MAGI1_MOUSE
ID MAGI1_MOUSE Reviewed; 1471 AA.
AC Q6RHR9; O54893; O54894; O54895;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1;
DE AltName: Full=BAI1-associated protein 1;
DE Short=BAP-1;
DE AltName: Full=Membrane-associated guanylate kinase inverted 1;
DE Short=MAGI-1;
GN Name=Magi1; Synonyms=Baiap1, Bap1;
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), AND INTERACTION WITH ESAM.
RC STRAIN=129/SvHe; TISSUE=Brain endothelium;
RX PubMed=15383320; DOI=10.1016/j.yexcr.2004.07.010;
RA Wegmann F., Ebnet K., Du Pasquier L., Vestweber D., Butz S.;
RT "Endothelial adhesion molecule ESAM binds directly to the multidomain
RT adaptor MAGI-1 and recruits it to cell contacts.";
RL Exp. Cell Res. 300:121-133(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X CBA;
RX PubMed=9395497; DOI=10.1074/jbc.272.50.31589;
RA Dobrosotskaya I.Y., Guy R.K., James G.L.;
RT "MAGI-1, a membrane-associated guanylate kinase with a unique arrangement
RT of protein-protein interaction domains.";
RL J. Biol. Chem. 272:31589-31597(1997).
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CTNNB1.
RX PubMed=10772923; DOI=10.1006/bbrc.2000.2471;
RA Dobrosotskaya I.Y., James G.L.;
RT "MAGI-1 interacts with beta-catenin and is associated with cell-cell
RT adhesion structures.";
RL Biochem. Biophys. Res. Commun. 270:903-909(2000).
RN [4]
RP INTERACTION WITH NET1.
RX PubMed=11350080; DOI=10.1006/bbrc.2001.4880;
RA Dobrosotskaya I.Y.;
RT "Identification of mNET1 as a candidate ligand for the first PDZ domain of
RT MAGI-1.";
RL Biochem. Biophys. Res. Commun. 283:969-975(2001).
RN [5]
RP INTERACTION WITH LRP2, TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=11274227; DOI=10.1681/asn.v124667;
RA Patrie K.M., Drescher A.J., Goyal M., Wiggins R.C., Margolis B.;
RT "The membrane-associated guanylate kinase protein MAGI-1 binds megalin and
RT is present in glomerular podocytes.";
RL J. Am. Soc. Nephrol. 12:667-677(2001).
RN [6]
RP INTERACTION WITH DLL1.
RX PubMed=15509766; DOI=10.1242/dev.01417;
RA Wright G.J., Leslie J.D., Ariza-McNaughton L., Lewis J.;
RT "Delta proteins and MAGI proteins: an interaction of Notch ligands with
RT intracellular scaffolding molecules and its significance for zebrafish
RT development.";
RL Development 131:5659-5669(2004).
RN [7]
RP INTERACTION WITH ASIC3, AND FUNCTION.
RX PubMed=15317815; DOI=10.1074/jbc.m405874200;
RA Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.;
RT "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have
RT opposite effects on H+- gated current.";
RL J. Biol. Chem. 279:46962-46968(2004).
RN [8]
RP INTERACTION WITH CXADR.
RX PubMed=15304526; DOI=10.1242/jcs.01300;
RA Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L.,
RA Zabner J.;
RT "A role for the PDZ-binding domain of the coxsackie B virus and adenovirus
RT receptor (CAR) in cell adhesion and growth.";
RL J. Cell Sci. 117:4401-4409(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, 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 play a role as scaffolding protein at cell-cell
CC junctions. May regulate acid-induced ASIC3 currents by modulating its
CC expression at the cell surface. {ECO:0000269|PubMed:15317815}.
CC -!- SUBUNIT: Interacts through its WW 2 domain with SYNPO and through its
CC PDZ 5 domain with ACTN4. Interacts with cytoplasmic domain of ADGRB1.
CC Interacts via its WW domains with DRPLA (By similarity). Interacts with
CC ESAM, LRP2 and CXADR (PubMed:15383320, PubMed:11274227,
CC PubMed:15304526). Isoform 2 interacts with CTNNB1 (PubMed:10772923).
CC Interacts through its PDZ 1 domain with NET1 (PubMed:11350080).
CC Interacts with ASIC3 and AMOT (By similarity) (PubMed:15317815).
CC Interacts with FCHSD2 (By similarity). Interacts with IGSF5/JAM4 and
CC through its PDZ 2 and 3 domains with NPHS1 forming a tripartite complex
CC (By similarity). Interacts with DDN. May interact (via PDZ domain) with
CC RAPGEF2 (By similarity). Interacts with DLL1 (PubMed:15509766).
CC Interacts with KCNJ10 and possibly with KCNJ10/KCNJ16 heterodimer; this
CC interaction may facilitate KCNJ10/KCNJ16 potassium channel expression
CC at the basolateral membrane in kidney tubular cells (By similarity).
CC Interacts with PRRG4 (via cytoplasmic domain) (By similarity).
CC {ECO:0000250|UniProtKB:Q4L1J4, ECO:0000250|UniProtKB:Q96QZ7,
CC ECO:0000269|PubMed:10772923, ECO:0000269|PubMed:11274227,
CC ECO:0000269|PubMed:11350080, ECO:0000269|PubMed:15304526,
CC ECO:0000269|PubMed:15317815, ECO:0000269|PubMed:15383320,
CC ECO:0000269|PubMed:15509766}.
CC -!- INTERACTION:
CC Q6RHR9; Q9Z206: Net1; NbExp=6; IntAct=EBI-7440897, EBI-7840997;
CC Q6RHR9-1; Q9BZD6: PRRG4; Xeno; NbExp=2; IntAct=EBI-7441112, EBI-3918643;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}. Cell
CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Cell
CC junction, tight junction {ECO:0000250}. Note=Localizes to epithelial
CC cells tight junctions. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}. Cell
CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=MAGI1c alpha beta2 gamma, MAGI-1c;
CC IsoId=Q6RHR9-1; Sequence=Displayed;
CC Name=2; Synonyms=MAGI-1b;
CC IsoId=Q6RHR9-2; Sequence=VSP_011673, VSP_011674, VSP_011675,
CC VSP_011676, VSP_011677;
CC Name=3; Synonyms=MAGI-1a;
CC IsoId=Q6RHR9-3; Sequence=VSP_011678, VSP_011679, VSP_011677;
CC -!- TISSUE SPECIFICITY: Widely expressed, including kidney glomeruli.
CC {ECO:0000269|PubMed:11274227, ECO:0000269|PubMed:9395497}.
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DR EMBL; AY497557; AAS77818.1; -; mRNA.
DR EMBL; AF027503; AAB91995.1; -; mRNA.
DR EMBL; AF027504; AAB91996.1; -; mRNA.
DR EMBL; AF027505; AAB91997.1; -; mRNA.
DR CCDS; CCDS20377.1; -. [Q6RHR9-1]
DR PIR; T42372; T42372.
DR RefSeq; NP_001025021.1; NM_001029850.4. [Q6RHR9-1]
DR RefSeq; NP_034497.1; NM_010367.3.
DR PDB; 2I04; X-ray; 2.15 A; A/B=463-546.
DR PDB; 5ZYS; X-ray; 1.78 A; A=826-918.
DR PDBsum; 2I04; -.
DR PDBsum; 5ZYS; -.
DR AlphaFoldDB; Q6RHR9; -.
DR BMRB; Q6RHR9; -.
DR SMR; Q6RHR9; -.
DR BioGRID; 200129; 19.
DR ELM; Q6RHR9; -.
DR IntAct; Q6RHR9; 7.
DR MINT; Q6RHR9; -.
DR STRING; 10090.ENSMUSP00000086730; -.
DR iPTMnet; Q6RHR9; -.
DR PhosphoSitePlus; Q6RHR9; -.
DR MaxQB; Q6RHR9; -.
DR PaxDb; Q6RHR9; -.
DR PRIDE; Q6RHR9; -.
DR ProteomicsDB; 252717; -. [Q6RHR9-1]
DR ProteomicsDB; 252718; -. [Q6RHR9-2]
DR ProteomicsDB; 252719; -. [Q6RHR9-3]
DR Antibodypedia; 15389; 193 antibodies from 26 providers.
DR DNASU; 14924; -.
DR Ensembl; ENSMUST00000089317; ENSMUSP00000086730; ENSMUSG00000045095. [Q6RHR9-1]
DR GeneID; 14924; -.
DR KEGG; mmu:14924; -.
DR UCSC; uc009czj.2; mouse. [Q6RHR9-1]
DR UCSC; uc009czk.2; mouse. [Q6RHR9-2]
DR CTD; 9223; -.
DR MGI; MGI:1203522; Magi1.
DR VEuPathDB; HostDB:ENSMUSG00000045095; -.
DR eggNOG; KOG3209; Eukaryota.
DR GeneTree; ENSGT00940000155820; -.
DR InParanoid; Q6RHR9; -.
DR OMA; KILDRNC; -.
DR OrthoDB; 284488at2759; -.
DR PhylomeDB; Q6RHR9; -.
DR TreeFam; TF316816; -.
DR BioGRID-ORCS; 14924; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Magi1; mouse.
DR EvolutionaryTrace; Q6RHR9; -.
DR PRO; PR:Q6RHR9; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q6RHR9; protein.
DR Bgee; ENSMUSG00000045095; Expressed in ventricular zone and 233 other tissues.
DR ExpressionAtlas; Q6RHR9; baseline and differential.
DR Genevisible; Q6RHR9; MM.
DR GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0071944; C:cell periphery; ISO:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0051393; F:alpha-actinin binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:InterPro.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.30.42.10; -; 6.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR030033; MAGI1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10316:SF12; PTHR10316:SF12; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 5.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 6.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF50156; SSF50156; 6.
DR SUPFAM; SSF51045; SSF51045; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell junction;
KW Cell membrane; Cytoplasm; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1471
FT /note="Membrane-associated guanylate kinase, WW and PDZ
FT domain-containing protein 1"
FT /id="PRO_0000094590"
FT DOMAIN 17..105
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 96..287
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT DOMAIN 300..333
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 359..392
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 464..546
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 635..713
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 833..915
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 990..1074
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1132..1214
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 233..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1074
FT /note="Interaction with FCHSD2"
FT /evidence="ECO:0000250"
FT REGION 1092..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1262..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QZ7"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QZ7"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QZ7"
FT MOD_RES 792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QZ7"
FT MOD_RES 1341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QZ7"
FT MOD_RES 1392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QZ7"
FT VAR_SEQ 348..359
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9395497"
FT /id="VSP_011673"
FT VAR_SEQ 798..826
FT /note="PMSPSPASGLSKGERDREINSTNFGECQI -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9395497"
FT /id="VSP_011674"
FT VAR_SEQ 1019..1074
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9395497"
FT /id="VSP_011675"
FT VAR_SEQ 1221..1268
FT /note="DPSSDRNGPSTGAQGVPEVRPGPPDHRPHPALESSYPPELHKSSQHAE ->
FT AMIPPKIAACMRNEKLGEACFYLMGHNQTTTPAATGTAPPPVHKVFRK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9395497"
FT /id="VSP_011676"
FT VAR_SEQ 1221..1236
FT /note="DPSSDRNGPSTGAQGV -> GGSNYENIPSFPGMTP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9395497"
FT /id="VSP_011678"
FT VAR_SEQ 1238..1268
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9395497"
FT /id="VSP_011679"
FT VAR_SEQ 1269..1471
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:9395497"
FT /id="VSP_011677"
FT CONFLICT 726
FT /note="Missing (in Ref. 2; AAB91995)"
FT /evidence="ECO:0000305"
FT CONFLICT 1342
FT /note="A -> D (in Ref. 2; AAB91997)"
FT /evidence="ECO:0000305"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:2I04"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:2I04"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:2I04"
FT HELIX 498..502
FT /evidence="ECO:0007829|PDB:2I04"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:2I04"
FT HELIX 524..532
FT /evidence="ECO:0007829|PDB:2I04"
FT STRAND 539..545
FT /evidence="ECO:0007829|PDB:2I04"
FT STRAND 829..837
FT /evidence="ECO:0007829|PDB:5ZYS"
FT STRAND 842..849
FT /evidence="ECO:0007829|PDB:5ZYS"
FT STRAND 857..862
FT /evidence="ECO:0007829|PDB:5ZYS"
FT HELIX 867..871
FT /evidence="ECO:0007829|PDB:5ZYS"
FT STRAND 879..883
FT /evidence="ECO:0007829|PDB:5ZYS"
FT HELIX 893..906
FT /evidence="ECO:0007829|PDB:5ZYS"
FT STRAND 908..916
FT /evidence="ECO:0007829|PDB:5ZYS"
SQ SEQUENCE 1471 AA; 161974 MW; 6C780C71CAC37CB1 CRC64;
MSKVIQKKNH WTGRVHECTV KRGPQGELGV TVLGGAEHGE FPYVGAVAAA EAAGLPGGGE
GPKLAEGELL LEVQGVRVSG LPRYDVLGVI DSCKEAVTFK AVRQGGRLNK DLRHFLNQRF
QKGSPDHELQ QTIRDNLYRH AVPCTTRSPR EGEVPGVDYS FLTVKEFLDL EQSGTLLEVG
TYEGNYYGTP KPPSQPVSGK VITTDALHSL QSGSKQSTPK RTKSYNDMQN AGIVHPENEE
EEDVPEMNSS FTADSGDQDE HTLQEATLPP VNSSILAAPI TDPSQKFPQY LPLSAEDNLG
PLPENWEMAY TENGEVYFID HNTKTTSWLD PRCLNKQQKP LEECEDDEGV HTEELDSELE
LPAGWEKIED PVYGVYYVDH INRKTQYENP VLEAKRKKQL EQQQQQQQPQ PPQPEEWTED
HASVVPPVAP SHPPSNPEPA RETPLQGKPF FTRNPSELKG KFIHTKLRKS SRGFGFTVVG
GDEPDEFLQI KSLVLDGPAA LDGKMETGDV IVSVNDTCVL GHTHAQVVKI FQSIPIGASV
DLELCRGYPL PFDPDDPNTS LVTSVAILDK EPIIVNGQET YDSPASHSSK TGKVSSMKDA
RPSSPADVAS NSSHGYPNDT VSLASSIATQ PELITVHIVK GPMGFGFTIA DSPGGGGQRV
KQIVDSPRCR GLKEGDLIVE VNKKNVQALT HNQVVDMLIE CPKGSEVTLL VQRGGLPVPK
KSPKSQPLER KDSQNSSQHS VSSHRSLHTA SPSHGIQVLP EYLPADAPAP DQTDSSGQKK
PDPFKIWAQS RSMYENRPMS PSPASGLSKG ERDREINSTN FGECQIPDYQ EQDIFLWRKE
TGFGFRILGG NEPGEPIYIG HIVPLGAADT DGRLRSGDEL ICVDGTPVIG KSHQLVVQLM
QQAAKQGHVN LTVRRKVVFA VPKAENEVPS PASSHHSSNQ PASLTEEKRT PQGSQNSLNT
VSSGSGSTSG IGSGGGGGSG VVSAVLQPYD VEIRRGENEG FGFVIVSSVS RPEAGTTFGR
IIEGSPADRC GKLKVGDRIL AVNGCSITNK SHSDIVNLIK EAGNTVTLRI IPGDESSNAT
LLTNAEKIAT ITTTHAPSQQ GTQETRTTTK PKQDSQFEFK GPQAAQEQDF YTVELERGAK
GFGFSLRGGR EYNMDLYVLR LAEDGPAERC GKMRIGDEIL EINGETTKNM KHSRAIELIK
NGGRRVRLFL RRGDGSVPEY DPSSDRNGPS TGAQGVPEVR PGPPDHRPHP ALESSYPPEL
HKSSQHAEKR AHAKDPKGNR EHSKQPNEHH TWNGTSRKQD SGACRPKDRP PDAWREAQPE
RTATNGSKRR SPEKRREGTR SADNTLERRE KHEKRREISP ERKRERSPTR RKDSSPSRRR
RSLERLLDQR RSPERRRGGS PERRAKSTDR RRARSPERRR ERSLDKRNRD DKVGHREREE
AGLKLEAGRS PRNPPEQRRR PYKECSTDLS I
