Full text data of EPS15L1
EPS15L1
(EPS15R)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein; Eps15R)
Epidermal growth factor receptor substrate 15-like 1 (Eps15-related protein; Eps15R)
UniProt
Q9UBC2
ID EP15R_HUMAN Reviewed; 864 AA.
AC Q9UBC2; A2RRF3; A5PL29; B4DKA3;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=Epidermal growth factor receptor substrate 15-like 1;
DE AltName: Full=Eps15-related protein;
DE Short=Eps15R;
GN Name=EPS15L1; Synonyms=EPS15R;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Nakashima S., Morinaka K., Ikeda M., Kishida S., Koyama S.,
RA Kikuchi A.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Thalamus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=9407958;
RA Carbone R., Fre S., Iannolo G., Belleudi F., Mancini P., Pelicci P.G.,
RA Torrisi M.R., Di Fiore P.P.;
RT "eps15 and eps15R are essential components of the endocytic pathway.";
RL Cancer Res. 57:5498-5504(1997).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS
RP SPECTROMETRY.
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-255; SER-560;
RP THR-577 AND THR-797, AND MASS SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP INTERACTION WITH FCHO2.
RX PubMed=20448150; DOI=10.1126/science.1188462;
RA Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y.,
RA Mittal R., McMahon H.T.;
RT "FCHo proteins are nucleators of clathrin-mediated endocytosis.";
RL Science 328:1281-1284(2010).
RN [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP FUNCTION, AND INTERACTION WITH DAB2.
RX PubMed=22648170; DOI=10.1091/mbc.E11-12-1007;
RA Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.;
RT "The clathrin adaptor Dab2 recruits EH domain scaffold proteins to
RT regulate integrin beta1 endocytosis.";
RL Mol. Biol. Cell 23:2905-2916(2012).
RN [18]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
CC -!- FUNCTION: Seems to be a constitutive component of clathrin-coated
CC pits that is required for receptor-mediated endocytosis. Involved
CC in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor
CC (TFR); internalization of ITGB1 as DAB2-dependent cargo but not
CC TFR seems to require association with DAB2.
CC -!- SUBUNIT: Interacts with EPS15, AGFG1/HRB and AGFG2/HRBL.
CC Associates with the clathrin-associated adapter protein complex 2
CC (AP-2) (By similarity). Interacts with FCHO1. Interacts with
CC FCHO2. Interacts (via EH domains) with DAB2.
CC -!- INTERACTION:
CC Q969G5:PRKCDBP; NbExp=2; IntAct=EBI-2556746, EBI-3893101;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC (By similarity). Nucleus (By similarity). Membrane, coated pit (By
CC similarity). Note=Localized to plasma membrane coated pits (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UBC2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBC2-2; Sequence=VSP_042200;
CC Name=3;
CC IsoId=Q9UBC2-3; Sequence=VSP_045429;
CC Name=4;
CC IsoId=Q9UBC2-4; Sequence=VSP_046904, VSP_046905;
CC Note=No experimental confirmation available;
CC -!- PTM: Phosphorylated on tyrosine residues by EGFR (By similarity).
CC -!- SIMILARITY: Contains 1 EF-hand domain.
CC -!- SIMILARITY: Contains 3 EH domains.
CC -!- CAUTION: Studies in clathrin-mediated endocytosis used a siRNA
CC mixture of EPS15 and EPS15L1 (PubMed:22648170).
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DR EMBL; AF110265; AAF21930.1; -; mRNA.
DR EMBL; AB015346; BAA88118.1; -; mRNA.
DR EMBL; AK024166; BAG51266.1; -; mRNA.
DR EMBL; AK296473; BAG59115.1; -; mRNA.
DR EMBL; AC008764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84542.1; -; Genomic_DNA.
DR EMBL; BC131590; AAI31591.1; -; mRNA.
DR EMBL; BC142716; AAI42717.1; -; mRNA.
DR RefSeq; NP_001245303.1; NM_001258374.1.
DR RefSeq; NP_001245304.1; NM_001258375.1.
DR RefSeq; NP_001245305.1; NM_001258376.1.
DR RefSeq; NP_067058.1; NM_021235.2.
DR UniGene; Hs.654639; -.
DR UniGene; Hs.744842; -.
DR ProteinModelPortal; Q9UBC2; -.
DR SMR; Q9UBC2; 11-105, 121-214, 269-362.
DR IntAct; Q9UBC2; 10.
DR MINT; MINT-1538779; -.
DR STRING; 9606.ENSP00000248070; -.
DR DMDM; 61223942; -.
DR PaxDb; Q9UBC2; -.
DR PRIDE; Q9UBC2; -.
DR Ensembl; ENST00000248070; ENSP00000248070; ENSG00000127527.
DR Ensembl; ENST00000455140; ENSP00000393313; ENSG00000127527.
DR Ensembl; ENST00000535753; ENSP00000440103; ENSG00000127527.
DR Ensembl; ENST00000597937; ENSP00000472267; ENSG00000127527.
DR Ensembl; ENST00000602022; ENSP00000471981; ENSG00000127527.
DR GeneID; 58513; -.
DR KEGG; hsa:58513; -.
DR UCSC; uc002nec.2; human.
DR CTD; 58513; -.
DR GeneCards; GC19M016466; -.
DR HGNC; HGNC:24634; EPS15L1.
DR HPA; HPA019237; -.
DR neXtProt; NX_Q9UBC2; -.
DR PharmGKB; PA134906266; -.
DR eggNOG; NOG301764; -.
DR HOGENOM; HOG000004804; -.
DR HOVERGEN; HBG005591; -.
DR InParanoid; Q9UBC2; -.
DR OMA; MDDPFKN; -.
DR OrthoDB; EOG7JHM68; -.
DR PhylomeDB; Q9UBC2; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; EPS15L1; human.
DR GeneWiki; EPS15L1; -.
DR GenomeRNAi; 58513; -.
DR NextBio; 65055; -.
DR PRO; PR:Q9UBC2; -.
DR ArrayExpress; Q9UBC2; -.
DR Bgee; Q9UBC2; -.
DR CleanEx; HS_EPS15L1; -.
DR Genevestigator; Q9UBC2; -.
DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR Gene3D; 1.10.238.10; -; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EPS15_homology.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00027; EH; 3.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS50031; EH; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Cell membrane; Coated pit;
KW Coiled coil; Complete proteome; Endocytosis; Membrane; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 864 Epidermal growth factor receptor
FT substrate 15-like 1.
FT /FTId=PRO_0000146118.
FT DOMAIN 15 104 EH 1.
FT DOMAIN 127 215 EH 2.
FT DOMAIN 159 194 EF-hand.
FT DOMAIN 275 365 EH 3.
FT REPEAT 618 620 1.
FT REPEAT 640 642 2.
FT REPEAT 645 647 3.
FT REPEAT 650 652 4.
FT REPEAT 656 658 5.
FT REPEAT 661 663 6.
FT REPEAT 667 669 7.
FT REPEAT 685 687 8.
FT REPEAT 690 692 9.
FT REPEAT 709 711 10.
FT REPEAT 728 730 11.
FT REPEAT 754 756 12.
FT REPEAT 806 808 13.
FT REPEAT 812 814 14.
FT REPEAT 833 835 15.
FT CA_BIND 172 184 Potential.
FT REGION 15 368 Interaction with DAB2 (By similarity).
FT REGION 618 835 15 X 3 AA repeats of D-P-F.
FT COMPBIAS 750 816 Pro-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 74 74 Phosphotyrosine (By similarity).
FT MOD_RES 108 108 Phosphoserine (By similarity).
FT MOD_RES 229 229 Phosphoserine.
FT MOD_RES 244 244 Phosphoserine.
FT MOD_RES 255 255 Phosphoserine.
FT MOD_RES 560 560 Phosphoserine.
FT MOD_RES 564 564 Phosphotyrosine (By similarity).
FT MOD_RES 577 577 Phosphothreonine.
FT MOD_RES 797 797 Phosphothreonine.
FT VAR_SEQ 598 601 DDPF -> VKVE (in isoform 4).
FT /FTId=VSP_046904.
FT VAR_SEQ 602 864 Missing (in isoform 4).
FT /FTId=VSP_046905.
FT VAR_SEQ 750 864 PPPSGPFTSSLGGAGFSDDPFKSKQDTPALPPKKPAPPRPK
FT PPSGKSTPVSQLGSADFPEAPDPFQPLGADSGDPFQSKKGF
FT GDPFSGKDPFVPSSAAKPSKASASGFADFTSVS -> VKVH
FT L (in isoform 3).
FT /FTId=VSP_045429.
FT VAR_SEQ 863 864 VS -> FGNEEQQLAWAKRESEKAEQERLARLRRQEQEDLE
FT LAIALSKADMPAA (in isoform 2).
FT /FTId=VSP_042200.
FT CONFLICT 680 680 K -> E (in Ref. 3; BAG59115).
SQ SEQUENCE 864 AA; 94255 MW; F4126069F6E00387 CRC64;
MAAPLIPLSQ QIPTGNSLYE SYYKQVDPAY TGRVGASEAA LFLKKSGLSD IILGKIWDLA
DPEGKGFLDK QGFYVALRLV ACAQSGHEVT LSNLNLSMPP PKFHDTSSPL MVTPPSAEAH
WAVRVEEKAK FDGIFESLLP INGLLSGDKV KPVLMNSKLP LDVLGRVWDL SDIDKDGHLD
RDEFAVAMHL VYRALEKEPV PSALPPSLIP PSKRKKTVFP GAVPVLPASP PPKDSLRSTP
SHGSVSSLNS TGSLSPKHSL KQTQPTVNWV VPVADKMRFD EIFLKTDLDL DGYVSGQEVK
EIFMHSGLTQ NLLAHIWALA DTRQTGKLSK DQFALAMYFI QQKVSKGIDP PQVLSPDMVP
PSERGTPGPD SSGSLGSGEF TGVKELDDIS QEIAQLQREK YSLEQDIREK EEAIRQKTSE
VQELQNDLDR ETSSLQELEA QKQDAQDRLD EMDQQKAKLR DMLSDVRQKC QDETQMISSL
KTQIQSQESD LKSQEDDLNR AKSELNRLQQ EETQLEQSIQ AGRVQLETII KSLKSTQDEI
NQARSKLSQL HESRQEAHRS LEQYDQVLDG AHGASLTDLA NLSEGVSLAE RGSFGAMDDP
FKNKALLFSN NTQELHPDPF QTEDPFKSDP FKGADPFKGD PFQNDPFAEQ QTTSTDPFGG
DPFKESDPFR GSATDDFFKK QTKNDPFTSD PFTKNPSLPS KLDPFESSDP FSSSSVSSKG
SDPFGTLDPF GSGSFNSAEG FADFSQMSKP PPSGPFTSSL GGAGFSDDPF KSKQDTPALP
PKKPAPPRPK PPSGKSTPVS QLGSADFPEA PDPFQPLGAD SGDPFQSKKG FGDPFSGKDP
FVPSSAAKPS KASASGFADF TSVS
//
ID EP15R_HUMAN Reviewed; 864 AA.
AC Q9UBC2; A2RRF3; A5PL29; B4DKA3;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 121.
DE RecName: Full=Epidermal growth factor receptor substrate 15-like 1;
DE AltName: Full=Eps15-related protein;
DE Short=Eps15R;
GN Name=EPS15L1; Synonyms=EPS15R;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Nakashima S., Morinaka K., Ikeda M., Kishida S., Koyama S.,
RA Kikuchi A.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND SUBCELLULAR LOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Thalamus;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=9407958;
RA Carbone R., Fre S., Iannolo G., Belleudi F., Mancini P., Pelicci P.G.,
RA Torrisi M.R., Di Fiore P.P.;
RT "eps15 and eps15R are essential components of the endocytic pathway.";
RL Cancer Res. 57:5498-5504(1997).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS
RP SPECTROMETRY.
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244; SER-255; SER-560;
RP THR-577 AND THR-797, AND MASS SPECTROMETRY.
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP INTERACTION WITH FCHO2.
RX PubMed=20448150; DOI=10.1126/science.1188462;
RA Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y.,
RA Mittal R., McMahon H.T.;
RT "FCHo proteins are nucleators of clathrin-mediated endocytosis.";
RL Science 328:1281-1284(2010).
RN [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP FUNCTION, AND INTERACTION WITH DAB2.
RX PubMed=22648170; DOI=10.1091/mbc.E11-12-1007;
RA Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.;
RT "The clathrin adaptor Dab2 recruits EH domain scaffold proteins to
RT regulate integrin beta1 endocytosis.";
RL Mol. Biol. Cell 23:2905-2916(2012).
RN [18]
RP INTERACTION WITH FCHO1.
RX PubMed=22484487; DOI=10.1038/ncb2473;
RA Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B.,
RA Tsang M., Traub L.M.;
RT "Distinct and separable activities of the endocytic clathrin-coat
RT components Fcho1/2 and AP-2 in developmental patterning.";
RL Nat. Cell Biol. 14:488-501(2012).
CC -!- FUNCTION: Seems to be a constitutive component of clathrin-coated
CC pits that is required for receptor-mediated endocytosis. Involved
CC in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor
CC (TFR); internalization of ITGB1 as DAB2-dependent cargo but not
CC TFR seems to require association with DAB2.
CC -!- SUBUNIT: Interacts with EPS15, AGFG1/HRB and AGFG2/HRBL.
CC Associates with the clathrin-associated adapter protein complex 2
CC (AP-2) (By similarity). Interacts with FCHO1. Interacts with
CC FCHO2. Interacts (via EH domains) with DAB2.
CC -!- INTERACTION:
CC Q969G5:PRKCDBP; NbExp=2; IntAct=EBI-2556746, EBI-3893101;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC (By similarity). Nucleus (By similarity). Membrane, coated pit (By
CC similarity). Note=Localized to plasma membrane coated pits (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UBC2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBC2-2; Sequence=VSP_042200;
CC Name=3;
CC IsoId=Q9UBC2-3; Sequence=VSP_045429;
CC Name=4;
CC IsoId=Q9UBC2-4; Sequence=VSP_046904, VSP_046905;
CC Note=No experimental confirmation available;
CC -!- PTM: Phosphorylated on tyrosine residues by EGFR (By similarity).
CC -!- SIMILARITY: Contains 1 EF-hand domain.
CC -!- SIMILARITY: Contains 3 EH domains.
CC -!- CAUTION: Studies in clathrin-mediated endocytosis used a siRNA
CC mixture of EPS15 and EPS15L1 (PubMed:22648170).
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DR EMBL; AF110265; AAF21930.1; -; mRNA.
DR EMBL; AB015346; BAA88118.1; -; mRNA.
DR EMBL; AK024166; BAG51266.1; -; mRNA.
DR EMBL; AK296473; BAG59115.1; -; mRNA.
DR EMBL; AC008764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84542.1; -; Genomic_DNA.
DR EMBL; BC131590; AAI31591.1; -; mRNA.
DR EMBL; BC142716; AAI42717.1; -; mRNA.
DR RefSeq; NP_001245303.1; NM_001258374.1.
DR RefSeq; NP_001245304.1; NM_001258375.1.
DR RefSeq; NP_001245305.1; NM_001258376.1.
DR RefSeq; NP_067058.1; NM_021235.2.
DR UniGene; Hs.654639; -.
DR UniGene; Hs.744842; -.
DR ProteinModelPortal; Q9UBC2; -.
DR SMR; Q9UBC2; 11-105, 121-214, 269-362.
DR IntAct; Q9UBC2; 10.
DR MINT; MINT-1538779; -.
DR STRING; 9606.ENSP00000248070; -.
DR DMDM; 61223942; -.
DR PaxDb; Q9UBC2; -.
DR PRIDE; Q9UBC2; -.
DR Ensembl; ENST00000248070; ENSP00000248070; ENSG00000127527.
DR Ensembl; ENST00000455140; ENSP00000393313; ENSG00000127527.
DR Ensembl; ENST00000535753; ENSP00000440103; ENSG00000127527.
DR Ensembl; ENST00000597937; ENSP00000472267; ENSG00000127527.
DR Ensembl; ENST00000602022; ENSP00000471981; ENSG00000127527.
DR GeneID; 58513; -.
DR KEGG; hsa:58513; -.
DR UCSC; uc002nec.2; human.
DR CTD; 58513; -.
DR GeneCards; GC19M016466; -.
DR HGNC; HGNC:24634; EPS15L1.
DR HPA; HPA019237; -.
DR neXtProt; NX_Q9UBC2; -.
DR PharmGKB; PA134906266; -.
DR eggNOG; NOG301764; -.
DR HOGENOM; HOG000004804; -.
DR HOVERGEN; HBG005591; -.
DR InParanoid; Q9UBC2; -.
DR OMA; MDDPFKN; -.
DR OrthoDB; EOG7JHM68; -.
DR PhylomeDB; Q9UBC2; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; EPS15L1; human.
DR GeneWiki; EPS15L1; -.
DR GenomeRNAi; 58513; -.
DR NextBio; 65055; -.
DR PRO; PR:Q9UBC2; -.
DR ArrayExpress; Q9UBC2; -.
DR Bgee; Q9UBC2; -.
DR CleanEx; HS_EPS15L1; -.
DR Genevestigator; Q9UBC2; -.
DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR Gene3D; 1.10.238.10; -; 3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EPS15_homology.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00027; EH; 3.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS50031; EH; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calcium; Cell membrane; Coated pit;
KW Coiled coil; Complete proteome; Endocytosis; Membrane; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 864 Epidermal growth factor receptor
FT substrate 15-like 1.
FT /FTId=PRO_0000146118.
FT DOMAIN 15 104 EH 1.
FT DOMAIN 127 215 EH 2.
FT DOMAIN 159 194 EF-hand.
FT DOMAIN 275 365 EH 3.
FT REPEAT 618 620 1.
FT REPEAT 640 642 2.
FT REPEAT 645 647 3.
FT REPEAT 650 652 4.
FT REPEAT 656 658 5.
FT REPEAT 661 663 6.
FT REPEAT 667 669 7.
FT REPEAT 685 687 8.
FT REPEAT 690 692 9.
FT REPEAT 709 711 10.
FT REPEAT 728 730 11.
FT REPEAT 754 756 12.
FT REPEAT 806 808 13.
FT REPEAT 812 814 14.
FT REPEAT 833 835 15.
FT CA_BIND 172 184 Potential.
FT REGION 15 368 Interaction with DAB2 (By similarity).
FT REGION 618 835 15 X 3 AA repeats of D-P-F.
FT COMPBIAS 750 816 Pro-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 74 74 Phosphotyrosine (By similarity).
FT MOD_RES 108 108 Phosphoserine (By similarity).
FT MOD_RES 229 229 Phosphoserine.
FT MOD_RES 244 244 Phosphoserine.
FT MOD_RES 255 255 Phosphoserine.
FT MOD_RES 560 560 Phosphoserine.
FT MOD_RES 564 564 Phosphotyrosine (By similarity).
FT MOD_RES 577 577 Phosphothreonine.
FT MOD_RES 797 797 Phosphothreonine.
FT VAR_SEQ 598 601 DDPF -> VKVE (in isoform 4).
FT /FTId=VSP_046904.
FT VAR_SEQ 602 864 Missing (in isoform 4).
FT /FTId=VSP_046905.
FT VAR_SEQ 750 864 PPPSGPFTSSLGGAGFSDDPFKSKQDTPALPPKKPAPPRPK
FT PPSGKSTPVSQLGSADFPEAPDPFQPLGADSGDPFQSKKGF
FT GDPFSGKDPFVPSSAAKPSKASASGFADFTSVS -> VKVH
FT L (in isoform 3).
FT /FTId=VSP_045429.
FT VAR_SEQ 863 864 VS -> FGNEEQQLAWAKRESEKAEQERLARLRRQEQEDLE
FT LAIALSKADMPAA (in isoform 2).
FT /FTId=VSP_042200.
FT CONFLICT 680 680 K -> E (in Ref. 3; BAG59115).
SQ SEQUENCE 864 AA; 94255 MW; F4126069F6E00387 CRC64;
MAAPLIPLSQ QIPTGNSLYE SYYKQVDPAY TGRVGASEAA LFLKKSGLSD IILGKIWDLA
DPEGKGFLDK QGFYVALRLV ACAQSGHEVT LSNLNLSMPP PKFHDTSSPL MVTPPSAEAH
WAVRVEEKAK FDGIFESLLP INGLLSGDKV KPVLMNSKLP LDVLGRVWDL SDIDKDGHLD
RDEFAVAMHL VYRALEKEPV PSALPPSLIP PSKRKKTVFP GAVPVLPASP PPKDSLRSTP
SHGSVSSLNS TGSLSPKHSL KQTQPTVNWV VPVADKMRFD EIFLKTDLDL DGYVSGQEVK
EIFMHSGLTQ NLLAHIWALA DTRQTGKLSK DQFALAMYFI QQKVSKGIDP PQVLSPDMVP
PSERGTPGPD SSGSLGSGEF TGVKELDDIS QEIAQLQREK YSLEQDIREK EEAIRQKTSE
VQELQNDLDR ETSSLQELEA QKQDAQDRLD EMDQQKAKLR DMLSDVRQKC QDETQMISSL
KTQIQSQESD LKSQEDDLNR AKSELNRLQQ EETQLEQSIQ AGRVQLETII KSLKSTQDEI
NQARSKLSQL HESRQEAHRS LEQYDQVLDG AHGASLTDLA NLSEGVSLAE RGSFGAMDDP
FKNKALLFSN NTQELHPDPF QTEDPFKSDP FKGADPFKGD PFQNDPFAEQ QTTSTDPFGG
DPFKESDPFR GSATDDFFKK QTKNDPFTSD PFTKNPSLPS KLDPFESSDP FSSSSVSSKG
SDPFGTLDPF GSGSFNSAEG FADFSQMSKP PPSGPFTSSL GGAGFSDDPF KSKQDTPALP
PKKPAPPRPK PPSGKSTPVS QLGSADFPEA PDPFQPLGAD SGDPFQSKKG FGDPFSGKDP
FVPSSAAKPS KASASGFADF TSVS
//