ICEF1_HUMAN
ID ICEF1_HUMAN Reviewed; 437 AA.
AC Q8WWN9; A8K1K2; B7ZL78; B7ZL80; G3V132; O43153; Q5HYL8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Interactor protein for cytohesin exchange factors 1;
DE AltName: Full=Phosphoinositide-binding protein PIP3-E;
GN Name=IPCEF1; Synonyms=KIAA0403;
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 IPCEF1-1), AND INTERACTION WITH
RP PHOSPHATIDYLINOSITOL 3-PHOSPHATE.
RX PubMed=11804589; DOI=10.1016/s1097-2765(02)00434-3;
RA Krugmann S., Anderson K.E., Ridley S.H., Risso N., McGregor A.,
RA Coadwell J., Davidson K., Eguinoa A., Ellson C.D., Lipp P., Manifava M.,
RA Ktistakis N., Painter G., Thuring J.W., Cooper M.A., Lim Z.-Y.,
RA Holmes A.B., Dove S.K., Michell R.H., Grewal A., Nazarian A.,
RA Erdjument-Bromage H., Tempst P., Stephens L.R., Hawkins P.T.;
RT "Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho
RT GTPases, by selective capture on phosphoinositide affinity matrices.";
RL Mol. Cell 9:95-108(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IPCEF1-2).
RC TISSUE=Corpus callosum;
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] (ISOFORM IPCEF1-2).
RC TISSUE=Endometrium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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] (ISOFORMS IPCEF1-1 AND IPCEF1-2).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-437.
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [8]
RP ALTERNATIVE SPLICING, AND INTERACTION WITH CYTH2.
RX PubMed=22085542; DOI=10.1016/j.yexcr.2011.10.018;
RA Attar M.A., Salem J.C., Pursel H.S., Santy L.C.;
RT "CNK3 and IPCEF1 produce a single protein that is required for HGF
RT dependent Arf6 activation and migration.";
RL Exp. Cell Res. 318:228-237(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND IDENTIFICATION BY
RP 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).
RN [10] {ECO:0007744|PDB:5MR1}
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 42-142.
RA Newman J.A., Aitkenhead H., Wang D., Burgess-Brown N., Williams E.,
RA von-Delft F., Arrowsmith C.H., Edwards A., Bountra C., Gileadi O.;
RT "Crystal structure of the pleckstrin homology domain of interactor protein
RT for cytohesin exchange factors 1 (IPCEF1).";
RL Submitted (DEC-2016) to the PDB data bank.
CC -!- FUNCTION: Enhances the promotion of guanine-nucleotide exchange by
CC PSCD2 on ARF6 in a concentration-dependent manner. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with guanine-nucleotide exchange factors PSCD1,
CC PSCD2, PSCD3 and PSCD4 (By similarity). Interacts (via C-terminus) with
CC cytohesin-2 CYTH2 (PubMed:22085542). {ECO:0000250,
CC ECO:0000269|PubMed:22085542}.
CC -!- INTERACTION:
CC Q8WWN9; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-4401965, EBI-739624;
CC Q8WWN9; Q15438: CYTH1; NbExp=6; IntAct=EBI-4401965, EBI-997830;
CC Q8WWN9; Q99418: CYTH2; NbExp=6; IntAct=EBI-4401965, EBI-448974;
CC Q8WWN9; O43739-2: CYTH3; NbExp=3; IntAct=EBI-4401965, EBI-11974015;
CC Q8WWN9; Q9UIA0: CYTH4; NbExp=6; IntAct=EBI-4401965, EBI-11521003;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Translocated with PSCD2 to the plasma membrane upon
CC epidermal growth factor (EGF) stimulation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=IPCEF1-1;
CC IsoId=Q8WWN9-1; Sequence=Displayed;
CC Name=IPCEF1-2;
CC IsoId=Q8WWN9-2; Sequence=VSP_032682;
CC Name=CNK3-IPCEF1-1; Synonyms=CNK3/IPCEF1 Long-1;
CC IsoId=G9CGD6-1; Sequence=External;
CC Name=CNK3-IPCEF1-2; Synonyms=CNK3/IPCEF1 Long-2;
CC IsoId=G9CGD6-2; Sequence=External;
CC Name=CNK3-IPCEF1-3; Synonyms=CNK3/IPCEF1 Short;
CC IsoId=G9CGD6-3; Sequence=External;
CC -!- CAUTION: It is uncertain whether Met-1 or Met-29 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AJ310566; CAC83949.1; -; mRNA.
DR EMBL; AK289917; BAF82606.1; -; mRNA.
DR EMBL; BX647254; CAI46054.1; -; mRNA.
DR EMBL; AL445220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL033376; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL132774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF510943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47701.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47702.1; -; Genomic_DNA.
DR EMBL; BC105015; AAI05016.1; -; mRNA.
DR EMBL; BC105043; AAI05044.1; -; mRNA.
DR EMBL; BC143623; AAI43624.1; -; mRNA.
DR EMBL; BC143629; AAI43630.1; -; mRNA.
DR EMBL; AB007863; BAA23699.1; -; mRNA.
DR CCDS; CCDS47509.1; -. [Q8WWN9-2]
DR CCDS; CCDS5245.1; -. [Q8WWN9-1]
DR RefSeq; NP_001124171.1; NM_001130699.1. [Q8WWN9-2]
DR RefSeq; NP_001124172.1; NM_001130700.1. [Q8WWN9-2]
DR RefSeq; NP_056368.1; NM_015553.2. [Q8WWN9-1]
DR RefSeq; XP_005266976.1; XM_005266919.4.
DR RefSeq; XP_005266978.1; XM_005266921.4.
DR RefSeq; XP_005266980.1; XM_005266923.3.
DR RefSeq; XP_011534044.1; XM_011535742.2.
DR RefSeq; XP_016866206.1; XM_017010717.1.
DR RefSeq; XP_016866207.1; XM_017010718.1.
DR PDB; 5MR1; X-ray; 1.20 A; A=42-142.
DR PDBsum; 5MR1; -.
DR AlphaFoldDB; Q8WWN9; -.
DR SMR; Q8WWN9; -.
DR BioGRID; 117500; 11.
DR IntAct; Q8WWN9; 8.
DR iPTMnet; Q8WWN9; -.
DR PhosphoSitePlus; Q8WWN9; -.
DR BioMuta; IPCEF1; -.
DR DMDM; 74751582; -.
DR jPOST; Q8WWN9; -.
DR MassIVE; Q8WWN9; -.
DR PaxDb; Q8WWN9; -.
DR PeptideAtlas; Q8WWN9; -.
DR PRIDE; Q8WWN9; -.
DR ProteomicsDB; 32242; -.
DR ProteomicsDB; 74916; -. [Q8WWN9-1]
DR ProteomicsDB; 74917; -. [Q8WWN9-2]
DR Antibodypedia; 33399; 132 antibodies from 18 providers.
DR DNASU; 26034; -.
DR Ensembl; ENST00000265198.8; ENSP00000265198.4; ENSG00000074706.14. [Q8WWN9-1]
DR Ensembl; ENST00000367220.9; ENSP00000356189.4; ENSG00000074706.14. [Q8WWN9-2]
DR Ensembl; ENST00000422970.6; ENSP00000394751.2; ENSG00000074706.14. [Q8WWN9-2]
DR GeneID; 26034; -.
DR KEGG; hsa:26034; -.
DR MANE-Select; ENST00000367220.9; ENSP00000356189.4; NM_001130700.2; NP_001124172.1. [Q8WWN9-2]
DR UCSC; uc003qpw.4; human. [Q8WWN9-1]
DR UCSC; uc063skh.1; human.
DR CTD; 26034; -.
DR DisGeNET; 26034; -.
DR GeneCards; IPCEF1; -.
DR HGNC; HGNC:21204; IPCEF1.
DR HPA; ENSG00000074706; Group enriched (bone marrow, brain, lymphoid tissue, thyroid gland).
DR neXtProt; NX_Q8WWN9; -.
DR OpenTargets; ENSG00000074706; -.
DR PharmGKB; PA164721033; -.
DR VEuPathDB; HostDB:ENSG00000074706; -.
DR eggNOG; KOG1738; Eukaryota.
DR GeneTree; ENSGT00940000154428; -.
DR InParanoid; Q8WWN9; -.
DR OMA; ADTHCLA; -.
DR OrthoDB; 1121556at2759; -.
DR PhylomeDB; Q8WWN9; -.
DR TreeFam; TF326495; -.
DR PathwayCommons; Q8WWN9; -.
DR SignaLink; Q8WWN9; -.
DR BioGRID-ORCS; 26034; 15 hits in 1059 CRISPR screens.
DR ChiTaRS; IPCEF1; human.
DR GenomeRNAi; 26034; -.
DR Pharos; Q8WWN9; Tbio.
DR PRO; PR:Q8WWN9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8WWN9; protein.
DR Bgee; ENSG00000074706; Expressed in endothelial cell and 149 other tissues.
DR ExpressionAtlas; Q8WWN9; baseline and differential.
DR Genevisible; Q8WWN9; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005344; F:oxygen carrier activity; NAS:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; ISS:UniProtKB.
DR GO; GO:0015671; P:oxygen transport; NAS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..437
FT /note="Interactor protein for cytohesin exchange factors 1"
FT /id="PRO_0000326630"
FT DOMAIN 41..140
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 143..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..320
FT /note="CRAC domain"
FT REGION 339..348
FT /note="CRAC domain"
FT REGION 389..437
FT /note="Required for interaction with CYTH2"
FT /evidence="ECO:0000269|PubMed:22085542"
FT REGION 406..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 12
FT /note="L -> LQ (in isoform IPCEF1-2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_032682"
FT VARIANT 194
FT /note="S -> P (in dbSNP:rs1060390)"
FT /id="VAR_042410"
FT CONFLICT 267
FT /note="S -> G (in Ref. 3; CAI46054)"
FT /evidence="ECO:0000305"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:5MR1"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:5MR1"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:5MR1"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5MR1"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:5MR1"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:5MR1"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:5MR1"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:5MR1"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:5MR1"
SQ SEQUENCE 437 AA; 48993 MW; 60BC1790FBBD377C CRC64;
MTSYMAIDGS ALVPLRQKPR RKTQGFLTMS RRRISCKDLG HADCQGWLYK KKEKGSFLSN
KWKKFWVILK GSSLYWYSNQ MAEKADGFVN LPDFTVERAS ECKKKHAFKI SHPQIKTFYF
AAENVQEMNV WLNKLGSAVI HQESTTKDEE CYSESEQEDP EIAAETPPPP HASQTQSLTA
QQASSSSPSL SGTSYSFSSL ENTVKTPSSF PSSLSKERQS LPDTVNSLSA AEDEGQPITF
AVQVHSPVPS EAGIHKALEN SFVTSESGFL NSLSSDDTSS LSSNHDHLTV PDKPAGSKIM
DKEETKVSED DEMEKLYKSL EQASLSPLGD RRPSTKKELR KSFVKRCKNP SINEKLHKIR
TLNSTLKCKE HDLAMINQLL DDPKLTARKY REWKVMNTLL IQDIYQQQRA SPAPDDTDDT
PQELKKSPSS PSVENSI
