ID   NECP1_PONAB             Reviewed;         275 AA.
AC   Q5R630; Q5R6A3;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 81.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Colocalizes
CC       with AP-2 at the plasma membrane. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NECAP family. {ECO:0000305}.
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DR   EMBL; CR860591; CAH92713.1; -; mRNA.
DR   EMBL; CR860669; CAH92786.1; -; mRNA.
DR   RefSeq; NP_001127586.1; NM_001134114.1.
DR   AlphaFoldDB; Q5R630; -.
DR   SMR; Q5R630; -.
DR   STRING; 9601.ENSPPYP00000004834; -.
DR   GeneID; 100174665; -.
DR   KEGG; pon:100174665; -.
DR   CTD; 25977; -.
DR   eggNOG; KOG2500; Eukaryota.
DR   HOGENOM; CLU_069884_1_1_1; -.
DR   InParanoid; Q5R630; -.
DR   OrthoDB; 1605812at2759; -.
DR   TreeFam; TF314482; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
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   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   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasmic vesicle; Endocytosis; Membrane; Methylation;
KW   Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT   CHAIN           1..275
FT                   /note="Adaptin ear-binding coat-associated protein 1"
FT                   /id="PRO_0000213069"
FT   REGION          166..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           252..255
FT                   /note="WXXF motif 1"
FT   MOTIF           272..275
FT                   /note="WXXF motif 2"
FT   COMPBIAS        242..275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         180
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC96"
FT   MOD_RES         211
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC96"
FT   CONFLICT        170
FT                   /note="E -> K (in Ref. 1; CAH92713)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   275 AA;  29664 MW;  3EEA36BEDEC22502 CRC64;
     MAAELEYESV LCVKPDVSVY RIPPRASNRG YRASDWKLDQ PDWTGRLRIT SKGKTAYIKL
     EDKVSGELFA QAPVEQYPGI AVETVTDSSR YFVIRIQDGT GRSAFIGIGF TDRGDAFDFN
     VSLQDHFKWV KQESEISKES QEMDARPKLD LGFKEGQTIK LSIGNITNKE GGASKPRTAR
     GGGLSLLPPP PGGKVTIPPP SSSVAISNHV TPPPIPKSNH GGSDADILLD LDSPAPVTTP
     APTPVSASND LWGDFSTASS SVPNQAPQPS NWVQF