K1107_MOUSE
ID K1107_MOUSE Reviewed; 1239 AA.
AC Q80TK0; E9PUC9; E9QLA8; Q3TPG8; Q8BRQ7; Q8BRS6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 6.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=AP2-interacting clathrin-endocytosis protein {ECO:0000303|PubMed:29262337};
DE Short=APache {ECO:0000303|PubMed:29262337};
GN Name=Kiaa1107;
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].
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] OF 1-969.
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-1239.
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [5]
RP FUNCTION, INTERACTION WITH AP2A1 AND AP2B1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
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:0000269|PubMed:29262337}.
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:0000269|PubMed:29262337}. Presynapse
CC {ECO:0000269|PubMed:29262337}. 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:0000269|PubMed:29262337}.
CC -!- TISSUE SPECIFICITY: Neuron-specific protein. Primarily expressed in
CC brain, with the highest levels in the cerebral cortex, hippocampus, and
CC striatum (at protein level). Not detected in glial cells.
CC {ECO:0000269|PubMed:29262337}.
CC -!- DEVELOPMENTAL STAGE: In the developing brain cortex, expressed at 18
CC dpc. Expression increases during postnatal development to reach a
CC plateau at 1 month of age. {ECO:0000269|PubMed:29262337}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31628.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC117574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC126598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK043587; BAC31589.1; -; mRNA.
DR EMBL; AK043720; BAC31628.1; ALT_FRAME; mRNA.
DR EMBL; AK164388; BAE37768.1; -; mRNA.
DR EMBL; AK122444; BAC65726.3; -; Transcribed_RNA.
DR RefSeq; NP_001007575.2; NM_001007574.2.
DR AlphaFoldDB; Q80TK0; -.
DR BioGRID; 231135; 6.
DR IntAct; Q80TK0; 1.
DR MINT; Q80TK0; -.
DR iPTMnet; Q80TK0; -.
DR PhosphoSitePlus; Q80TK0; -.
DR MaxQB; Q80TK0; -.
DR PaxDb; Q80TK0; -.
DR PRIDE; Q80TK0; -.
DR ProteomicsDB; 301711; -.
DR ProteomicsDB; 365951; -.
DR Ensembl; ENSMUST00000100951; ENSMUSP00000098511; ENSMUSG00000111375.
DR GeneID; 100503185; -.
DR CTD; 284697; -.
DR MGI; MGI:2445097; A830010M20Rik.
DR VEuPathDB; HostDB:ENSMUSG00000111375; -.
DR eggNOG; ENOG502QUK4; Eukaryota.
DR GeneTree; ENSGT00940000154382; -.
DR HOGENOM; CLU_002418_0_0_1; -.
DR InParanoid; Q80TK0; -.
DR OrthoDB; 213120at2759; -.
DR BioGRID-ORCS; 231570; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q80TK0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80TK0; protein.
DR Bgee; ENSMUSG00000111375; Expressed in habenula and 201 other tissues.
DR ExpressionAtlas; Q80TK0; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0044297; C:cell body; IDA: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; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0150007; P:clathrin-dependent synaptic vesicle endocytosis; IMP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0016182; P:synaptic vesicle budding from endosome; IDA:SynGO.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0036466; P:synaptic vesicle recycling via endosome; IMP: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 Cell projection; Cytoplasmic vesicle; Endocytosis; Reference proteome;
KW Synapse.
FT CHAIN 1..1239
FT /note="AP2-interacting clathrin-endocytosis protein"
FT /id="PRO_0000320678"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1083
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1204..1227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 11
FT /note="V -> A (in Ref. 3; BAC65726)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="V -> A (in Ref. 3; BAC65726)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="Missing (in Ref. 2; BAC31628)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="D -> N (in Ref. 3; BAC65726)"
FT /evidence="ECO:0000305"
FT CONFLICT 1011
FT /note="S -> N (in Ref. 3; BAC65726)"
FT /evidence="ECO:0000305"
FT CONFLICT 1085..1086
FT /note="DI -> NV (in Ref. 3; BAC65726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1239 AA; 134060 MW; E2C62E25E8139E09 CRC64;
MHLDDQQKIQ VAALDKGDDR RLGRKPVLTS SQQRRQGSDV DVLKIKPWTE NNKKPCQTSL
STNQKMRSDG LGASGHASST NRNSINKVSK HGDSTKMSKV VKEMKTGGKY VSGKSKTMVK
PQTENSDHTK IEGLSSTVVG RPSRVTAAGR KDPVHGKGVQ NQEVETTGAR PKVLTANLNV
QARAKPLQTL RGKDSTCPAS VGPSSRSTHS STELLASMGS VDETKENGSV EDKCRDGKPY
VSDSPGQMVS NGVMSTAAVK SRAVARITNG TASNKSFTHE QDSHGNSSVI KRGDGKGLSA
SAPQTAAKKR GSSNGCTAAQ PRTKSAPPTL AQAQGSQGES PHSVKSSVSS RQSDENVTRL
RHGTDKQIPK RKVVKQGHTT LQKVNAKLVP MPKIPSQPKK GGTVNSKDSK QKVLPGQIML
QSHASQRPSK PEVAEKSVLH GVSDSRNHVS KQRPHESPCT LACDTSGPEV SQIPCRPQPQ
SPLGSQEKKR LELACQDRST LGDSVKRELR SELAGIEQSH TSAYKDSSQC NGNPNCGSIA
ALKSVISNPN ENLINSNPVH NSDSANTEQA YLSDRERETG RENTDTEPSM SCINGKAFLC
VPEGTSSTLN PTQSDRRLTF HGAAQSQLPD DCATEDSKCA TVTSAVSSKC LLGQPSEKNC
KNMEMSETPE SHGTPEAPFV GPWDLNTGAT HQRESPESDT GSATTSSDDI KPRSEDYDAG
GSQDDEGSHD RGISKCSTAL CHDFLGRSSS DTSTPEELKV HEGDLRTEVR VRKQGGGDHQ
IHSASDDEIP RKKPEPWSRS TIGYPREKGS TPRGSIPSAQ EGDQVSSSAD ETEDERSEAE
NVGENSSPCS SGTQQVQGII NLAFDDGAEH ESREFSATKK FRRSVLLSVD ECEEVGSDEG
EGHTPFQPSL DSLSPSDVFD GVSYEHHGRT GYSRFFKENE ATTAEHNHNK GNGGYKNESF
LLNSRSKDFE KQDKQCVSTD QKTRLDVPPK GSQQLFPENE EVISKREAAH SFQQHSTFMD
GDTKSQERPC HLELHQRELS SNIPKISSVK SLDSCPSQGL PQEGQVKESR PTPPKGANNA
VFSGDIDDCD TMAQTSMYDH RPSKTLSPIY EMSLTAACEQ EVESETHVAD RGSEDEQHFA
KQDWTLLRQL LSEQDANLNI TSSLPEDLSL AQYLINQTLL LARDSSKPQG SAHADTWNRW
SELSSPLDDS ATSATTASVS STDCSPQGEW TILELETQH
