NECP2_MOUSE
ID NECP2_MOUSE Reviewed; 266 AA.
AC Q9D1J1; Q3U1M1; Q9CV41;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Adaptin ear-binding coat-associated protein 2;
DE AltName: Full=NECAP endocytosis-associated protein 2;
DE Short=NECAP-2;
GN Name=Necap2;
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 [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Tongue;
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].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [4]
RP INTERACTION WITH GGA1; GGA2; GGA3 AND AP1G1.
RX PubMed=14665628; DOI=10.1074/jbc.m311873200;
RA Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S.;
RT "Definition of the consensus motif recognized by gamma-adaptin ear
RT domains.";
RL J. Biol. Chem. 279:8018-8028(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC 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: 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. {ECO:0000269|PubMed:14665628}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC membrane {ECO:0000269|PubMed:14555962}. Cell membrane
CC {ECO:0000269|PubMed:14555962}. Note=Colocalizes with AP-2 at the plasma
CC membrane.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC skeletal muscles and testis (at protein level).
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 -!- SIMILARITY: Belongs to the NECAP family. {ECO:0000305}.
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DR EMBL; BK000657; DAA01434.1; -; mRNA.
DR EMBL; AK003463; BAB22803.1; -; mRNA.
DR EMBL; AK009714; BAB26458.1; -; mRNA.
DR EMBL; AK155871; BAE33474.1; -; mRNA.
DR EMBL; BC037069; AAH37069.1; -; mRNA.
DR CCDS; CCDS18862.1; -.
DR RefSeq; NP_079659.1; NM_025383.3.
DR PDB; 6OWO; EM; 3.20 A; N=1-266.
DR PDB; 6OXL; EM; 3.50 A; N=1-266.
DR PDBsum; 6OWO; -.
DR PDBsum; 6OXL; -.
DR AlphaFoldDB; Q9D1J1; -.
DR SMR; Q9D1J1; -.
DR BioGRID; 211250; 5.
DR IntAct; Q9D1J1; 6.
DR MINT; Q9D1J1; -.
DR STRING; 10090.ENSMUSP00000030760; -.
DR iPTMnet; Q9D1J1; -.
DR PhosphoSitePlus; Q9D1J1; -.
DR EPD; Q9D1J1; -.
DR jPOST; Q9D1J1; -.
DR MaxQB; Q9D1J1; -.
DR PaxDb; Q9D1J1; -.
DR PRIDE; Q9D1J1; -.
DR ProteomicsDB; 252801; -.
DR Antibodypedia; 29202; 64 antibodies from 22 providers.
DR DNASU; 66147; -.
DR Ensembl; ENSMUST00000030760; ENSMUSP00000030760; ENSMUSG00000028923.
DR GeneID; 66147; -.
DR KEGG; mmu:66147; -.
DR UCSC; uc008vnu.2; mouse.
DR CTD; 55707; -.
DR MGI; MGI:1913397; Necap2.
DR VEuPathDB; HostDB:ENSMUSG00000028923; -.
DR eggNOG; KOG2500; Eukaryota.
DR GeneTree; ENSGT00390000009359; -.
DR HOGENOM; CLU_069884_1_0_1; -.
DR InParanoid; Q9D1J1; -.
DR OMA; NEGHRAQ; -.
DR OrthoDB; 1605812at2759; -.
DR PhylomeDB; Q9D1J1; -.
DR TreeFam; TF314482; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 66147; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Necap2; mouse.
DR PRO; PR:Q9D1J1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D1J1; protein.
DR Bgee; ENSMUSG00000028923; Expressed in stroma of bone marrow and 253 other tissues.
DR ExpressionAtlas; Q9D1J1; baseline and differential.
DR Genevisible; Q9D1J1; MM.
DR GO; GO:0030125; C:clathrin vesicle coat; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
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 3D-structure; Cell membrane; Cytoplasmic vesicle; Endocytosis; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..266
FT /note="Adaptin ear-binding coat-associated protein 2"
FT /id="PRO_0000213072"
FT REGION 165..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 243..246
FT /note="WXXF motif 1"
FT MOTIF 263..266
FT /note="WXXF motif 2"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT STRAND 8..19
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6OXL"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:6OWO"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:6OWO"
FT HELIX 112..136
FT /evidence="ECO:0007829|PDB:6OWO"
SQ SEQUENCE 266 AA; 28598 MW; 8687FFFF9DD901BD CRC64;
MEESEYESVL CVKPEVHVYR IPPRATNRGY RASEWQLDQP SWSGRLRITA KGKVAYIKLE
DRTSGELFAQ APVDQFPGTA VESVTDSSRY FVIRIEDGNG RRAFIGLGFG DRGDAFDFNV
ALQDHFKWVK QQCEFAKQAQ NPDEGPKLDL GFKDGQTIKI NIANMRKKEG AAGTPRARPT
SAGGLSLLPP PPGGKSSTVI PPSGEQLSVG GSLVQPAVVS GSGGATELWP QSKPAAAATA
DIWGDFTKST GSPSSQSQPG TGWVQF
