ACAP2_HUMAN
ID ACAP2_HUMAN Reviewed; 778 AA.
AC Q15057; A8K2V4; Q8N5Z8; Q9UQR3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2;
DE AltName: Full=Centaurin-beta-2;
DE Short=Cnt-b2;
GN Name=ACAP2; Synonyms=CENTB2, KIAA0041;
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], FUNCTION, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF ARG-442.
RC TISSUE=Leukocyte;
RX PubMed=11062263; DOI=10.1083/jcb.151.3.627;
RA Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J., Hsu V.W.,
RA Donaldson J.G., Randazzo P.A.;
RT "ACAPs are arf6 GTPase-activating proteins that function in the cell
RT periphery.";
RL J. Cell Biol. 151:627-638(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584044; DOI=10.1093/dnares/1.5.223;
RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N.,
RA Kawarabayasi Y., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. II. The
RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 1:223-229(1994).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-742, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521; SER-581 AND SER-775, AND
RP 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 [16]
RP 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: GTPase-activating protein (GAP) for ADP ribosylation factor 6
CC (ARF6). {ECO:0000269|PubMed:11062263}.
CC -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2) and phosphatidic acid.
CC {ECO:0000269|PubMed:11062263}.
CC -!- SUBUNIT: Interacts with RAB35 (GTP-bound form); the interaction is
CC direct and probably recruits ACAP2 to membranes. Interacts with
CC MICALL1; the interaction is indirect through RAB35 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level in lung.
CC {ECO:0000269|PubMed:11062263}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA05064.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB41450.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ238248; CAB41450.1; ALT_FRAME; mRNA.
DR EMBL; D26069; BAA05064.2; ALT_INIT; mRNA.
DR EMBL; AK290369; BAF83058.1; -; mRNA.
DR EMBL; CH471052; EAW78027.1; -; Genomic_DNA.
DR EMBL; BC031005; AAH31005.1; -; mRNA.
DR EMBL; BC060767; AAH60767.1; -; mRNA.
DR CCDS; CCDS33924.1; -.
DR RefSeq; NP_036419.3; NM_012287.5.
DR PDB; 6IF3; X-ray; 1.50 A; A=601-770.
DR PDBsum; 6IF3; -.
DR AlphaFoldDB; Q15057; -.
DR SMR; Q15057; -.
DR BioGRID; 117073; 36.
DR IntAct; Q15057; 12.
DR MINT; Q15057; -.
DR STRING; 9606.ENSP00000324287; -.
DR GlyGen; Q15057; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15057; -.
DR MetOSite; Q15057; -.
DR PhosphoSitePlus; Q15057; -.
DR BioMuta; ACAP2; -.
DR DMDM; 39932727; -.
DR EPD; Q15057; -.
DR jPOST; Q15057; -.
DR MassIVE; Q15057; -.
DR MaxQB; Q15057; -.
DR PaxDb; Q15057; -.
DR PeptideAtlas; Q15057; -.
DR PRIDE; Q15057; -.
DR ProteomicsDB; 60412; -.
DR Antibodypedia; 19460; 219 antibodies from 36 providers.
DR DNASU; 23527; -.
DR Ensembl; ENST00000326793.11; ENSP00000324287.6; ENSG00000114331.16.
DR GeneID; 23527; -.
DR KEGG; hsa:23527; -.
DR MANE-Select; ENST00000326793.11; ENSP00000324287.6; NM_012287.6; NP_036419.3.
DR UCSC; uc003fun.5; human.
DR CTD; 23527; -.
DR DisGeNET; 23527; -.
DR GeneCards; ACAP2; -.
DR HGNC; HGNC:16469; ACAP2.
DR HPA; ENSG00000114331; Low tissue specificity.
DR MIM; 607766; gene.
DR neXtProt; NX_Q15057; -.
DR OpenTargets; ENSG00000114331; -.
DR PharmGKB; PA26407; -.
DR VEuPathDB; HostDB:ENSG00000114331; -.
DR eggNOG; KOG0521; Eukaryota.
DR GeneTree; ENSGT00940000156389; -.
DR HOGENOM; CLU_012513_0_1_1; -.
DR InParanoid; Q15057; -.
DR OMA; GSVMSCE; -.
DR OrthoDB; 751525at2759; -.
DR PhylomeDB; Q15057; -.
DR TreeFam; TF318315; -.
DR PathwayCommons; Q15057; -.
DR SignaLink; Q15057; -.
DR BioGRID-ORCS; 23527; 46 hits in 1078 CRISPR screens.
DR ChiTaRS; ACAP2; human.
DR GeneWiki; CENTB2; -.
DR GenomeRNAi; 23527; -.
DR Pharos; Q15057; Tbio.
DR PRO; PR:Q15057; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q15057; protein.
DR Bgee; ENSG00000114331; Expressed in epithelium of nasopharynx and 201 other tissues.
DR ExpressionAtlas; Q15057; baseline and differential.
DR Genevisible; Q15057; HS.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030029; P:actin filament-based process; IDA:MGI.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23180; PTHR23180; 2.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Coiled coil; Endosome; GTPase activation;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..778
FT /note="Arf-GAP with coiled-coil, ANK repeat and PH domain-
FT containing protein 2"
FT /id="PRO_0000074210"
FT DOMAIN 1..226
FT /note="BAR"
FT DOMAIN 266..361
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 399..520
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REPEAT 640..669
FT /note="ANK 1"
FT REPEAT 673..702
FT /note="ANK 2"
FT REPEAT 706..735
FT /note="ANK 3"
FT ZN_FING 414..437
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT REGION 371..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQK5"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZQK5"
FT MOD_RES 742
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 442
FT /note="R->Q: Loss of GAP activity."
FT /evidence="ECO:0000269|PubMed:11062263"
FT CONFLICT 5
FT /note="V -> G (in Ref. 1; CAB41450)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="C -> G (in Ref. 1; CAB41450)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="V -> G (in Ref. 1; CAB41450)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="S -> R (in Ref. 1; CAB41450)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="E -> K (in Ref. 1; CAB41450)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="L -> V (in Ref. 1; CAB41450)"
FT /evidence="ECO:0000305"
FT CONFLICT 564
FT /note="G -> E (in Ref. 6; AAH60767)"
FT /evidence="ECO:0000305"
FT HELIX 606..615
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 619..627
FT /evidence="ECO:0007829|PDB:6IF3"
FT TURN 637..641
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 644..651
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 654..662
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 677..684
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 687..695
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 710..716
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 720..737
FT /evidence="ECO:0007829|PDB:6IF3"
FT HELIX 753..757
FT /evidence="ECO:0007829|PDB:6IF3"
SQ SEQUENCE 778 AA; 88029 MW; 64B620957FEE6195 CRC64;
MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCVANKQFM
NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF
KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEATNILT ATRKCFRHIA LDYVLQINVL
QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ
KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI
ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES ALQRVQCIPG NASCCDCGLA
DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE
ANVEKMGIKK PQPGQRQEKE AYIRAKYVER KFVDKYSISL SPPEQQKKFV SKSSEEKRLS
ISKFGPGDQV RASAQSSVRS NDSGIQQSSD DGRESLPSTV SANSLYEPEG ERQDSSMFLD
SKHLNPGLQL YRASYEKNLP KMAEALAHGA DVNWANSEEN KATPLIQAVL GGSLVTCEFL
LQNGANVNQR DVQGRGPLHH ATVLGHTGQV CLFLKRGANQ HATDEEGKDP LSIAVEAANA
DIVTLLRLAR MNEEMRESEG LYGQPGDETY QDIFRDFSQM ASNNPEKLNR FQQDSQKF
