MYO9B_MOUSE
ID MYO9B_MOUSE Reviewed; 2114 AA.
AC Q9QY06; Q9QY07; Q9QY08; Q9QY09;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Unconventional myosin-IXb;
DE AltName: Full=Unconventional myosin-9b;
GN Name=Myo9b; Synonyms=Myr5;
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 [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, VARIANTS,
RP AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=10580159; DOI=10.1016/s0378-1119(99)00459-x;
RA Grewal P.K., Jones A.-M., Maconochie M., Lemmers R.J.F., Frants R.R.,
RA Hewitt J.E.;
RT "Cloning of the murine unconventional myosin gene Myo9b and identification
RT of alternative splicing.";
RL Gene 240:389-398(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1175 AND THR-1317, 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1218, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1175; SER-1266; SER-1325;
RP SER-1335; SER-1647; SER-1949; THR-1962 AND SER-2098, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Binds actin
CC with high affinity both in the absence and presence of ATP and its
CC mechanochemical activity is inhibited by calcium ions. Also acts as a
CC GTPase activator for RHOA. Plays a role in the regulation of cell
CC migration via its role as RHOA GTPase activator. This is regulated by
CC its interaction with the SLIT2 receptor ROBO1; interaction with ROBO1
CC impairs interaction with RHOA and subsequent activation of RHOA GTPase
CC activity, and thereby leads to increased levels of active, GTP-bound
CC RHOA. {ECO:0000250|UniProtKB:Q13459}.
CC -!- SUBUNIT: Interacts (via IQ domains) with CALM. Interacts with RHOA.
CC Interacts (via Rho-GAP domain) with ROBO1; this inhibits the
CC interaction with RHOA and the stimulation of RHOA GTPase activity, and
CC thereby increases the levels of active RHOA.
CC {ECO:0000250|UniProtKB:Q13459}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q13459}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q13459}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q13459}. Note=In undifferentiated cells
CC colocalizes with F-actin in the cell periphery while in differentiated
CC cells its localization is cytoplasmic with the highest levels in the
CC perinuclear region. {ECO:0000250|UniProtKB:Q13459}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9QY06-1; Sequence=Displayed;
CC Name=2; Synonyms=Q;
CC IsoId=Q9QY06-2; Sequence=VSP_003363;
CC Name=3; Synonyms=C;
CC IsoId=Q9QY06-3; Sequence=VSP_003364, VSP_003365;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, heart, muscle and inner
CC ear. {ECO:0000269|PubMed:10580159}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-9 (MYH9). {ECO:0000305}.
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DR EMBL; AF143687; AAF00122.1; -; Genomic_DNA.
DR EMBL; AF143685; AAF00120.1; -; mRNA.
DR EMBL; AF143686; AAF00121.1; ALT_FRAME; mRNA.
DR EMBL; AF143683; AAF00118.1; -; mRNA.
DR AlphaFoldDB; Q9QY06; -.
DR SMR; Q9QY06; -.
DR STRING; 10090.ENSMUSP00000129220; -.
DR iPTMnet; Q9QY06; -.
DR PhosphoSitePlus; Q9QY06; -.
DR EPD; Q9QY06; -.
DR jPOST; Q9QY06; -.
DR MaxQB; Q9QY06; -.
DR PaxDb; Q9QY06; -.
DR PeptideAtlas; Q9QY06; -.
DR PRIDE; Q9QY06; -.
DR ProteomicsDB; 286105; -. [Q9QY06-1]
DR ProteomicsDB; 286106; -. [Q9QY06-2]
DR ProteomicsDB; 286107; -. [Q9QY06-3]
DR MGI; MGI:106624; Myo9b.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR InParanoid; Q9QY06; -.
DR PhylomeDB; Q9QY06; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-8985586; SLIT2:ROBO1 increases RHOA activity.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9035034; RHOF GTPase cycle.
DR ChiTaRS; Myo9b; mouse.
DR PRO; PR:Q9QY06; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QY06; protein.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032433; C:filopodium tip; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0043008; F:ATP-dependent protein binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0003774; F:cytoskeletal motor activity; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0000146; F:microfilament motor activity; IDA:MGI.
DR GO; GO:0048495; F:Roundabout binding; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
DR GO; GO:0033275; P:actin-myosin filament sliding; ISO:MGI.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:MGI.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IMP:MGI.
DR GO; GO:0048246; P:macrophage chemotaxis; IMP:MGI.
DR GO; GO:0002548; P:monocyte chemotaxis; IMP:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:MGI.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:MGI.
DR GO; GO:0035385; P:Roundabout signaling pathway; ISS:UniProtKB.
DR CDD; cd00029; C1; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.850.10; -; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR028557; MYO9B.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036023; MYSc_Myo9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF2; PTHR46184:SF2; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 1.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW GTPase activation; Metal-binding; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT CHAIN 2..2114
FT /note="Unconventional myosin-IXb"
FT /id="PRO_0000123470"
FT DOMAIN 15..114
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 146..953
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 957..977
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 979..1000
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1001..1023
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1024..1053
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1661..1846
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 1590..1639
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 714..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..855
FT /note="Actin-binding"
FT REGION 940..1044
FT /note="Neck or regulatory domain"
FT REGION 1045..2114
FT /note="Tail"
FT REGION 1045..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1702
FT /note="Interaction with RHOA"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT REGION 1940..2006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2092..2114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1562..1592
FT /evidence="ECO:0000255"
FT COILED 1839..1859
FT /evidence="ECO:0000255"
FT COILED 1915..1945
FT /evidence="ECO:0000255"
FT COMPBIAS 1129..1175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..1954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..2000
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1045
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63358"
FT MOD_RES 1106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 1220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63358"
FT MOD_RES 1235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63358"
FT MOD_RES 1264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1317
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1929
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 1949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1956
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63358"
FT MOD_RES 1962
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2007
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13459"
FT MOD_RES 2098
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 740
FT /note="R -> RCTGLDFSFERSEELDVNAFEDIMAFYESR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003363"
FT VAR_SEQ 1875..1890
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003364"
FT VAR_SEQ 1977..2114
FT /note="GPPAPALPCPISPTLSPLPEAAAPPRGRPTSFVTVRVKTPRRTPIMPMANIK
FT LPPGLPLHLTSWAPALQEAVVPVKRREPPARRQDQVHSVYIAPGADLPSQSTLIALDHD
FT TILPGTKRRYSDPPTYCLPPSSGQANG -> E (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003365"
FT VARIANT 1243
FT /note="L -> LEVSPVLPSSSL (in strain: C57BL/6; contains an
FT in-frame 33 bp imperfect duplication)"
FT VARIANT 2083
FT /note="A -> P"
SQ SEQUENCE 2114 AA; 238834 MW; D774D4B1B2788045 CRC64;
MSAHEAGSSG RRQQATYHLH IYPQLSSAGS QTSCRVTATK DSTTSDVIQD VVASLHLDGS
KHYVLVEVKE SGGEEWVLDA SDSPVHRVLL WPRRAQDEHP QEDGYYFLLQ ERNADGSIQY
LPIQLLAQPT AACRLVERGL LPRPQADFDD LCNLPELTEA NLLQNLKLRF MQQKIYTYAG
SILVAINPFK FLPIYNPKYV KMYENQQLGK LEPHVFALAD VAYYAMLRKH VNQCIVISGE
SGSGKTQSTN FLIHCLTALS QKGYASGVER TILGAGPVLE AFGNAKTAHN NNSSRFGKFI
QVNYLENGIV RGAVVEKYLL EKSRLVSQEK DERNYHVFYY LLLGVSEEER LEFQLKQPQD
YFYLNQHNLN IEDGEDLKHD FERLQQAMEM VGFLPATKKQ IFSVLSAILY LGNVTYKKRA
TGRDEGLEVG PPEVLDTLSQ LLKVKRETLV EVLTKRKTVT VNDKLILPYS LSEAITARDS
MAKSLYSALF DWIVLRINHA LLNKKDMEEA VSCLSIGVLD IFGFEDFERN SFEQFCINYA
NEQLQYYFTQ HIFKLEQEEY QGEGISWHNI DYTDNVGCIH LISKKPTGLF YLLDEESNFP
HATSHTLLAK FKQQHEDNKY FLGTPVLEPA FIIQHFAGRV KYQIKDFREK NMDYMRPDIV
ALLRGSDSSY VRQLIGMDPV AVFRWAVLRA AIRAMAVLRE AGRLRAERAE KAAGISSPAT
RSHMEELPRG ASTPSEKLYR DLHNQIIKSL KGLPWQGEDP RRLLQSLSLL QKPRTSFLKS
KGIKQKQIIP KNLLDSKSLR LIISMTLHDR TTKSLLHLHK KKKPPSISAQ FQTSLNKLLE
ALGKAEPFFI RCIRSNAEKK ELCFDDELVL QQLRYTGMLE TVRIRRSGYS AKYTFQDFTE
QFQVLLPKDV QPCREAIAAL LEKLQVDRQN YQIGKTKVFL KETERQTLQE KLHGEVLRRI
LQLQSWFRMV LERKHFVQMK HAALTIQACW RSYRVRRALE RTQAAVYLQA AWRGYLQRQA
YHHQRHSIIR LQSLCRGHLQ RRSFSQMVSE KQKAEQAREA AGGKLSEGEP GPVAAGEQLS
EHPVEDPESL GVEAETWMNK SPDGMSPKKE TPSPEMETAA QKTVPAESHE KVSSSREKRE
SRRQRGLEHV ERQNKHIQSC REESSTHREP SRRASLEIGE SFPEGTKGPR EDGLEAWTET
TAPSSSKQAQ VVGDPPGSPS PVQRPTTLAL DSRVSPMLPS SSLESPKDKD KDESSTKAQD
KPESPSGSTQ IQRYQHPDTE RLATAVEIWR GKKLASAVLS QSLDLSEKHR ATGAALTPTE
ERRISFSTSD ISKLSPVKTS AEIDGDFSSK KPSIHKKKSG DPSAGPDAGL SPGSQGDSKS
AFKRLFLHKA KDKKPSLEGV EETESNGGQA AQETPARKTL DVPSSQQHRH TTGEKPLKGK
KNRNRKVGQI TVSEKWRESV FRKITNANEL KFLDEFLLNK VNDLRSQKTP IESLFIEATE
RFRSNIKTMY SVPNGKIHVG YKDLMENYQI VVSNLAAERG EKDTNLVLNV FQSLLDEFTR
SYNKTDFERA KSKAQKKKRK QERAVQEHNG HVFASYQVNI PQSCEQCLSY IWLMDKALLC
SVCKMTCHKK CVHKIQSYCS YTGRRKSELG AEPGHFGVCV DSLTSDKASV PIVLEKLLEH
VEMHGLYTEG LYRKSGAANR TRELRQALQT DPAAVKLEDF PIHAITGVLK QWLRELPEPL
MTFAQYGDFL RAVELPEKQE QLSAIYAVLD HLPEANHTSL ERLIFHLVKV ALLEDVNRMS
PGALAIIFAP CLLRCPDNSD PLTSMKDVLK ITTCVEMLIK EQMRKYKMKM EEINHLEAAE
SIAFRRLSLL RQNAPWPLKL GFSSPYEGVR IKSPRTPVVQ DLELGALSEE AAGGDEDREK
EILMERIQSI KEEKEDITYR LPELDPRGSD EENLDSETSA STESLLEERG VRGAVEGPPA
PALPCPISPT LSPLPEAAAP PRGRPTSFVT VRVKTPRRTP IMPMANIKLP PGLPLHLTSW
APALQEAVVP VKRREPPARR QDQVHSVYIA PGADLPSQST LIALDHDTIL PGTKRRYSDP
PTYCLPPSSG QANG
