProteomicsDB; 269020; -. [Q9Z0R6-2]
DR UCSC; uc007mxy.1; mouse. [Q9Z0R6-2]
DR MGI; MGI:1338049; Itsn2.
DR eggNOG; KOG1029; Eukaryota.
DR eggNOG; KOG4305; Eukaryota.
DR InParanoid; Q9Z0R6; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-9013420; RHOU GTPase cycle.
DR ChiTaRS; Itsn2; mouse.
DR PRO; PR:Q9Z0R6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9Z0R6; protein.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0150007; P:clathrin-dependent synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR CDD; cd00052; EH; 2.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11988; SH3_Intersectin2_1; 1.
DR CDD; cd11990; SH3_Intersectin2_2; 1.
DR CDD; cd11992; SH3_Intersectin2_3; 1.
DR CDD; cd11994; SH3_Intersectin2_4; 1.
DR CDD; cd11996; SH3_Intersectin2_5; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR InterPro; IPR027029; Intersectin-2.
DR InterPro; IPR035737; Intersectin-2_SH3_1.
DR InterPro; IPR035738; Intersectin-2_SH3_2.
DR InterPro; IPR035739; Intersectin-2_SH3_3.
DR InterPro; IPR035740; Intersectin-2_SH3_4.
DR InterPro; IPR035741; Intersectin-2_SH3_5.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR11216:SF29; PTHR11216:SF29; 3.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12763; EF-hand_4; 2.
DR Pfam; PF16652; PH_13; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF14604; SH3_9; 2.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00027; EH; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 5.
DR SUPFAM; SSF47473; SSF47473; 2.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF50044; SSF50044; 5.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50031; EH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Coiled coil; Cytoplasm; Differentiation;
KW Endocytosis; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..1659
FT /note="Intersectin-2"
FT /id="PRO_0000080962"
FT DOMAIN 22..110
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 54..89
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 245..334
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 278..313
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 718..779
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 852..910
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 942..1000
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1014..1078
FT /note="SH3 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1088..1147
FT /note="SH3 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1170..1357
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1396..1506
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1514..1630
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 220..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 365..717
FT /evidence="ECO:0000255"
FT COMPBIAS 220..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 71
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 78
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 1602
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1605
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1608
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZM3"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZM3"
FT MOD_RES 554
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 574
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZM3"
FT MOD_RES 836
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 922
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455,
FT ECO:0007744|PubMed:17947660, ECO:0007744|PubMed:19144319"
FT VAR_SEQ 1188..1198
FT /note="DDLQLVIEVFQ -> GLQLFEQKTLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10064583"
FT /id="VSP_003896"
FT VAR_SEQ 1199..1659
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10064583"
FT /id="VSP_003897"
FT CONFLICT 452..453
FT /note="KQ -> NT (in Ref. 2; AAD19748)"
FT /evidence="ECO:0000305"
FT CONFLICT 1162
FT /note="D -> G (in Ref. 2; AAD19748)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1659 AA; 188908 MW; 840F16B3A0DACDD6 CRC64;
MMAQFPTAMN GGPNMWAITS EERTKHDKQF DNLKPSGGYI TGDQARTFFL QSGLPAPVLA
EIWALSDLNK DGKMDQQEFS IAMKLIKLKL QGQQLPVVLP PIMKQPPMFS PLISARFGMG
SMPNLSIHQP LPPVAPIATP LSSATSGTSI PPLMMPAPLV PSVSTSSLPN GTASLIQPLS
IPYSSSTLPH ASSYSLMMGG FGGASIQKAQ SLIDLGSSSS TSSTASLSGN SPKTGTSEWA
VPQPSRLKYR QKFNSLDKGM SGYLSGFQAR NALLQSNLSQ TQLATIWTLA DIDGDGQLKA
EEFILAMHLT DMAKAGQPLP LTLPPELVPP SFRGGKQVDS VNGTLPSYQK TQEEEPQKKL
PVTFEDKRKA NYERGNMELE KRRQVLMEQQ QREAERKAQK EKEEWERKQR ELQEQEWKKQ
LELEKRLEKQ RELERQREEE RRKEIERREA AKQELERQRR LEWERLRRQE LLSQKTREQE
DIVRLSSRKK SLHLELEAVN GKHQQISGRL QDVQIRKQTQ KTELEVLDKQ CDLEIMEIKQ
LQQELKEYQN KLIYLVPEKQ LLNERIKNMQ LSNTPDSGIS LLHKKSSEKE ELCQRLKEQL
DALEKETASK LSEMDSFNNQ LKELRESYNT QQLALEQLHK IKRDKLKEIE RKRLEQIQKK
KLEDEAARKA KQGKENLWRE SIRKEEEEKQ KRLQEEKSQD KTQEEERKAE AKQSETASAL
VNYRALYPFE ARNHDEMSFS SGDIIQVDEK TVGEPGWLYG SFQGKFGWFP CNYVEKVLSS
EKALSPKKAL LPPTVSLSAT STSSQPPASV TDYHNVSFSN LTVNTTWQQK SAFTRTVSPG
SVSPIHGQGQ AVENLKAQAL CSWTAKKENH LNFSKHDVIT VLEQQENWWF GEVHGGRGWF
PKSYVKLIPG NEVQRGEPEA LYAAVTKKPT STAYPVTSTA YPVGEDYIAL YSYSSVEPGD
LTFTEGEEIL VTQKDGEWWT GSIGERTGIF PSNYVRPKDQ ENFGNASKSG ASNKKPEIAQ
VTSAYAASGT EQLSLAPGQL ILILKKNTSG WWQGELQARG KKRQKGWFPA SHVKLLGPSS
ERTMPTFHAV CQVIAMYDYM ANNEDELNFS KGQLINVMNK DDPDWWQGET NGLTGLFPSN
YVKMTTDSDP SQQWCADLQA LDTMQPTERK RQGYIHELIQ TEERYMDDDL QLVIEVFQKR
MAEEGFLTEA DMALIFVNWK ELIMSNTKLL RALRVRKKTG GEKMPVQMIG DILAAELSHM
QAYIRFCSCQ LNGATLLQQK TDEDTDFKEF LKKLASDPRC KGMPLSSFLL KPMQRITRYP
LLIRSILENT PQSHVDHSSL KLALERAEEL CSQVNEGVRE KENSDRLEWI QAHVQCEGLA
EQLIFNSLTN CLGPRKLLHS GKLYKTKSNK ELHAFLFNDF LLLTYLVRQF AAASGHEKLF
NSKSSAQFRM YKTPIFLNEV LVKLPTDPSG DEPVFHISHI DRVYTLRTDN INERTAWVQK
IKGASEQYID TEKKKREKAY QARSQKTSGI GRLMVHVIEA TELKACKPNG KSNPYCEVSM
GSQSYTTRTL QDTLNPKWNF NCQFFIKDLY QDVLCLTMFD RDQFSPDDFL GRTEVPVAKI
RTEQESKGPT TRRLLLHEVP TGEVWVRFDL QLFEQKTLL
