AFTIN_MOUSE
ID AFTIN_MOUSE Reviewed; 931 AA.
AC Q80WT5; Q5SSE6; Q99KJ1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Aftiphilin;
GN Name=Aftph; Synonyms=Afth;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of clathrin-coated vesicles (By similarity).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q6ULP2}.
CC -!- SUBUNIT: Self-associates (By similarity). Interacts with GGA1 (via GAE
CC domain) (By similarity). Interacts with GGA3 (via GAE domain), AP1G1
CC (via GAE domain) and AP1G2 (via GAE domain) (By similarity). Component
CC of the aftiphilin/p200/gamma-synergin complex, at least composed of
CC AFTPH/aftiphilin, HEATR5B/p200a and SYNRG/gamma-synergin, which plays a
CC role in the AP1G1/AP-1-mediated protein trafficking from early to
CC recycling endosomes (By similarity). Within the complex interacts with
CC HEATR5B/p200a and SYNRG/gamma-synergin; the interactions are direct (By
CC similarity). Interacts with AP1G1/AP-1; the interaction is required to
CC recruit AFTPH/aftiphilin to the perinuclear region of the cell (By
CC similarity). Interacts with CLTCL1/Clathrin (By similarity).
CC {ECO:0000250|UniProtKB:Q6ULP2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6ULP2}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q6ULP2}.
CC Cytoplasmic vesicle, clathrin-coated vesicle
CC {ECO:0000250|UniProtKB:Q6ULP2}. Note=Co-localizes with AP1G1/AP-1 in
CC the cytoplasm (By similarity). Recruited to the perinuclear region by
CC AP1G1/AP-1 (By similarity). {ECO:0000250|UniProtKB:Q6ULP2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80WT5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80WT5-2; Sequence=VSP_013242;
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 -!- SEQUENCE CAUTION:
CC Sequence=CAI24910.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI25738.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL663115; CAI25737.1; -; Genomic_DNA.
DR EMBL; AL645599; CAI25737.1; JOINED; Genomic_DNA.
DR EMBL; AL663115; CAI25738.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL645599; CAI25738.1; JOINED; Genomic_DNA.
DR EMBL; AL645599; CAI24909.1; -; Genomic_DNA.
DR EMBL; AL663115; CAI24909.1; JOINED; Genomic_DNA.
DR EMBL; AL645599; CAI24910.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL663115; CAI24910.1; JOINED; Genomic_DNA.
DR EMBL; BC004630; AAH04630.1; -; mRNA.
DR EMBL; BC052036; AAH52036.1; -; mRNA.
DR CCDS; CCDS24459.1; -. [Q80WT5-2]
DR CCDS; CCDS70146.1; -. [Q80WT5-1]
DR RefSeq; NP_001239432.1; NM_001252503.2.
DR RefSeq; NP_001277474.1; NM_001290545.1. [Q80WT5-1]
DR RefSeq; NP_852076.1; NM_181411.4. [Q80WT5-2]
DR AlphaFoldDB; Q80WT5; -.
DR BioGRID; 229758; 2.
DR MINT; Q80WT5; -.
DR STRING; 10090.ENSMUSP00000036778; -.
DR iPTMnet; Q80WT5; -.
DR PhosphoSitePlus; Q80WT5; -.
DR EPD; Q80WT5; -.
DR jPOST; Q80WT5; -.
DR MaxQB; Q80WT5; -.
DR PaxDb; Q80WT5; -.
DR PeptideAtlas; Q80WT5; -.
DR PRIDE; Q80WT5; -.
DR ProteomicsDB; 285621; -. [Q80WT5-1]
DR ProteomicsDB; 285622; -. [Q80WT5-2]
DR Antibodypedia; 30831; 110 antibodies from 22 providers.
DR DNASU; 216549; -.
DR Ensembl; ENSMUST00000035350; ENSMUSP00000036778; ENSMUSG00000049659. [Q80WT5-2]
DR Ensembl; ENSMUST00000146722; ENSMUSP00000121612; ENSMUSG00000049659. [Q80WT5-1]
DR GeneID; 216549; -.
DR KEGG; mmu:216549; -.
DR UCSC; uc007idh.3; mouse. [Q80WT5-2]
DR UCSC; uc056yjx.1; mouse. [Q80WT5-1]
DR CTD; 54812; -.
DR MGI; MGI:1923012; Aftph.
DR VEuPathDB; HostDB:ENSMUSG00000049659; -.
DR eggNOG; ENOG502QPXF; Eukaryota.
DR GeneTree; ENSGT00940000154186; -.
DR HOGENOM; CLU_017041_0_0_1; -.
DR InParanoid; Q80WT5; -.
DR OMA; EEWHESK; -.
DR OrthoDB; 155710at2759; -.
DR PhylomeDB; Q80WT5; -.
DR TreeFam; TF331532; -.
DR BioGRID-ORCS; 216549; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Aftph; mouse.
DR PRO; PR:Q80WT5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q80WT5; protein.
DR Bgee; ENSMUSG00000049659; Expressed in dentate gyrus of hippocampal formation granule cell and 240 other tissues.
DR ExpressionAtlas; Q80WT5; baseline and differential.
DR Genevisible; Q80WT5; MM.
DR GO; GO:0030121; C:AP-1 adaptor complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISO:MGI.
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..931
FT /note="Aftiphilin"
FT /id="PRO_0000064489"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..825
FT /note="Clathrin-binding"
FT /evidence="ECO:0000255"
FT MOTIF 28..31
FT /note="WXXF motif 1"
FT MOTIF 433..436
FT /note="WXXF motif 2"
FT MOTIF 476..479
FT /note="WXXF motif 3"
FT MOTIF 712..714
FT /note="CLTCL1/Clathrin-binding"
FT /evidence="ECO:0000250|UniProtKB:Q6ULP2"
FT COMPBIAS 379..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ULP2"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 613
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ULP2"
FT VAR_SEQ 815..841
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_013242"
SQ SEQUENCE 931 AA; 101131 MW; FE1C64F3B7270620 CRC64;
MEPDIIRMYS SSPPPLDNGA EDDEEDEFGE FGGFSEVSPS GVGFVDFDTP DYTRPKEDFV
PSNHFMPIHE YSEDVDSLTS FKSVQNGNDK DITAELSTPV KSQSDVVLST TSKEMIPSKT
LDPSIDGMES LEDLDKVVVQ GPSTGQLRSF SPGDFRTDKN IVHQTKQLES CNGEKPPCLE
ILTNGFAGLE TVNPQGTDDL DNVADSKGSK PLNTCGTECI LESAASHATE FADFSTFSQT
ERTQLEEIEC PVLNDGDTLT IQGNSKGPRV KELNCVKEVT LDGSFEDTGN TEREHQVCVS
EIHAVADRGL SVEKQDLQTL QQDEFLNSRI QSEAWSLVDS SENSEAITKE RCKMEKNDLF
ASKCADLSMD SVKTSDVNEI GSSKEENRKL TNPKSPDPDP TGQNALDDSA ASMKNGDSGN
GFVTCHDTNE DDFGDFGTAN GTTPPFVTST QDSMSDVTFE DSSEHFLHLS EPGDDFGEFE
DTNAVSCQEE MRFTESDLRQ TSDGLSEECP LAGESGGKDS KPDSKLKNGQ DSEFGDFDSV
PNTQGSAFQD SDDFADFSSA GPSQAVDWNA FEDEQKDGCS WAAFGDQQET ESHHLKEVWQ
SQRTDETMGT LGTPKMHSVS SAASKGAVAS GHLQEPGTSV QTALLNRLER IFEACFPSVF
VPDVEEEVSS LKHLLETHSS PAKTREALAD RGELRGVWTE LQDIHDAHGL RYQWGGSHSN
KKLLCSLGID TRNILFTGNK KQPVIVPMYA AGLGMLEPTK EPLKPLSAAE KIASIGQTTV
MTPEINTCTS DPFQESLPPV QFDWSSSGLT NPLDASGGST LLNLDFFGPV DDSSSSSSTI
PGVDPELYEL TTAKLETSTS SLRVTDAFAK LMSTVEKTST STRKPKREEH LSEEAMKVIA
SLPDLTFMHA KVLMFPATLT PSMSSQEQAD A
