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Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1 (Centaurin-delta-2) (Cnt-d2)

 ARAP1_HUMAN             Reviewed;        1450 AA.
Q96P48; A3KLL7; B2RTS2; O94879; Q4LDD5; Q59FI7; Q6PHS3; Q8WU51;
Q96HP6; Q96L71;
27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 3.
30-AUG-2017, entry version 160.
RecName: Full=Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1;
AltName: Full=Centaurin-delta-2;
Short=Cnt-d2;
Name=ARAP1; Synonyms=CENTD2, KIAA0782;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=11804590; DOI=10.1016/S1097-2765(02)00428-8;
Miura K., Jacques K.M., Stauffer S., Kubosaki A., Zhu K., Hirsch D.S.,
Resau J., Zheng Y., Randazzo P.A.;
"ARAP1: a point of convergence for Arf and Rho signaling.";
Mol. Cell 9:109-119(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
Krugmann S., Coadwell J., Stephens L.R., Hawkins P.T.;
"ARAP1 splice variants in man and mouse.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:277-286(1998).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Randazzo P.A., Yoon H.-Y., Miura K.;
"Human ARAP1b.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
GLU-1047.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 792-1450 (ISOFORMS 2/3/5).
TISSUE=Brain, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 315-1450 (ISOFORM 1).
Hong W.;
"KIAA0782 as a member (centaurin delta2) of the ArfGAP centaurin
family.";
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-354, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
INTERACTION WITH TNFRSF10A, AND SUBCELLULAR LOCATION.
PubMed=18165900; DOI=10.1007/s10495-007-0171-8;
Simova S., Klima M., Cermak L., Sourkova V., Andera L.;
"Arf and Rho GAP adapter protein ARAP1 participates in the
mobilization of TRAIL-R1/DR4 to the plasma membrane.";
Apoptosis 13:423-436(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; TYR-431 AND
SER-1435, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738 AND SER-1435, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428; TYR-504; SER-738
AND SER-1428, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent
GTPase-activating protein that modulates actin cytoskeleton
remodeling by regulating ARF and RHO family members. Is activated
by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3)
binding. Can be activated by phosphatidylinositol 3,4-bisphosphate
(PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Has a
preference for ARF1 and ARF5 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:11804590}.
-!- SUBUNIT: Interacts with TNFRSF10A. {ECO:0000269|PubMed:18165900}.
-!- INTERACTION:
P27958:- (xeno); NbExp=3; IntAct=EBI-710003, EBI-8753518;
O00220:TNFRSF10A; NbExp=4; IntAct=EBI-710003, EBI-518861;
P12956:XRCC6; NbExp=2; IntAct=EBI-710003, EBI-353208;
-!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack
membrane; Peripheral membrane protein. Cell membrane.
Note=Associated with Golgi stacks in resting cells. Throughout the
cytoplasm and in surface protrusion in cells that are in the
process of attaching to a surface and spreading.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=6;
IsoId=Q96P48-6; Sequence=Displayed;
Name=1;
IsoId=Q96P48-1; Sequence=VSP_036607, VSP_036608;
Name=2;
IsoId=Q96P48-2; Sequence=VSP_036607, VSP_036608, VSP_000311;
Name=3;
IsoId=Q96P48-3; Sequence=VSP_000311;
Name=4;
IsoId=Q96P48-4; Sequence=VSP_015000;
Note=No experimental confirmation available.;
Name=5;
IsoId=Q96P48-5; Sequence=VSP_014998, VSP_015001, VSP_000311;
Note=No experimental confirmation available.;
Name=7;
IsoId=Q96P48-7; Sequence=VSP_015000, VSP_043530, VSP_000311;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in heart, skeletal muscle, spleen,
kidney, liver, placenta, lung, peripheral blood leukocytes,
adrenal gland, bone marrow, brain, lymph node, mammary gland,
prostate, spinal cord, stomach, thyroid and trachea.
{ECO:0000269|PubMed:11804590}.
-!- SEQUENCE CAUTION:
Sequence=BAA34502.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAD92710.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY049732; AAL12169.1; -; mRNA.
EMBL; AJ621557; CAF21317.1; -; mRNA.
EMBL; AB018325; BAA34502.2; ALT_INIT; mRNA.
EMBL; AY553630; AAT36325.1; -; mRNA.
EMBL; AB209473; BAD92710.1; ALT_INIT; mRNA.
EMBL; AP002381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP003065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC008315; AAH08315.1; -; mRNA.
EMBL; BC021244; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC056401; AAH56401.1; -; mRNA.
EMBL; BC140792; AAI40793.1; -; mRNA.
EMBL; AF411983; AAL04167.1; -; mRNA.
CCDS; CCDS41687.1; -. [Q96P48-6]
CCDS; CCDS44671.1; -. [Q96P48-7]
CCDS; CCDS8217.2; -. [Q96P48-4]
PIR; C59431; C59431.
RefSeq; NP_001035207.1; NM_001040118.2. [Q96P48-6]
RefSeq; NP_001128662.1; NM_001135190.1. [Q96P48-7]
RefSeq; NP_056057.2; NM_015242.4. [Q96P48-4]
UniGene; Hs.503165; -.
PDB; 4X1V; X-ray; 1.58 A; B=76-91.
PDBsum; 4X1V; -.
ProteinModelPortal; Q96P48; -.
SMR; Q96P48; -.
BioGrid; 125548; 26.
IntAct; Q96P48; 14.
MINT; MINT-1395507; -.
STRING; 9606.ENSP00000377233; -.
iPTMnet; Q96P48; -.
PhosphoSitePlus; Q96P48; -.
BioMuta; ARAP1; -.
DMDM; 226694321; -.
EPD; Q96P48; -.
PaxDb; Q96P48; -.
PeptideAtlas; Q96P48; -.
PRIDE; Q96P48; -.
Ensembl; ENST00000334211; ENSP00000335506; ENSG00000186635. [Q96P48-4]
Ensembl; ENST00000359373; ENSP00000352332; ENSG00000186635. [Q96P48-3]
Ensembl; ENST00000393605; ENSP00000377230; ENSG00000186635. [Q96P48-1]
Ensembl; ENST00000393609; ENSP00000377233; ENSG00000186635. [Q96P48-6]
Ensembl; ENST00000429686; ENSP00000403127; ENSG00000186635. [Q96P48-7]
GeneID; 116985; -.
KEGG; hsa:116985; -.
UCSC; uc001osr.4; human. [Q96P48-6]
CTD; 116985; -.
DisGeNET; 116985; -.
GeneCards; ARAP1; -.
H-InvDB; HIX0079401; -.
H-InvDB; HIX0171326; -.
HGNC; HGNC:16925; ARAP1.
HPA; CAB020703; -.
HPA; HPA070383; -.
MIM; 606646; gene.
neXtProt; NX_Q96P48; -.
OpenTargets; ENSG00000186635; -.
PharmGKB; PA164715867; -.
eggNOG; KOG1117; Eukaryota.
eggNOG; COG5347; LUCA.
GeneTree; ENSGT00860000133715; -.
HOGENOM; HOG000246988; -.
HOVERGEN; HBG106625; -.
InParanoid; Q96P48; -.
KO; K18439; -.
OMA; GAPETSH; -.
OrthoDB; EOG091G00AN; -.
PhylomeDB; Q96P48; -.
TreeFam; TF105769; -.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
ChiTaRS; ARAP1; human.
GeneWiki; CENTD2; -.
GenomeRNAi; 116985; -.
PRO; PR:Q96P48; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000186635; -.
CleanEx; HS_ARAP1; -.
ExpressionAtlas; Q96P48; baseline and differential.
Genevisible; Q96P48; HS.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
GO; GO:0031702; F:type 1 angiotensin receptor binding; IEA:Ensembl.
GO; GO:0030037; P:actin filament reorganization involved in cell cycle; TAS:UniProtKB.
GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:UniProtKB.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0051270; P:regulation of cellular component movement; IMP:UniProtKB.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 2.30.29.30; -; 5.
InterPro; IPR001164; ArfGAP.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR000159; RA_dom.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
Pfam; PF01412; ArfGap; 1.
Pfam; PF00169; PH; 3.
Pfam; PF00788; RA; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF00536; SAM_1; 1.
PRINTS; PR00405; REVINTRACTNG.
SMART; SM00105; ArfGap; 1.
SMART; SM00233; PH; 5.
SMART; SM00324; RhoGAP; 1.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF50729; SSF50729; 6.
PROSITE; PS50115; ARFGAP; 1.
PROSITE; PS50003; PH_DOMAIN; 4.
PROSITE; PS50200; RA; 1.
PROSITE; PS50238; RHOGAP; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Cytoplasm; Golgi apparatus; GTPase activation; Membrane;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Zinc; Zinc-finger.
CHAIN 1 1450 Arf-GAP with Rho-GAP domain, ANK repeat
and PH domain-containing protein 1.
/FTId=PRO_0000074214.
DOMAIN 6 70 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 327 419 PH 1. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 440 529 PH 2. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 535 660 Arf-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00288}.
DOMAIN 743 850 PH 3. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 954 1139 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
DOMAIN 1172 1261 Ras-associating. {ECO:0000255|PROSITE-
ProRule:PRU00166}.
DOMAIN 1274 1396 PH 4. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
ZN_FING 550 576 C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00288}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 354 354 Phosphothreonine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 428 428 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 431 431 Phosphotyrosine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 504 504 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1428 1428 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1435 1435 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
VAR_SEQ 1 760 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014998.
VAR_SEQ 1 245 Missing (in isoform 4 and isoform 7).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9872452}.
/FTId=VSP_015000.
VAR_SEQ 1 240 Missing (in isoform 1 and isoform 2).
{ECO:0000303|PubMed:11804590,
ECO:0000303|Ref.5, ECO:0000303|Ref.9}.
/FTId=VSP_036607.
VAR_SEQ 241 249 APARVMTKK -> MTLSGSRGQ (in isoform 1 and
isoform 2). {ECO:0000303|PubMed:11804590,
ECO:0000303|Ref.5, ECO:0000303|Ref.9}.
/FTId=VSP_036608.
VAR_SEQ 604 664 Missing (in isoform 7).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043530.
VAR_SEQ 761 767 QDRRARE -> MDASGKG (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015001.
VAR_SEQ 1320 1330 Missing (in isoform 2, isoform 3, isoform
5 and isoform 7).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.6}.
/FTId=VSP_000311.
VARIANT 358 358 R -> Q (in dbSNP:rs34976830).
/FTId=VAR_055529.
VARIANT 1047 1047 Q -> E (in dbSNP:rs56200889).
{ECO:0000269|Ref.6}.
/FTId=VAR_061023.
CONFLICT 1408 1408 V -> M (in Ref. 8; AAH56401).
{ECO:0000305}.
SEQUENCE 1450 AA; 162192 MW; A4B6CCC28EC4CD0D CRC64;
MAEAGDAALS VAEWLRALHL EQYTGLFEQH GLVWATECQG LSDTRLMDMG MLLPGHRRRI
LAGLLRAHTS PAPAPRPTPR PVPMKRHIFR SPPVPATPPE PLPTTTEDEG LPAAPPIPPR
RSCLPPTCFT TPSTAAPDPV LPPLPAKRHL AELSVPPVPP RTGPPRLLVS LPTKEEESLL
PSLSSPPQPQ SEEPLSTLPQ GPPQPPSPPP CPPEIPPKPV RLFPEFDDSD YDEVPEEGPG
APARVMTKKE EPPPSRVPRA VRVASLLSEG EELSGDDQGD EEEDDHAYEG VPNGGWHTSS
LSLSLPSTIA APHPMDGPPG GSTPVTPVIK AGWLDKNPPQ GSYIYQKRWV RLDTDHLRYF
DSNKDAYSKR FISVACISHV AAIGDQKFEV ITNNRTFAFR AESDVERKEW MQALQQAMAE
QRARARLSSA YLLGVPGSEQ PDRAGSLELR GFKNKLYVAV VGDKVQLYKN LEEYHLGIGI
TFIDMSVGNV KEVDRRSFDL TTPYRIFSFS ADSELEKEQW LEAMQGAIAE ALSTSEVAER
IWAAAPNRFC ADCGAPQPDW ASINLCVVIC KRCAGEHRGL GAGVSKVRSL KMDRKVWTET
LIELFLQLGN GAGNRFWAAN VPPSEALQPS SSPSTRRCHL EAKYREGKYR RYHPLFGNQE
ELDKALCAAV TTTDLAETQA LLGCGAGINC FSGDPEAPTP LALAEQAGQT LQMEFLRNNR
TTEVPRLDSM KPLEKHYSVV LPTVSHSGFL YKTASAGKLL QDRRAREEFS RRWCVLGDGV
LSYFENERAV TPNGEIRASE IVCLAVPPPD THGFEHTFEV YTEGERLYLF GLESAEQAHE
WVKCIAKAFV PPLAEDLLAR DFERLGRLPY KAGLSLQRAQ EGWFSLSGSE LRAVFPEGPC
EEPLQLRKLQ ELSIQGDSEN QVLVLVERRR TLYIQGERRL DFMGWLGAIQ KAAASMGDTL
SEQQLGDSDI PVIVYRCVDY ITQCGLTSEG IYRKCGQTSK TQRLLESLRQ DARSVHLKEG
EQHVDDVSSA LKRFLRDLPD GLFTRAQRLT WLEASEIEDE EEKVSRYREL LVRLPPVNRA
TVKALISHLY CVQCFSDTNQ MNVHNLAIVF GPTLFQTDGQ DYKAGRVVED LINHYVVVFS
VDEEELRKQR EEITAIVKMR VAGTASGTQH AGDFICTVYL EEKKAETEQH IKVPASMTAE
ELTLEILDRR NVGIREKDYW TCFEVNEREE AERPLHFAEK VLPILHGLGT DSHLVVKKHQ
AMEAMLLYLA SRVGDTKHGM MKFREDRSLL GLGLPSGGFH DRYFILNSSC LRLYKEVRSQ
RPWSGAPETS HRPEKEWPIK SLKVYLGVKK KLRPPTCWGF TVVHETEKHE KQQWYLCCDT
QMELREWFAT FLFVQHDGLV WPSEPSRVSR AVPEVRLGSV SLIPLRGSEN EMRRSVAAFT
ADPLSLLRNV


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