RGPA2_HUMAN
ID RGPA2_HUMAN Reviewed; 1873 AA.
AC Q2PPJ7; Q4VXU6; Q5JUA3; Q5JUA4; Q5T9K3; Q96CX9; Q9BQT7; Q9H9D9; Q9ULE8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ral GTPase-activating protein subunit alpha-2;
DE AltName: Full=250 kDa substrate of Akt;
DE Short=AS250;
DE AltName: Full=p220;
GN Name=RALGAPA2; Synonyms=C20orf74, KIAA1272;
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 [MRNA] (ISOFORM 1), INTERACTION WITH RALGAPB,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-486; SER-696 AND THR-715.
RX PubMed=16490346; DOI=10.1016/j.cellsig.2006.01.002;
RA Gridley S., Chavez J.A., Lane W.S., Lienhard G.E.;
RT "Adipocytes contain a novel complex similar to the tuberous sclerosis
RT complex.";
RL Cell. Signal. 18:1626-1632(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 813-1873 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1539-1873 (ISOFORM 2).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1571-1873 (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820 AND SER-821, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820 AND SER-821, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486; SER-696; SER-820 AND
RP SER-821, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486; SER-820 AND SER-1593,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Catalytic subunit of the heterodimeric RalGAP2 complex which
CC acts as a GTPase activator for the Ras-like small GTPases RALA and
CC RALB. {ECO:0000250}.
CC -!- SUBUNIT: Component of the heterodimeric RalGAP2 complex with RALGAPB.
CC Heterodimerization is required for activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16490346}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2PPJ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2PPJ7-2; Sequence=VSP_025247;
CC Name=3;
CC IsoId=Q2PPJ7-3; Sequence=VSP_025248;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH13749.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14290.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ310704; ABC33805.1; -; mRNA.
DR EMBL; AL078634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB033098; BAA86586.1; -; mRNA.
DR EMBL; AK022881; BAB14290.1; ALT_INIT; mRNA.
DR EMBL; BC013749; AAH13749.1; ALT_FRAME; mRNA.
DR CCDS; CCDS46584.1; -. [Q2PPJ7-1]
DR RefSeq; NP_065076.2; NM_020343.3. [Q2PPJ7-1]
DR AlphaFoldDB; Q2PPJ7; -.
DR SMR; Q2PPJ7; -.
DR BioGRID; 121435; 30.
DR IntAct; Q2PPJ7; 7.
DR MINT; Q2PPJ7; -.
DR STRING; 9606.ENSP00000202677; -.
DR iPTMnet; Q2PPJ7; -.
DR PhosphoSitePlus; Q2PPJ7; -.
DR SwissPalm; Q2PPJ7; -.
DR BioMuta; RALGAPA2; -.
DR DMDM; 147742932; -.
DR EPD; Q2PPJ7; -.
DR jPOST; Q2PPJ7; -.
DR MassIVE; Q2PPJ7; -.
DR MaxQB; Q2PPJ7; -.
DR PaxDb; Q2PPJ7; -.
DR PeptideAtlas; Q2PPJ7; -.
DR PRIDE; Q2PPJ7; -.
DR ProteomicsDB; 61429; -. [Q2PPJ7-1]
DR ProteomicsDB; 61430; -. [Q2PPJ7-2]
DR ProteomicsDB; 61431; -. [Q2PPJ7-3]
DR Antibodypedia; 59154; 55 antibodies from 16 providers.
DR DNASU; 57186; -.
DR Ensembl; ENST00000202677.12; ENSP00000202677.6; ENSG00000188559.16. [Q2PPJ7-1]
DR GeneID; 57186; -.
DR KEGG; hsa:57186; -.
DR MANE-Select; ENST00000202677.12; ENSP00000202677.6; NM_020343.4; NP_065076.2.
DR UCSC; uc002wrz.4; human. [Q2PPJ7-1]
DR CTD; 57186; -.
DR DisGeNET; 57186; -.
DR GeneCards; RALGAPA2; -.
DR HGNC; HGNC:16207; RALGAPA2.
DR HPA; ENSG00000188559; Low tissue specificity.
DR MIM; 618836; gene.
DR neXtProt; NX_Q2PPJ7; -.
DR OpenTargets; ENSG00000188559; -.
DR PharmGKB; PA25784; -.
DR VEuPathDB; HostDB:ENSG00000188559; -.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00950000183139; -.
DR HOGENOM; CLU_001676_0_0_1; -.
DR InParanoid; Q2PPJ7; -.
DR OMA; WWPREQM; -.
DR OrthoDB; 157372at2759; -.
DR PhylomeDB; Q2PPJ7; -.
DR TreeFam; TF324484; -.
DR PathwayCommons; Q2PPJ7; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR SignaLink; Q2PPJ7; -.
DR BioGRID-ORCS; 57186; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; RALGAPA2; human.
DR GenomeRNAi; 57186; -.
DR Pharos; Q2PPJ7; Tdark.
DR PRO; PR:Q2PPJ7; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q2PPJ7; protein.
DR Bgee; ENSG00000188559; Expressed in tibialis anterior and 185 other tissues.
DR ExpressionAtlas; Q2PPJ7; baseline and differential.
DR Genevisible; Q2PPJ7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR InterPro; IPR027107; Tuberin/Ral-act_asu.
DR PANTHER; PTHR10063; PTHR10063; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1873
FT /note="Ral GTPase-activating protein subunit alpha-2"
FT /id="PRO_0000286972"
FT DOMAIN 1635..1843
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 341..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..846
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A3KGS3"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A3KGS3"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A3KGS3"
FT MOD_RES 486
FT /note="Phosphoserine; by PKB"
FT /evidence="ECO:0000269|PubMed:16490346,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 696
FT /note="Phosphoserine; by PKB"
FT /evidence="ECO:0000269|PubMed:16490346,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 715
FT /note="Phosphothreonine; by PKB"
FT /evidence="ECO:0000269|PubMed:16490346"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1832..1873
FT /note="FYEERALYLEAIIQNHREVMTFEDFAAQVFSPSPSYSLSGTD -> LYLFAL
FT NV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025247"
FT VAR_SEQ 1832..1873
FT /note="FYEERALYLEAIIQNHREVMTFEDFAAQVFSPSPSYSLSGTD -> PRVR
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10574462"
FT /id="VSP_025248"
FT VARIANT 492
FT /note="S -> N (in dbSNP:rs6137081)"
FT /id="VAR_049157"
FT CONFLICT 1488
FT /note="N -> S (in Ref. 1; ABC33805 and 3; BAA86586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1873 AA; 210770 MW; DC33C087B4802541 CRC64;
MFSRRSHGDV KKSTQKVLDP KKDVLTRLKH LRALLDNVDA NDLKQFFETN YSQIYFIFYE
NFIALENSLK LKGNNKSQRE ELDSILFLFE KILQFLPERI FFRWHYQSIG STLKKLLHTG
NSIKIRCEGI RLFLLWLQAL QTNCAEEQVL IFACLVPGFP AVMSSRGPCT LETLINPSPS
VADVKIYPEE ITPLLPAISG EKIAEDQTCF FLQILLKYMV IQAASLEWKN KENQDTGFKF
LFTLFRKYYL PHLFPSFTKL TNIYKPVLDI PHLRPKPVYI TTTRDNENIY STKIPYMAAR
VVFIKWIVTF FLEKKYLTAT QNTKNGVDVL PKIIQTVGGG AVQERAPELD GGGPTEQDKS
HSNSSTLSDR RLSNSSLCSI EEEHRMVYEM VQRILLSTRG YVNFVNEVFH QAFLLPSCEI
AVTRKVVQVY RKWILQDKPV FMEEPDRKDV AQEDAEKLGF SETDSKEASS ESSGHKRSSS
WGRTYSFTSA MSRGCVTEEE NTNVKAGVQA LLQVFLTNSA NIFLLEPCAE VPVLLKEQVD
ACKAVLIIFR RMIMELTMNK KTWEQMLQIL LRITEAVMQK PKDKQIKDLF AQSLAGLLFR
TLMVAWIRAN LCVYISRELW DDFLGVLSSL TEWEELINEW ANIMDSLTAV LARTVYGVEM
TNLPLDKLSE QKEKKQRGKG CVLDPQKGTT VGRSFSLSWR SHPDVTEPMR FRSATTSGAP
GVEKARNIVR QKATEVEECQ QSENAPAAGS GHLTVGQQQQ VLRSSSTSDI PEPLCSDSSQ
GQKAENTQNS SSSEPQPIQE NKGHVKREHE GITILVRRSS SPAELDLKDD LQQTQGKCRE
RQKSESTNSD TTLGCTNEAE LSMGPWQTCE EDPELNTPTD VVADADARHW LQLSPTDASN
LTDSSECLTD DCSIIAGGSL TGWHPDSAAV LWRRVLGILG DVNNIQSPKI HARVFCYLYE
LWYKLAKIRD NLAISLDNQS SPSPPVLIPP LRMFASWLFK AATLPNEYKE GKLQAYRLIC
AMMTRRQDVL PNSDFLVHFY LVMHLGLTSE DQDILNTIIR HCPPRFFSLG FPGFSMLVGD
FITAAARVLS TDILTAPRSE AVTVLGSLVC FPNTYQEIPL LQSVPEVNEA ITGTEDVKHY
LINILLKNAT EEPNEYARCI AVCSLGVWIC EELAQCTSHP QVKEAINVIG VTLKFPNKIV
AQVACDVLQL LVSYWEKLQM FETSLPRKMA EILVATVAFL LPSAEYSSVE TDKKFIVSLL
LCLLDWCMAL PVSVLLHPVS TAVLEEQHSA RAPLLDYIYR VLHCCVCGSS TYTQQSHYIL
TLADLSSTDY DPFLPLANVK SSEPVQYHSS AELGNLLTVE EEKKRRSLEL IPLTARMVMA
HLVNHLGHYP LSGGPAILHS LVSENHDNAH VEGSELSFEV FRSPNLQLFV FNDSTLISYL
QTPTEGPVGG SPVGSLSDVR VIVRDISGKY SWDGKVLYGP LEGCLAPNGR NPSFLISSWH
RDTFGPQKDS SQVEEGDDVL DKLLENIGHT SPECLLPSQL NLNEPSLTPC GMNYDQEKEI
IEVILRQNAQ EDEYIQSHNF DSAMKVTSQG QPSPVEPRGP FYFCRLLLDD LGMNSWDRRK
NFHLLKKNSK LLRELKNLDS RQCRETHKIA VFYIAEGQED KCSILSNERG SQAYEDFVAG
LGWEVDLSTH CGFMGGLQRN GSTGQTAPYY ATSTVEVIFH VSTRMPSDSD DSLTKKLRHL
GNDEVHIVWS EHSRDYRRGI IPTAFGDVSI IIYPMKNHMF FIAITKKPEV PFFGPLFDGA
IVSGKLLPSL VCATCINASR AVKCLIPLYQ SFYEERALYL EAIIQNHREV MTFEDFAAQV
FSPSPSYSLS GTD
