K1107_HUMAN
ID K1107_HUMAN Reviewed; 1279 AA.
AC Q9UPP5; A0A1B0GWG1; O14767; Q8N3X7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=AP2-interacting clathrin-endocytosis protein {ECO:0000303|PubMed:29262337};
DE Short=APache {ECO:0000303|PubMed:29262337};
GN Name=KIAA1107;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-79.
RC TISSUE=Frontal cortex;
RG The Stanley neuropathology consortium;
RA Yolken R., Leister F., Li S., Johnston N., Torrey E.F.;
RT "Development of subtraction libraries from the brains of individuals with
RT psychiatric diseases.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1279 (ISOFORM 1), AND VARIANT
RP ASN-918.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 836-1279 (ISOFORM 2), AND VARIANT
RP ASN-918.
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 [5]
RP INTERACTION WITH AP2A1 AND AP2B1.
RX PubMed=29262337; DOI=10.1016/j.celrep.2017.11.073;
RA Piccini A., Castroflorio E., Valente P., Guarnieri F.C., Aprile D.,
RA Michetti C., Bramini M., Giansante G., Pinto B., Savardi A., Cesca F.,
RA Bachi A., Cattaneo A., Wren J.D., Fassio A., Valtorta F., Benfenati F.,
RA Giovedi S.;
RT "APache is an AP2-interacting protein involved in synaptic vesicle
RT trafficking and neuronal development.";
RL Cell Rep. 21:3596-3611(2017).
CC -!- FUNCTION: Involved in clathrin-mediated endocytosis at the synapse.
CC Plays a role in neuronal development and in synaptic vesicle recycling
CC in mature neurons, a process required for normal synaptic transmission.
CC {ECO:0000250|UniProtKB:Q80TK0}.
CC -!- SUBUNIT: Interacts (via N-terminus) with adaptor protein complex AP-2
CC subunits alpha (AP2A1) and beta (AP2B1). {ECO:0000269|PubMed:29262337}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000250|UniProtKB:Q80TK0}. Presynapse
CC {ECO:0000250|UniProtKB:Q80TK0}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:D4A0X3}. Note=In primary cultures,
CC mainly present at axonal and presynaptic terminal levels of mature
CC neurons. In immature neurons, localizes to the cell body and growing
CC processes, including axons. {ECO:0000250|UniProtKB:Q80TK0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UPP5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPP5-2; Sequence=VSP_031737, VSP_031738;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC28132.1; Type=Erroneous initiation; Note=Extended N-terminus.; 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; AC104836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF017090; AAC28132.1; ALT_INIT; mRNA.
DR EMBL; AB029030; BAA83059.1; -; mRNA.
DR EMBL; BC037317; AAH37317.2; -; mRNA.
DR CCDS; CCDS44172.2; -. [Q9UPP5-1]
DR RefSeq; NP_056052.3; NM_015237.3. [Q9UPP5-1]
DR AlphaFoldDB; Q9UPP5; -.
DR BioGRID; 116883; 36.
DR IntAct; Q9UPP5; 28.
DR MINT; Q9UPP5; -.
DR STRING; 9606.ENSP00000359404; -.
DR iPTMnet; Q9UPP5; -.
DR PhosphoSitePlus; Q9UPP5; -.
DR BioMuta; KIAA1107; -.
DR DMDM; 172045554; -.
DR EPD; Q9UPP5; -.
DR jPOST; Q9UPP5; -.
DR MassIVE; Q9UPP5; -.
DR MaxQB; Q9UPP5; -.
DR PaxDb; Q9UPP5; -.
DR PeptideAtlas; Q9UPP5; -.
DR PRIDE; Q9UPP5; -.
DR ProteomicsDB; 85400; -. [Q9UPP5-1]
DR ProteomicsDB; 85401; -. [Q9UPP5-2]
DR Antibodypedia; 33636; 33 antibodies from 12 providers.
DR DNASU; 284697; -.
DR GeneID; 284697; -.
DR KEGG; hsa:284697; -.
DR CTD; 284697; -.
DR GeneCards; KIAA1107; -.
DR HGNC; HGNC:29192; KIAA1107.
DR HPA; ENSG00000189195; Group enriched (brain, retina, testis).
DR MIM; 617945; gene.
DR neXtProt; NX_Q9UPP5; -.
DR OpenTargets; ENSG00000189195; -.
DR PharmGKB; PA142671620; -.
DR VEuPathDB; HostDB:ENSG00000189195; -.
DR eggNOG; ENOG502QUK4; Eukaryota.
DR GeneTree; ENSGT00940000154382; -.
DR InParanoid; Q9UPP5; -.
DR OrthoDB; 213120at2759; -.
DR PhylomeDB; Q9UPP5; -.
DR PathwayCommons; Q9UPP5; -.
DR SignaLink; Q9UPP5; -.
DR BioGRID-ORCS; 23285; 17 hits in 1072 CRISPR screens.
DR ChiTaRS; KIAA1107; human.
DR GenomeRNAi; 23285; -.
DR Pharos; Q9UPP5; Tdark.
DR PRO; PR:Q9UPP5; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9UPP5; protein.
DR ExpressionAtlas; Q9UPP5; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0044306; C:neuron projection terminus; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0150007; P:clathrin-dependent synaptic vesicle endocytosis; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0036466; P:synaptic vesicle recycling via endosome; ISS:UniProtKB.
DR InterPro; IPR027907; DUF4596.
DR InterPro; IPR040121; KIAA1107.
DR PANTHER; PTHR22427:SF2; PTHR22427:SF2; 1.
DR Pfam; PF15363; DUF4596; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasmic vesicle; Endocytosis;
KW Reference proteome; Synapse.
FT CHAIN 1..1279
FT /note="AP2-interacting clathrin-endocytosis protein"
FT /id="PRO_0000320677"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..770
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1126..1129
FT /note="DIDD -> NVQK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031737"
FT VAR_SEQ 1130..1279
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031738"
FT VARIANT 292
FT /note="H -> R (in dbSNP:rs2128647)"
FT /id="VAR_060300"
FT VARIANT 312
FT /note="S -> I (in dbSNP:rs12084085)"
FT /id="VAR_060301"
FT VARIANT 392
FT /note="V -> L (in dbSNP:rs7552286)"
FT /id="VAR_060302"
FT VARIANT 472
FT /note="Q -> R (in dbSNP:rs11166332)"
FT /id="VAR_060303"
FT VARIANT 551
FT /note="D -> G (in dbSNP:rs7523466)"
FT /id="VAR_060304"
FT VARIANT 585
FT /note="N -> Y (in dbSNP:rs7523552)"
FT /id="VAR_060305"
FT VARIANT 696
FT /note="K -> E (in dbSNP:rs3738439)"
FT /id="VAR_060306"
FT VARIANT 815
FT /note="N -> S (in dbSNP:rs560389)"
FT /id="VAR_060307"
FT VARIANT 918
FT /note="T -> N (in dbSNP:rs565156)"
FT /id="VAR_060308"
FT VARIANT 953
FT /note="F -> V (in dbSNP:rs17578364)"
FT /id="VAR_060309"
FT VARIANT 1028
FT /note="V -> I (in dbSNP:rs566576)"
FT /id="VAR_060310"
FT CONFLICT 886
FT /note="F -> L (in Ref. 4; AAH37317)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1279 AA; 140918 MW; 6AB67B898C487F64 CRC64;
MSTDDQQKIQ AAAFDKGDDR RLGKKPIFSS SQQRKQVSDS GDIKIKSWRG NNKKECWSYL
STNKKMKSDG LGASGHSSST NRNSINKTLK QDDVKEKDGT KIASKITKEL KTGGKNVSGK
PKTVTKSKTE NGDKARLENM SPRQVVERSA TAAAAATGQK NLLNGKGVRN QEGQISGARP
KVLTGNLNVQ AKAKPLKKAT GKDSPCLSIA GPSSRSTDSS MEFSISTECL DEPKENGSTE
EEKPSGHKLS FCDSPGQMMK NSVDSVKNST VAIKSRPVSR VTNGTSNKKS IHEQDTNVNN
SVLKKVSGKG CSEPVPQAIL KKRGTSNGCT AAQQRTKSTP SNLTKTQGSQ GESPNSVKSS
VSSRQSDENV AKLDHNTTTE KQAPKRKMVK QVHTALPKVN AKIVAMPKNL NQSKKGETLN
NKDSKQKMPP GQVISKTQPS SQRPLKHETS TVQKSMFHDV RDNNNKDSVS EQKPHKPLIN
LASEISDAEA LQSSCRPDPQ KPLNDQEKEK LALECQNISK LDKSLKHELE SKQICLDKSE
TKFPNHKETD DCDAANICCH SVGSDNVNSK FYSTTALKYM VSNPNENSLN SNPVCDLDST
SAGQIHLISD RENQVGRKDT NKQSSIKCVE DVSLCNPERT NGTLNSAQED KKSKVPVEGL
TIPSKLSDES AMDEDKHATA DSDVSSKCFS GQLSEKNSPK NMETSESPES HETPETPFVG
HWNLSTGVLH QRESPESDTG SATTSSDDIK PRSEDYDAGG SQDDDGSNDR GISKCGTMLC
HDFLGRSSSD TSTPEELKIY DSNLRIEVKM KKQSNNDLFQ VNSTSDDEIP RKRPEIWSRS
AIVHSREREN IPRGSVQFAQ EIDQVSSSAD ETEDERSEAE NVAENFSISN PAPQQFQGII
NLAFEDATEN ECREFSATKK FKRSVLLSVD ECEELGSDEG EVHTPFQASV DSFSPSDVFD
GISHEHHGRT CYSRFSRESE DNILECKQNK GNSVCKNEST VLDLSSIDSS RKNKQSVSAT
EKKNTIDVLS SRSRQLLRED KKVNNGSNVE NDIQQRSKFL DSDVKSQERP CHLDLHQREP
NSDIPKNSST KSLDSFRSQV LPQEGPVKES HSTTTEKANI ALSAGDIDDC DTLAQTRMYD
HRPSKTLSPI YEMDVIEAFE QKVESETHVT DMDFEDDQHF AKQDWTLLKQ LLSEQDSNLD
VTNSVPEDLS LAQYLINQTL LLARDSSKPQ GITHIDTLNR WSELTSPLDS SASITMASFS
SEDCSPQGEW TILELETQH
