AFTIN_HUMAN
ID AFTIN_HUMAN Reviewed; 936 AA.
AC Q6ULP2; D6W5E9; Q6ZM66; Q86VW3; Q8TCF3; Q9H7E3; Q9HAB9; Q9NXS4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Aftiphilin;
GN Name=AFTPH; Synonyms=AFTH;
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), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH GGA1; GGA3; AP1G1 AND AP1G2.
RC TISSUE=Brain;
RX PubMed=14665628; DOI=10.1074/jbc.m311873200;
RA Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S.;
RT "Definition of the consensus motif recognized by gamma-adaptin ear
RT domains.";
RL J. Biol. Chem. 279:8018-8028(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 347-936 (ISOFORM 5).
RC TISSUE=Colon, and Embryo;
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 3).
RC TISSUE=Amygdala;
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 724-936 (ISOFORM 4).
RC TISSUE=Brain, and Lung;
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 FUNCTION, SUBUNIT, IDENTIFICATION IN THE AFTIPHILIN-P200-GAMMA-SYNERGIN
RP COMPLEX, INTERACTION WITH HEATR5B; SYNRG; AP1G1; CLTCL1 AND GGA1,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 716-TYR--TRP-718.
RX PubMed=15758025; DOI=10.1091/mbc.e04-12-1077;
RA Hirst J., Borner G.H., Harbour M., Robinson M.S.;
RT "The aftiphilin/p200/gamma-synergin complex.";
RL Mol. Biol. Cell 16:2554-2565(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-617, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-617, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151 AND THR-617, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, 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).
CC -!- FUNCTION: Component of clathrin-coated vesicles (PubMed:15758025).
CC Component of the aftiphilin/p200/gamma-synergin complex, which plays
CC roles in AP1G1/AP-1-mediated protein trafficking including the
CC trafficking of transferrin from early to recycling endosomes, and the
CC membrane trafficking of furin and the lysosomal enzyme cathepsin D
CC between the trans-Golgi network (TGN) and endosomes (PubMed:15758025).
CC {ECO:0000269|PubMed:15758025}.
CC -!- SUBUNIT: Self-associates (PubMed:15758025). Interacts with GGA1 (via
CC GAE domain) (PubMed:14665628, PubMed:15758025). Interacts with GGA3
CC (via GAE domain), AP1G1 (via GAE domain) and AP1G2 (via GAE domain)
CC (PubMed:14665628). Component of the aftiphilin/p200/gamma-synergin
CC complex, at least composed of AFTPH/aftiphilin, HEATR5B/p200a and
CC SYNRG/gamma-synergin, which plays a role in the AP1G1/AP-1-mediated
CC protein trafficking from early to recycling endosomes
CC (PubMed:15758025). Within the complex interacts with HEATR5B/p200a and
CC SYNRG/gamma-synergin; the interactions are direct (PubMed:15758025).
CC Interacts with AP1G1/AP-1; the interaction is required to recruit
CC AFTPH/aftiphilin to the perinuclear region of the cell
CC (PubMed:15758025). Interacts with CLTCL1/Clathrin (PubMed:15758025).
CC {ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:15758025}.
CC -!- INTERACTION:
CC Q6ULP2; P63010: AP2B1; NbExp=2; IntAct=EBI-2848714, EBI-432924;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14665628,
CC ECO:0000269|PubMed:15758025}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:15758025}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:15758025}. Note=Co-localizes with AP1G1/AP-
CC 1 in the cytoplasm (PubMed:14665628, PubMed:15758025). Recruited to the
CC perinuclear region by AP1G1/AP-1 (PubMed:15758025).
CC {ECO:0000269|PubMed:14665628, ECO:0000269|PubMed:15758025}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6ULP2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ULP2-6; Sequence=VSP_059492, VSP_059495;
CC Name=3;
CC IsoId=Q6ULP2-7; Sequence=VSP_059493, VSP_059494;
CC Name=4;
CC IsoId=Q6ULP2-8; Sequence=VSP_059492;
CC Name=5;
CC IsoId=Q6ULP2-9; Sequence=VSP_059495;
CC -!- DOMAIN: The WXXF motifs mediate binding of accessory proteins to the
CC ear-domain of AP-1, GGAs and AP-2 through hydrophobic interactions.
CC Selective binding to the GAE domains of AP-1 or to the alpha-ear domain
CC of AP-2 is tuned by the acidic context surrounding the motif and the
CC properties of the second residue of the motif itself (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22247.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH22247.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB13930.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14949.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY367088; AAR14726.1; -; mRNA.
DR EMBL; AK000087; BAA90936.1; -; mRNA.
DR EMBL; AK021899; BAB13930.1; ALT_INIT; mRNA.
DR EMBL; AK024658; BAB14949.1; ALT_INIT; mRNA.
DR EMBL; AL833962; CAE46209.1; -; mRNA.
DR EMBL; CH471053; EAW99938.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99941.1; -; Genomic_DNA.
DR EMBL; BC022247; AAH22247.1; ALT_SEQ; mRNA.
DR EMBL; BC047529; AAH47529.1; -; mRNA.
DR CCDS; CCDS1878.1; -. [Q6ULP2-6]
DR CCDS; CCDS46303.1; -. [Q6ULP2-1]
DR RefSeq; NP_001002243.1; NM_001002243.2. [Q6ULP2-8]
DR RefSeq; NP_060127.3; NM_017657.4. [Q6ULP2-6]
DR RefSeq; NP_982261.2; NM_203437.3. [Q6ULP2-1]
DR RefSeq; XP_005264437.1; XM_005264380.1.
DR AlphaFoldDB; Q6ULP2; -.
DR BioGRID; 120169; 34.
DR ELM; Q6ULP2; -.
DR IntAct; Q6ULP2; 16.
DR MINT; Q6ULP2; -.
DR STRING; 9606.ENSP00000238855; -.
DR GlyGen; Q6ULP2; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q6ULP2; -.
DR PhosphoSitePlus; Q6ULP2; -.
DR BioMuta; AFTPH; -.
DR DMDM; 62286617; -.
DR EPD; Q6ULP2; -.
DR jPOST; Q6ULP2; -.
DR MassIVE; Q6ULP2; -.
DR MaxQB; Q6ULP2; -.
DR PaxDb; Q6ULP2; -.
DR PeptideAtlas; Q6ULP2; -.
DR PRIDE; Q6ULP2; -.
DR ProteomicsDB; 67412; -. [Q6ULP2-1]
DR Antibodypedia; 30831; 110 antibodies from 22 providers.
DR DNASU; 54812; -.
DR Ensembl; ENST00000238855.11; ENSP00000238855.7; ENSG00000119844.16. [Q6ULP2-1]
DR Ensembl; ENST00000238856.8; ENSP00000238856.4; ENSG00000119844.16. [Q6ULP2-6]
DR Ensembl; ENST00000409933.5; ENSP00000387071.1; ENSG00000119844.16. [Q6ULP2-1]
DR GeneID; 54812; -.
DR KEGG; hsa:54812; -.
DR MANE-Select; ENST00000409933.6; ENSP00000387071.1; NM_203437.4; NP_982261.2.
DR UCSC; uc002scz.4; human. [Q6ULP2-1]
DR CTD; 54812; -.
DR DisGeNET; 54812; -.
DR GeneCards; AFTPH; -.
DR HGNC; HGNC:25951; AFTPH.
DR HPA; ENSG00000119844; Low tissue specificity.
DR MIM; 619628; gene.
DR neXtProt; NX_Q6ULP2; -.
DR OpenTargets; ENSG00000119844; -.
DR PharmGKB; PA145149871; -.
DR VEuPathDB; HostDB:ENSG00000119844; -.
DR eggNOG; ENOG502QPXF; Eukaryota.
DR GeneTree; ENSGT00940000154186; -.
DR HOGENOM; CLU_017041_0_0_1; -.
DR InParanoid; Q6ULP2; -.
DR OMA; EEWHESK; -.
DR OrthoDB; 155710at2759; -.
DR PhylomeDB; Q6ULP2; -.
DR TreeFam; TF331532; -.
DR PathwayCommons; Q6ULP2; -.
DR SignaLink; Q6ULP2; -.
DR BioGRID-ORCS; 54812; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; AFTPH; human.
DR GeneWiki; AFTPH; -.
DR GenomeRNAi; 54812; -.
DR Pharos; Q6ULP2; Tbio.
DR PRO; PR:Q6ULP2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6ULP2; protein.
DR Bgee; ENSG00000119844; Expressed in renal medulla and 208 other tissues.
DR ExpressionAtlas; Q6ULP2; baseline and differential.
DR Genevisible; Q6ULP2; HS.
DR GO; GO:0030121; C:AP-1 adaptor complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032588; C:trans-Golgi network membrane; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
DR GO; GO:0046907; P:intracellular transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR046359; Aftin-like.
DR InterPro; IPR029205; Clathrin-bd.
DR PANTHER; PTHR16156; PTHR16156; 1.
DR Pfam; PF15045; Clathrin_bdg; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..936
FT /note="Aftiphilin"
FT /id="PRO_0000064488"
FT REGION 1..523
FT /note="Interaction with AP1G1, AP1G2, GGA1 and GGA3"
FT /evidence="ECO:0000269|PubMed:14665628"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..610
FT /note="Interaction with AP1G1"
FT /evidence="ECO:0000269|PubMed:15758025"
FT REGION 589..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..829
FT /note="Clathrin-binding"
FT /evidence="ECO:0000255"
FT MOTIF 28..31
FT /note="WXXF motif 1"
FT MOTIF 432..435
FT /note="WXXF motif 2"
FT MOTIF 436..438
FT /note="WXXF motif 3 (partial)"
FT MOTIF 478..481
FT /note="WXXF motif 4"
FT MOTIF 716..718
FT /note="CLTCL1/Clathrin-binding"
FT /evidence="ECO:0000269|PubMed:15758025"
FT COMPBIAS 593..614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80WT5"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 617
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 819..846
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_059492"
FT VAR_SEQ 819..820
FT /note="AS -> GT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_059493"
FT VAR_SEQ 821..936
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_059494"
FT VAR_SEQ 887
FT /note="T -> TS (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_059495"
FT VARIANT 233
FT /note="D -> G (in dbSNP:rs35986567)"
FT /id="VAR_056728"
FT VARIANT 301
FT /note="E -> K (in dbSNP:rs3770740)"
FT /id="VAR_056729"
FT VARIANT 550
FT /note="N -> S (in dbSNP:rs3770739)"
FT /id="VAR_056730"
FT MUTAGEN 716..718
FT /note="YQW->SQS: Abolishes the interaction with
FT CLTCL1/Clathrin."
FT /evidence="ECO:0000269|PubMed:15758025"
FT CONFLICT 705
FT /note="L -> Q (in Ref. 2; BAB14949)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="D -> G (in Ref. 2; BAB13930)"
FT /evidence="ECO:0000305"
FT CONFLICT 850
FT /note="P -> L (in Ref. 1; AAR14726)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="E -> G (in Ref. 5; AAH22247)"
FT /evidence="ECO:0000305"
FT CONFLICT 904
FT /note="I -> V (in Ref. 5; AAH47529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 936 AA; 102113 MW; 7F84B4D6890BCDF7 CRC64;
MEPDIIRMYS SSPPPLDNGA EDDDDDEFGE FGGFSEVSPS GVGFVDFDTP DYTRPKEEFV
PSNHFMPIHE FSENVDSLTS FKSIKNGNDK DITAELSAPV KGQSDVLLST TSKEIISSEM
LATSIDGMER PGNLNKVVEQ RQNVGTLESF SPGDFRTNMN VVHQNKQLES CNGEKPPCLE
ILTNGFAVLE TVNPQGTDDL DNVADSKGRK PLSTHSTEYN LDSVPSPAEE FADFATFSKK
ERIQLEEIEC AVLNDREALT IRENNKINRV NELNSVKEVA LGRSLDNKGD TDGEDQVCVS
EISIVTNRGF SVEKQGLPTL QQDEFLQSGV QSKAWSLVDS ADNSEAIRRE QCKTEEKLDL
LTSKCAHLCM DSVKTSDDEV GSPKEESRKF TNFQSPNIDP TEENDLDDSL SVKNGDSSND
FVTCNDINED DFGDFGDFGS ASGSTPPFVT GTQDSMSDAT FEESSEHFPH FSEPGDDFGE
FGDINAVSCQ EETILTKSDL KQTSDNLSEE CQLARKSSGT GTEPVAKLKN GQEGEIGHFD
SVPNIQDDCN GFQDSDDFAD FSSAGPSQVV DWNAFEDEQK DSCSWAAFGD QQATESHHRK
EAWQSHRTDE NIDTPGTPKT HSVPSATSKG AVASGHLQES ATSVQTALLN RLERIFEACF
PSILVPDAEE EVTSLKHLLE TSTLPIKTRE ALPESGELLD VWTELQDIHD AHGLRYQWGG
SHSNKKLLSS LGIDTRNILF TGNKKQPVIV PMYAAGLGML EPTKEPLKPL SAAEKIASIG
QTATMSPDMN TCTSDQFQES LPPVQFDWSS SGLTNPLDAS GGSTLLNLDF FGPVDDSSSS
SSTTIPGVDP ELYELTTSKL EISTSSLKVT DAFARLMSTV EKTSTSTRKP KREEHLSEEA
IKVIAGLPDL TFMHAKVLMF PATLTPSTSS QEKADG
