K1107_RAT
ID K1107_RAT Reviewed; 1237 AA.
AC D4A0X3;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 3.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=AP2-interacting clathrin-endocytosis protein {ECO:0000303|PubMed:29262337};
DE Short=APache {ECO:0000303|PubMed:29262337};
GN Name=Kiaa1107; Synonyms=Btbd8;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
CC {ECO:0000250|UniProtKB:Q80TK0}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:29262337}. Presynapse
CC {ECO:0000269|PubMed:29262337}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000269|PubMed:29262337}. Note=In primary cultures, mainly
CC present at axonal and presynaptic terminal levels of mature neurons. In
CC immature neurons, localizes to the cell body and growing processes,
CC including axons. {ECO:0000250|UniProtKB:Q80TK0}.
CC -!- TISSUE SPECIFICITY: Neuron-specific protein. Expressed in brain (at
CC protein level). {ECO:0000269|PubMed:29262337}.
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DR EMBL; AC106605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017454900.1; XM_017599411.1.
DR AlphaFoldDB; D4A0X3; -.
DR STRING; 10116.ENSRNOP00000038747; -.
DR iPTMnet; D4A0X3; -.
DR PhosphoSitePlus; D4A0X3; -.
DR PaxDb; D4A0X3; -.
DR PRIDE; D4A0X3; -.
DR GeneID; 100364240; -.
DR CTD; 284697; -.
DR RGD; 2321418; Btbd8.
DR eggNOG; ENOG502QUK4; Eukaryota.
DR HOGENOM; CLU_002418_0_0_1; -.
DR InParanoid; D4A0X3; -.
DR TreeFam; TF335820; -.
DR PRO; PR:D4A0X3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030122; C:AP-2 adaptor complex; ISO:RGD.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0044306; C:neuron projection terminus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA: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:0016182; P:synaptic vesicle budding from endosome; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:RGD.
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 Cell projection; Cytoplasmic vesicle; Endocytosis; Reference proteome;
KW Synapse.
FT CHAIN 1..1237
FT /note="AP2-interacting clathrin-endocytosis protein"
FT /id="PRO_0000444635"
FT REGION 1..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1135
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 52..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..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 382..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1033
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1237 AA; 133257 MW; 41E203CA7D97213E CRC64;
MHIDDQQKIQ AAALDKGDDR RLGRKPVLSS SQQRRQGSDV IKIKPWTGNN KKLCRASPST
NEKMRSDGLG ASGHASGTHR NSVNKVSKHG EGTKVSKVTT EVKTGATHVP GKPKTTIKPQ
TENNAHTKLE SISSTVVGRP ARMAATGRKD LAHGKGIQNQ EGETTGARPK VLTANLNTQA
RAKPLQTVKG KDNGCSATVG PSSRSANSSM ERLASTGSVD ETKENGSVED KSCDKKPYVS
ASPGQMVYNG VTSTVAVKSR PVSRVTSGTS SKKSFIHEQG PSVTSSVIKK GRGSSKGLND
SAPQTAAKRG GSSNGYAAAQ PRTKSAPPTL AQTQGSQGES PHSVKSSISS RQSDESVTRL
RHGTDKQMPK RKVVKQGHAT LQKVNAKPTP KNPSQSTKGG TMTSKDSKQK VLPGQVTLQS
QASQRPSNPE AATTQRSVLH GVNDNRSQVF KQRPPESLVN LASDTNGPEA SPSPCRPQPQ
SPLGNQEKTR QEREHQDGST LGDSVKHELR SELTSIEQSH TPAYKVSSQC SANPNCGCIA
SLKPVTSNPS ENWINSNTAN TDQVCVSDRE RQTGRKGTDR EPSVNCVARK AALPSVPAGM
SGTLKSAQDD RKLPFHREEL SAQGHLPHDC ATEDSKCATP TSAVSSRCLL GQPSEKGYKN
MEASGTSESH EAPEAPFMGP WDLNTSATHQ RESPESDTGS ATTSSDDIKP RSEDYDAGGS
QDDEGSHDRG VSKCSTALCH DFLGRSSSDT STPEELKVHE GDLRTEVRVR KPGGGDLPLH
SASDDETPRK KPDPWSRSTI VHPREKGSAP RGSVPSAQEV DQVSSSADET EDERSEAENV
REHSSPSNSG TQHVQGIINL AFEDGTEHES REFSATKKFR RSVLLSVDEC EEVGSDEGEG
HTPLQPSLDS LSPSDVFDGV SYEHHGRTGY SRFFKENEAT TAEHKYSRGN DGHKNEGFLL
SPRSRDFPRQ GKQCVSTGEK TRLDVPPKAS QQPFPESKDM TSKREVAHGL QQHGTLTDGD
TRSQERPCHL ELHQREPSST IPKISSARSL DSCPSQVLPQ DGQVTATHPT PPKRANNAVF
SGDIDDCDTM AQTTMYDHRP SKTLSPIHEM SLTAACEQKE ESGTHVADRA SEDEQPFAKQ
DWTLLKQLLS EQDANLNVTS SLPEDLSLAQ YLINQTLLLA RDSSKPQGSA HADTWNRWSE
LSSPLDDLTA SATTVSVSST DCSPQGEWTI LELETQH
