NECP1_RAT
ID NECP1_RAT Reviewed; 277 AA.
AC P69682; Q4QR67;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Adaptin ear-binding coat-associated protein 1;
DE AltName: Full=NECAP endocytosis-associated protein 1;
DE Short=NECAP-1;
GN Name=Necap1;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 PROTEIN SEQUENCE OF 103-128 AND 161-169, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, AND INTERACTION WITH
RP AP1G1 AND AP2A1.
RX PubMed=14555962; DOI=10.1038/sj.embor.embor7400004;
RA Ritter B., Philie J., Girard M., Tung E.C., Blondeau F., McPherson P.S.;
RT "Identification of a family of endocytic proteins that define a new alpha-
RT adaptin ear-binding motif.";
RL EMBO Rep. 4:1089-1095(2003).
RN [5]
RP DOMAIN, AND INTERACTION WITH AP2A2.
RX PubMed=15292237; DOI=10.1074/jbc.m408095200;
RA Mishra S.K., Hawryluk M.J., Brett T.J., Keyel P.A., Dupin A.L., Jha A.,
RA Heuser J.E., Fremont D.H., Traub L.M.;
RT "Dual engagement regulation of protein interactions with the AP-2 adaptor
RT alpha appendage.";
RL J. Biol. Chem. 279:46191-46203(2004).
RN [6]
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).
CC -!- FUNCTION: Involved in endocytosis. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with AP1G1 and AP2A1 components of the adapter
CC protein complexes AP-1 and AP-2. Interacts with the GAE domain proteins
CC GGA1, GGA2 and GGA3 (By similarity). Interacts with AP2A2.
CC {ECO:0000250, ECO:0000269|PubMed:14555962,
CC ECO:0000269|PubMed:15292237}.
CC -!- INTERACTION:
CC P69682; P49418: AMPH; Xeno; NbExp=3; IntAct=EBI-7592718, EBI-7121510;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000269|PubMed:14555962}. Cell membrane
CC {ECO:0000269|PubMed:14555962}. Note=Partially colocalizes with AP-2 at
CC the plasma membrane.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain (at protein
CC level). {ECO:0000269|PubMed:14555962}.
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. The WXXF motif 1,
CC which is preceded by an acidic residue and has a glycine in second
CC position mediates specific interaction with AP-1. The WXXF motif 2,
CC which is followed by the C-terminal carboxyl group negative charge,
CC allows specific interaction with AP-2. {ECO:0000269|PubMed:14555962,
CC ECO:0000269|PubMed:15292237}.
CC -!- SIMILARITY: Belongs to the NECAP family. {ECO:0000305}.
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DR EMBL; AABR03032682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC097496; AAH97496.1; -; mRNA.
DR RefSeq; NP_001025090.1; NM_001029919.2.
DR AlphaFoldDB; P69682; -.
DR SMR; P69682; -.
DR BioGRID; 300059; 10.
DR DIP; DIP-44064N; -.
DR IntAct; P69682; 6.
DR MINT; P69682; -.
DR STRING; 10116.ENSRNOP00000013272; -.
DR iPTMnet; P69682; -.
DR PhosphoSitePlus; P69682; -.
DR jPOST; P69682; -.
DR PaxDb; P69682; -.
DR PRIDE; P69682; -.
DR GeneID; 312694; -.
DR KEGG; rno:312694; -.
DR UCSC; RGD:1306053; rat.
DR CTD; 25977; -.
DR RGD; 1306053; Necap1.
DR VEuPathDB; HostDB:ENSRNOG00000009236; -.
DR eggNOG; KOG2500; Eukaryota.
DR HOGENOM; CLU_069884_1_1_1; -.
DR InParanoid; P69682; -.
DR OMA; TFSNHNT; -.
DR OrthoDB; 1605812at2759; -.
DR PhylomeDB; P69682; -.
DR TreeFam; TF314482; -.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P69682; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000009236; Expressed in cerebellum and 19 other tissues.
DR Genevisible; P69682; RN.
DR GO; GO:0030125; C:clathrin vesicle coat; ISO:RGD.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd13228; PHear_NECAP; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR012466; NECAP_PHear.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF07933; DUF1681; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Direct protein sequencing; Endocytosis;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..277
FT /note="Adaptin ear-binding coat-associated protein 1"
FT /id="PRO_0000213070"
FT REGION 164..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 254..257
FT /note="WXXF motif 1"
FT MOTIF 274..277
FT /note="WXXF motif 2"
FT COMPBIAS 164..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NC96"
SQ SEQUENCE 277 AA; 29792 MW; F8DCDABF95C838C0 CRC64;
MAAELEYESV LCVKPDVSVY RIPPRASNRG YRASDWKLDQ PDWTGRLRIT SKGKIAYIKL
EDKVSGELFA QAPVEQYPGI AVETVADSSR YFVIRIQDGT GRSAFIGIGF TDRGDAFDFN
VSLQDHFKWV KQETEISKES QEMDSRPKLD LGFKEGQTIK LSIGNITAKK GGTSKPRASG
TGGLSLLPPP PGGKVTIPPP SSSVAISNHV TPPPIPKSNH GSNDSDILLD LDSPAPVPTS
APAPAPASTS NDLWGDFSTA SSSVPNQAPQ PSNWVQF
