PKHA8_HUMAN
ID PKHA8_HUMAN Reviewed; 519 AA.
AC Q96JA3; B4DH00; Q7Z5V8; Q9BU78; Q9H274; Q9H8Z7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Pleckstrin homology domain-containing family A member 8;
DE Short=PH domain-containing family A member 8;
DE AltName: Full=Phosphatidylinositol-four-phosphate adapter protein 2;
DE Short=FAPP-2;
DE Short=Phosphoinositol 4-phosphate adapter protein 2;
DE Short=hFAPP2;
DE AltName: Full=Serologically defined breast cancer antigen NY-BR-86;
GN Name=PLEKHA8; Synonyms=FAPP2;
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).
RC TISSUE=Brain;
RX PubMed=11001876; DOI=10.1042/0264-6021:3510019;
RA Dowler S.J., Currie R.A., Campbell D.G., Deak M., Kular G., Downes C.P.,
RA Alessi D.R.;
RT "Identification of pleckstrin-homology-domain-containing proteins with
RT novel phosphoinositide-binding specificities.";
RL Biochem. J. 351:19-31(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-365.
RC TISSUE=Mammary gland;
RX PubMed=12747765;
RA Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., Gure A.O.,
RA Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.;
RT "Humoral immunity to human breast cancer: antigen definition and
RT quantitative analysis of mRNA expression.";
RL Cancer Immun. 1:4-4(2001).
RN [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH ARF1, DOMAIN, PHOSPHOLIPID-BINDING,
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15107860; DOI=10.1038/ncb1119;
RA Godi A., Di Campli A., Konstantakopoulos A., Di Tullio G., Alessi D.R.,
RA Kular G.S., Daniele T., Marra P., Lucocq J.M., De Matteis M.A.;
RT "FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and
RT PtdIns(4)P.";
RL Nat. Cell Biol. 6:393-404(2004).
RN [7]
RP FUNCTION.
RX PubMed=16103222; DOI=10.1083/jcb.200503078;
RA Vieira O.V., Verkade P., Manninen A., Simons K.;
RT "FAPP2 is involved in the transport of apical cargo in polarized MDCK
RT cells.";
RL J. Cell Biol. 170:521-526(2005).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ARG-18 AND TRP-407.
RX PubMed=17687330; DOI=10.1038/nature06097;
RA D'Angelo G., Polishchuk E., Di Tullio G., Santoro M., Di Campli A.,
RA Godi A., West G., Bielawski J., Chuang C.C., van der Spoel A.C.,
RA Platt F.M., Hannun Y.A., Polishchuk R., Mattjus P., De Matteis M.A.;
RT "Glycosphingolipid synthesis requires FAPP2 transfer of glucosylceramide.";
RL Nature 449:62-67(2007).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-368.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Cargo transport protein that is required for apical transport
CC from the Golgi complex. Transports AQP2 from the trans-Golgi network
CC (TGN) to sites of AQP2 phosphorylation. Mediates the non-vesicular
CC transport of glucosylceramide (GlcCer) from the trans-Golgi network
CC (TGN) to the plasma membrane and plays a pivotal role in the synthesis
CC of complex glycosphingolipids. Binding of both phosphatidylinositol 4-
CC phosphate (PIP) and ARF1 are essential for the GlcCer transfer ability.
CC Also required for primary cilium formation, possibly by being involved
CC in the transport of raft lipids to the apical membrane, and for
CC membrane tubulation. {ECO:0000269|PubMed:15107860,
CC ECO:0000269|PubMed:16103222, ECO:0000269|PubMed:17687330}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with ARF1; the
CC interaction together with phosphatidylinositol 4-phosphate binding is
CC required for FAPP2 GlcCer transfer ability. {ECO:0000250,
CC ECO:0000269|PubMed:15107860}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:15107860}. Membrane; Peripheral membrane protein
CC {ECO:0000269|PubMed:15107860}. Note=Binds through its PH domain to
CC PtdIns(4)P and ARF1, and subsequently localizes to TGN exit sites.
CC {ECO:0000269|PubMed:15107860}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96JA3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JA3-2; Sequence=VSP_028545, VSP_028546;
CC Name=3;
CC IsoId=Q96JA3-3; Sequence=VSP_028543, VSP_028544;
CC -!- TISSUE SPECIFICITY: Expressed in kidney cell lines.
CC {ECO:0000269|PubMed:15107860}.
CC -!- DOMAIN: The PH domain of FAPPS binds the small GTPase ARF1 and
CC phosphatidylinositol-4-phosphate (PtdIns4P) with high selectivity, and
CC is required for recruitment of FAPPs to the trans-Golgi network (TGN).
CC {ECO:0000269|PubMed:15107860}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG48267.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK55424.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF380162; AAK55424.1; ALT_SEQ; mRNA.
DR EMBL; AK023180; BAB14449.1; -; mRNA.
DR EMBL; AK294857; BAG57961.1; -; mRNA.
DR EMBL; CH471073; EAW93930.1; -; Genomic_DNA.
DR EMBL; BC002838; AAH02838.1; -; mRNA.
DR EMBL; BC053990; AAH53990.1; -; mRNA.
DR EMBL; AF308300; AAG48267.1; ALT_INIT; mRNA.
DR CCDS; CCDS5424.1; -. [Q96JA3-3]
DR CCDS; CCDS56473.1; -. [Q96JA3-1]
DR CCDS; CCDS87489.1; -. [Q96JA3-2]
DR RefSeq; NP_001183955.1; NM_001197026.1. [Q96JA3-1]
DR RefSeq; NP_001183956.1; NM_001197027.1.
DR RefSeq; NP_116028.1; NM_032639.3. [Q96JA3-3]
DR RefSeq; XP_011513896.1; XM_011515594.1.
DR PDB; 5KDI; X-ray; 1.45 A; A/B=309-519.
DR PDBsum; 5KDI; -.
DR AlphaFoldDB; Q96JA3; -.
DR SMR; Q96JA3; -.
DR BioGRID; 124225; 15.
DR IntAct; Q96JA3; 6.
DR STRING; 9606.ENSP00000397947; -.
DR iPTMnet; Q96JA3; -.
DR PhosphoSitePlus; Q96JA3; -.
DR BioMuta; PLEKHA8; -.
DR DMDM; 387912902; -.
DR EPD; Q96JA3; -.
DR jPOST; Q96JA3; -.
DR MassIVE; Q96JA3; -.
DR MaxQB; Q96JA3; -.
DR PaxDb; Q96JA3; -.
DR PeptideAtlas; Q96JA3; -.
DR PRIDE; Q96JA3; -.
DR ProteomicsDB; 76918; -. [Q96JA3-1]
DR ProteomicsDB; 76919; -. [Q96JA3-2]
DR ProteomicsDB; 76920; -. [Q96JA3-3]
DR Antibodypedia; 26151; 176 antibodies from 29 providers.
DR DNASU; 84725; -.
DR Ensembl; ENST00000258679.11; ENSP00000258679.7; ENSG00000106086.20. [Q96JA3-3]
DR Ensembl; ENST00000396257.6; ENSP00000379556.2; ENSG00000106086.20. [Q96JA3-2]
DR Ensembl; ENST00000440706.3; ENSP00000407802.2; ENSG00000106086.20. [Q96JA3-1]
DR Ensembl; ENST00000449726.6; ENSP00000397947.1; ENSG00000106086.20. [Q96JA3-1]
DR GeneID; 84725; -.
DR KEGG; hsa:84725; -.
DR MANE-Select; ENST00000449726.6; ENSP00000397947.1; NM_001197026.2; NP_001183955.1.
DR UCSC; uc003tan.4; human. [Q96JA3-1]
DR CTD; 84725; -.
DR DisGeNET; 84725; -.
DR GeneCards; PLEKHA8; -.
DR HGNC; HGNC:30037; PLEKHA8.
DR HPA; ENSG00000106086; Low tissue specificity.
DR MIM; 608639; gene.
DR neXtProt; NX_Q96JA3; -.
DR OpenTargets; ENSG00000106086; -.
DR PharmGKB; PA134926954; -.
DR VEuPathDB; HostDB:ENSG00000106086; -.
DR eggNOG; KOG3221; Eukaryota.
DR GeneTree; ENSGT00940000157288; -.
DR HOGENOM; CLU_039839_0_0_1; -.
DR InParanoid; Q96JA3; -.
DR OMA; SKMKHPV; -.
DR OrthoDB; 952122at2759; -.
DR TreeFam; TF317467; -.
DR PathwayCommons; Q96JA3; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR SignaLink; Q96JA3; -.
DR BioGRID-ORCS; 84725; 18 hits in 1044 CRISPR screens.
DR ChiTaRS; PLEKHA8; human.
DR GenomeRNAi; 84725; -.
DR Pharos; Q96JA3; Tbio.
DR PRO; PR:Q96JA3; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96JA3; protein.
DR Bgee; ENSG00000106086; Expressed in ventricular zone and 164 other tissues.
DR ExpressionAtlas; Q96JA3; baseline and differential.
DR Genevisible; Q96JA3; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:1902387; F:ceramide 1-phosphate binding; IBA:GO_Central.
DR GO; GO:1902388; F:ceramide 1-phosphate transfer activity; IBA:GO_Central.
DR GO; GO:0097001; F:ceramide binding; IDA:UniProtKB.
DR GO; GO:0051861; F:glycolipid binding; IDA:UniProtKB.
DR GO; GO:0017089; F:glycolipid transfer activity; IDA:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:UniProtKB.
DR GO; GO:0035627; P:ceramide transport; IBA:GO_Central.
DR GO; GO:0035621; P:ER to Golgi ceramide transport; IDA:UniProtKB.
DR GO; GO:0120009; P:intermembrane lipid transfer; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3520.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR036497; GLTP_sf.
DR InterPro; IPR014830; Glycolipid_transfer_prot_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF08718; GLTP; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF110004; SSF110004; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Golgi apparatus; Lipid transport;
KW Lipid-binding; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..519
FT /note="Pleckstrin homology domain-containing family A
FT member 8"
FT /id="PRO_0000306865"
FT DOMAIN 1..93
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 310..519
FT /note="Glycolipid transfer protein homology domain"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZY60"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZY60"
FT MOD_RES 153
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:D3ZY60"
FT VAR_SEQ 434..439
FT /note="NNAYGK -> RNPTEN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028543"
FT VAR_SEQ 441..519
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028544"
FT VAR_SEQ 455
FT /note="L -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028545"
FT VAR_SEQ 456..519
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028546"
FT VARIANT 368
FT /note="V -> E (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035444"
FT MUTAGEN 18
FT /note="R->L: Abolishes binding to phosphatylinositol 4-
FT phosphate, less association with Golgi and no preference
FT for TGN location."
FT /evidence="ECO:0000269|PubMed:17687330"
FT MUTAGEN 407
FT /note="W->A: Loss of glucosylceramide transfer activity
FT from the TGN to the plasma membrane."
FT /evidence="ECO:0000269|PubMed:17687330"
FT CONFLICT 232
FT /note="E -> G (in Ref. 4; BAB14449)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="T -> S (in Ref. 1; AAK55424)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="Y -> C (in Ref. 1; AAK55424)"
FT /evidence="ECO:0000305"
FT CONFLICT 359..365
FT /note="MDLVGNI -> DGSCWKY (in Ref. 5; AAG48267)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="G -> E (in Ref. 1; AAK55424)"
FT /evidence="ECO:0000305"
FT CONFLICT 370..372
FT /note="QKY -> RSI (in Ref. 4; BAB14449)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="A -> T (in Ref. 1; AAK55424)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="Q -> R (in Ref. 1; AAK55424)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="E -> K (in Ref. 1; AAK55424)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="L -> M (in Ref. 1; AAK55424)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="T -> A (in Ref. 1; AAK55424)"
FT /evidence="ECO:0000305"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:5KDI"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 332..340
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 343..349
FT /evidence="ECO:0007829|PDB:5KDI"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 355..372
FT /evidence="ECO:0007829|PDB:5KDI"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 382..391
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 401..423
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 429..439
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 447..458
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 463..468
FT /evidence="ECO:0007829|PDB:5KDI"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:5KDI"
FT HELIX 480..510
FT /evidence="ECO:0007829|PDB:5KDI"
SQ SEQUENCE 519 AA; 58261 MW; 3E2D0746C00C722B CRC64;
MEGVLYKWTN YLSGWQPRWF LLCGGILSYY DSPEDAWKGC KGSIQMAVCE IQVHSVDNTR
MDLIIPGEQY FYLKARSVAE RQRWLVALGS AKACLTDSRT QKEKEFAENT ENLKTKMSEL
RLYCDLLVQQ VDKTKEVTTT GVSNSEEGID VGTLLKSTCN TFLKTLEECM QIANAAFTSE
LLYRTPPGSP QLAMLKSSKM KHPIIPIHNS LERQMELSTC ENGSLNMEIN GEEEILMKNK
NSLYLKSAEI DCSISSEENT DDNITVQGEI RKEDGMENLK NHDNNLTQSG SDSSCSPECL
WEEGKEVIPT FFSTMNTSFS DIELLEDSGI PTEAFLASCY AVVPVLDKLG PTVFAPVKMD
LVGNIKKVNQ KYITNKEEFT TLQKIVLHEV EADVAQVRNS ATEALLWLKR GLKFLKGFLT
EVKNGEKDIQ TALNNAYGKT LRQHHGWVVR GVFALALRAA PSYEDFVAAL TVKEGDHQKE
AFSIGMQRDL SLYLPAMEKQ LAILDTLYEV HGLESDEVV
