RHG24_HUMAN
ID RHG24_HUMAN Reviewed; 748 AA.
AC Q8N264; Q4KMG1; Q6ZNV3; Q86TI5; Q86WE4; Q9H0T6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Rho GTPase-activating protein 24;
DE AltName: Full=Filamin-A-associated RhoGAP;
DE Short=FilGAP;
DE AltName: Full=RAC1- and CDC42-specific GTPase-activating protein of 72 kDa;
DE Short=RC-GAP72;
DE AltName: Full=Rho-type GTPase-activating protein 24;
DE AltName: Full=RhoGAP of 73 kDa;
DE AltName: Full=Sarcoma antigen NY-SAR-88;
DE AltName: Full=p73RhoGAP;
GN Name=ARHGAP24; Synonyms=FILGAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Spleen, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Chondrosarcoma;
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 [MRNA] OF 233-510.
RX PubMed=12601173; DOI=10.1073/pnas.0437972100;
RA Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B.,
RA Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.;
RT "Immunomic analysis of human sarcoma.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003).
RN [5]
RP IDENTIFICATION.
RX PubMed=15254788;
RA Katoh M., Katoh M.;
RT "Identification and characterization of ARHGAP24 and ARHGAP25 genes in
RT silico.";
RL Int. J. Mol. Med. 14:333-338(2004).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND MUTAGENESIS OF ARG-175.
RX PubMed=15302923; DOI=10.1073/pnas.0404631101;
RA Su Z.-J., Hahn C.N., Goodall G.J., Reck N.M., Leske A.F., Davy A.,
RA Kremmidiotis G., Vadas M.A., Gamble J.R.;
RT "A vascular cell-restricted RhoGAP, p73RhoGAP, is a key regulator of
RT angiogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12212-12217(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ARG-175.
RX PubMed=15611138; DOI=10.1074/jbc.m411990200;
RA Lavelin I., Geiger B.;
RT "Characterization of a novel GTPase-activating protein associated with
RT focal adhesions and the actin cytoskeleton.";
RL J. Biol. Chem. 280:7178-7185(2005).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FLNA,
RP AND PHOSPHORYLATION AT SER-391; SER-402; SER-413; SER-415; SER-437 AND
RP THR-452.
RX PubMed=16862148; DOI=10.1038/ncb1437;
RA Ohta Y., Hartwig J.H., Stossel T.P.;
RT "FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control
RT actin remodelling.";
RL Nat. Cell Biol. 8:803-814(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Rho GTPase-activating protein involved in cell polarity, cell
CC morphology and cytoskeletal organization. Acts as a GTPase activator
CC for the Rac-type GTPase by converting it to an inactive GDP-bound
CC state. Controls actin remodeling by inactivating Rac downstream of Rho
CC leading to suppress leading edge protrusion and promotes cell
CC retraction to achieve cellular polarity. Able to suppress RAC1 and
CC CDC42 activity in vitro. Overexpression induces cell rounding with
CC partial or complete disruption of actin stress fibers and formation of
CC membrane ruffles, lamellipodia, and filopodia. Isoform 2 is a vascular
CC cell-specific GAP involved in modulation of angiogenesis.
CC {ECO:0000269|PubMed:15302923, ECO:0000269|PubMed:15611138,
CC ECO:0000269|PubMed:16862148}.
CC -!- SUBUNIT: Interacts with FLNA. {ECO:0000269|PubMed:16862148}.
CC -!- INTERACTION:
CC Q8N264; P21333: FLNA; NbExp=6; IntAct=EBI-988764, EBI-350432;
CC Q8N264; P42858: HTT; NbExp=3; IntAct=EBI-988764, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, adherens
CC junction. Cell junction, focal adhesion. Cell projection.
CC Note=Localizes to actin stress fibers. In migrating cells, localizes to
CC membrane lamellae and protusions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8N264-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N264-2; Sequence=VSP_023712, VSP_023715;
CC Name=3;
CC IsoId=Q8N264-3; Sequence=VSP_023711;
CC Name=4;
CC IsoId=Q8N264-4; Sequence=VSP_023717, VSP_023718;
CC Name=5;
CC IsoId=Q8N264-5; Sequence=VSP_023713, VSP_023714, VSP_023716;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed with a higher level
CC in kidney. Isoform 2 is mainly expressed in endothelial cells.
CC {ECO:0000269|PubMed:15302923, ECO:0000269|PubMed:15611138,
CC ECO:0000269|PubMed:16862148}.
CC -!- INDUCTION: [Isoform 2]: Up-regulated during capillary tube formation in
CC umbilical vein endothelial cells. {ECO:0000269|PubMed:15302923}.
CC -!- DOMAIN: The coiled coil domain mediates the interaction with FLNA
CC leading to its recruitment to lamellae.
CC -!- PTM: Phosphorylated by ROCK, leading to activate the RacGAP activity.
CC {ECO:0000269|PubMed:16862148}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO65178.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL136646; CAB66581.1; -; mRNA.
DR EMBL; AK091196; BAC03606.1; -; mRNA.
DR EMBL; AK130576; BAC85384.1; -; mRNA.
DR EMBL; BC047918; AAH47918.1; -; mRNA.
DR EMBL; BC098580; AAH98580.1; -; mRNA.
DR EMBL; AY211925; AAO65178.1; ALT_FRAME; mRNA.
DR CCDS; CCDS34025.1; -. [Q8N264-1]
DR CCDS; CCDS3611.1; -. [Q8N264-2]
DR CCDS; CCDS43246.1; -. [Q8N264-3]
DR PIR; A59430; A59430.
DR RefSeq; NP_001020787.2; NM_001025616.2. [Q8N264-1]
DR RefSeq; NP_001036134.1; NM_001042669.1. [Q8N264-3]
DR RefSeq; NP_112595.2; NM_031305.2. [Q8N264-2]
DR RefSeq; XP_011530602.1; XM_011532300.2. [Q8N264-3]
DR AlphaFoldDB; Q8N264; -.
DR SMR; Q8N264; -.
DR BioGRID; 123663; 38.
DR DIP; DIP-35520N; -.
DR IntAct; Q8N264; 24.
DR STRING; 9606.ENSP00000378611; -.
DR iPTMnet; Q8N264; -.
DR PhosphoSitePlus; Q8N264; -.
DR BioMuta; ARHGAP24; -.
DR DMDM; 134035016; -.
DR EPD; Q8N264; -.
DR MassIVE; Q8N264; -.
DR MaxQB; Q8N264; -.
DR PaxDb; Q8N264; -.
DR PeptideAtlas; Q8N264; -.
DR PRIDE; Q8N264; -.
DR ProteomicsDB; 71656; -. [Q8N264-1]
DR ProteomicsDB; 71657; -. [Q8N264-2]
DR ProteomicsDB; 71658; -. [Q8N264-3]
DR ProteomicsDB; 71659; -. [Q8N264-4]
DR ProteomicsDB; 71660; -. [Q8N264-5]
DR Antibodypedia; 2133; 175 antibodies from 23 providers.
DR DNASU; 83478; -.
DR Ensembl; ENST00000264343.4; ENSP00000264343.4; ENSG00000138639.18. [Q8N264-2]
DR Ensembl; ENST00000395183.6; ENSP00000378610.2; ENSG00000138639.18. [Q8N264-3]
DR Ensembl; ENST00000395184.6; ENSP00000378611.1; ENSG00000138639.18. [Q8N264-1]
DR Ensembl; ENST00000503995.5; ENSP00000423206.1; ENSG00000138639.18. [Q8N264-4]
DR GeneID; 83478; -.
DR KEGG; hsa:83478; -.
DR MANE-Select; ENST00000395184.6; ENSP00000378611.1; NM_001025616.3; NP_001020787.2.
DR UCSC; uc003hpj.4; human. [Q8N264-1]
DR CTD; 83478; -.
DR DisGeNET; 83478; -.
DR GeneCards; ARHGAP24; -.
DR HGNC; HGNC:25361; ARHGAP24.
DR HPA; ENSG00000138639; Tissue enhanced (kidney).
DR MalaCards; ARHGAP24; -.
DR MIM; 610586; gene.
DR neXtProt; NX_Q8N264; -.
DR OpenTargets; ENSG00000138639; -.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR PharmGKB; PA134934054; -.
DR VEuPathDB; HostDB:ENSG00000138639; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00950000183015; -.
DR HOGENOM; CLU_047977_1_0_1; -.
DR InParanoid; Q8N264; -.
DR OMA; ELLYYYK; -.
DR OrthoDB; 917149at2759; -.
DR PhylomeDB; Q8N264; -.
DR TreeFam; TF323577; -.
DR PathwayCommons; Q8N264; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR SignaLink; Q8N264; -.
DR SIGNOR; Q8N264; -.
DR BioGRID-ORCS; 83478; 20 hits in 1075 CRISPR screens.
DR ChiTaRS; ARHGAP24; human.
DR GeneWiki; ARHGAP24; -.
DR GenomeRNAi; 83478; -.
DR Pharos; Q8N264; Tbio.
DR PRO; PR:Q8N264; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8N264; protein.
DR Bgee; ENSG00000138639; Expressed in renal medulla and 180 other tissues.
DR ExpressionAtlas; Q8N264; baseline and differential.
DR Genevisible; Q8N264; HS.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IBA:GO_Central.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IBA:GO_Central.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Cell junction; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..748
FT /note="Rho GTPase-activating protein 24"
FT /id="PRO_0000280473"
FT DOMAIN 19..125
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 135..329
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 649..729
FT /evidence="ECO:0000255"
FT COMPBIAS 354..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2Z7"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16862148"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4V1"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4V1"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16862148"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16862148"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16862148,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16862148"
FT MOD_RES 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16862148"
FT VAR_SEQ 1..95
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023711"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_023712"
FT VAR_SEQ 1
FT /note="M -> MWLRKKDWQIFNEQFLKKEHAVGFCFSKCVLVEFSLKCFKKIKSSYW
FT NNDALAFLGKKFLREKNKMTKKQTRNRQNKFPPKPALRSSPVHRVQHFPLLWKVKEPHY
FT HLFFFAFSYCWSWEPFPSEQQPCPASVLSSQQGKSISLIM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023713"
FT VAR_SEQ 91..94
FT /note="GDRD -> KIFS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023714"
FT VAR_SEQ 94..130
FT /note="DRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGG -> MPEDRNSGGCP
FT AGALASTPFIPKTTYRRIKRCFSFRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_023715"
FT VAR_SEQ 95..748
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023716"
FT VAR_SEQ 245..246
FT /note="GV -> VS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023717"
FT VAR_SEQ 247..748
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023718"
FT MUTAGEN 175
FT /note="R->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:15302923,
FT ECO:0000269|PubMed:15611138"
FT MUTAGEN 175
FT /note="R->K: Does not abolish the effect on actin stress
FT fibers but moderates its capability to induce membrane
FT protrusions."
FT /evidence="ECO:0000269|PubMed:15302923,
FT ECO:0000269|PubMed:15611138"
FT CONFLICT 140
FT /note="T -> A (in Ref. 2; BAC03606)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="Q -> L (in Ref. 1; CAB66581)"
FT /evidence="ECO:0000305"
FT CONFLICT 722
FT /note="M -> V (in Ref. 2; BAC03606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 748 AA; 84258 MW; 87A8E6DCA6869229 CRC64;
MEENNDSTEN PQQGQGRQNA IKCGWLRKQG GFVKTWHTRW FVLKGDQLYY FKDEDETKPL
GTIFLPGNKV SEHPCNEENP GKFLFEVVPG GDRDRMTANH ESYLLMASTQ NDMEDWVKSI
RRVIWGPFGG GIFGQKLEDT VRYEKRYGNR LAPMLVEQCV DFIRQRGLKE EGLFRLPGQA
NLVKELQDAF DCGEKPSFDS NTDVHTVASL LKLYLRELPE PVIPYAKYED FLSCAKLLSK
EEEAGVKELA KQVKSLPVVN YNLLKYICRF LDEVQSYSGV NKMSVQNLAT VFGPNILRPK
VEDPLTIMEG TVVVQQLMSV MISKHDCLFP KDAELQSKPQ DGVSNNNEIQ KKATMGQLQN
KENNNTKDSP SRQCSWDKSE SPQRSSMNNG SPTALSGSKT NSPKNSVHKL DVSRSPPLMV
KKNPAFNKGS GIVTNGSFSS SNAEGLEKTQ TTPNGSLQAR RSSSLKVSGT KMGTHSVQNG
TVRMGILNSD TLGNPTNVRN MSWLPNGYVT LRDNKQKEQA GELGQHNRLS TYDNVHQQFS
MMNLDDKQSI DSATWSTSSC EISLPENSNS CRSSTTTCPE QDFFGGNFED PVLDGPPQDD
LSHPRDYESK SDHRSVGGRS SRATSSSDNS ETFVGNSSSN HSALHSLVSS LKQEMTKQKI
EYESRIKSLE QRNLTLETEM MSLHDELDQE RKKFTMIEIK MRNAERAKED AEKRNDMLQK
EMEQFFSTFG ELTVEPRRTE RGNTIWIQ
