EPN4_BOVIN
ID EPN4_BOVIN Reviewed; 643 AA.
AC A7Z035;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Clathrin interactor 1;
DE AltName: Full=Epsin-4;
GN Name=CLINT1; Synonyms=EPN4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds to membranes enriched in phosphatidylinositol 4,5-
CC bisphosphate (PtdIns(4,5)P2). May have a role in transport via
CC clathrin-coated vesicles from the trans-Golgi network to endosomes.
CC Stimulates clathrin assembly (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds clathrin heavy chain and AP-2 (By similarity). Interacts
CC with VTI1B (By similarity). Interacts with GGA2 (via GAE domain) (By
CC similarity). Interacts with AP1G1 (via GAE domain) (By similarity).
CC Interacts with AP1G2 (via GAE domain) (By similarity).
CC {ECO:0000250|UniProtKB:Q14677}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00243};
CC Peripheral membrane protein {ECO:0000250}. Cytoplasmic vesicle,
CC clathrin-coated vesicle {ECO:0000250}. Note=Found throughout the cell,
CC with the exception of the cell surface. Concentrated in the perinuclear
CC region and associated with clathrin-coated vesicles close to the trans-
CC Golgi network (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
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DR EMBL; BC153233; AAI53234.1; -; mRNA.
DR RefSeq; NP_001098887.1; NM_001105417.1.
DR AlphaFoldDB; A7Z035; -.
DR SMR; A7Z035; -.
DR STRING; 9913.ENSBTAP00000021559; -.
DR PaxDb; A7Z035; -.
DR PeptideAtlas; A7Z035; -.
DR PRIDE; A7Z035; -.
DR Ensembl; ENSBTAT00000021559; ENSBTAP00000021559; ENSBTAG00000016199.
DR GeneID; 538540; -.
DR KEGG; bta:538540; -.
DR CTD; 9685; -.
DR VEuPathDB; HostDB:ENSBTAG00000016199; -.
DR VGNC; VGNC:27443; CLINT1.
DR eggNOG; KOG2057; Eukaryota.
DR GeneTree; ENSGT00940000155650; -.
DR HOGENOM; CLU_032178_1_0_1; -.
DR InParanoid; A7Z035; -.
DR OMA; AHYTGEK; -.
DR OrthoDB; 1263849at2759; -.
DR TreeFam; TF313361; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000016199; Expressed in abomasum and 105 other tissues.
DR ExpressionAtlas; A7Z035; baseline and differential.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005798; C:Golgi-associated vesicle; TAS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; TAS:BHF-UCL.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR030544; CLINT1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR PANTHER; PTHR12276:SF83; PTHR12276:SF83; 1.
DR Pfam; PF01417; ENTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; Endocytosis; Lipid-binding; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..643
FT /note="Clathrin interactor 1"
FT /id="PRO_0000328493"
FT DOMAIN 16..149
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 52..54
FT /note="Interaction with VTI1B"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT REGION 94..96
FT /note="Interaction with VTI1B"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT REGION 142..153
FT /note="Interaction with VTI1B"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT REGION 219..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KN9"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KN9"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 308
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
SQ SEQUENCE 643 AA; 70522 MW; AD3C958C0DE96638 CRC64;
MLNMWKVREL VDKATNVVMN YSEIESKVRE ATNDDPWGPS GQLMGEIAKA TFMYEQFPEL
MNMLWSRMLK DNKKNWRRVY KSLLLLAYLI RNGSERVVTS AREHIYDLRS LENYHFVDEH
GKDQGINIRQ KVKELVEFAQ DDDRLREERK KAKKNKDKYV GVSSDSVGGF RYSERYDPEP
KSKWDEEWDK NKSAFPFSDK LGELSDKIGS TIDDTISKFR RKDREDSPER CSDSDEEKKA
RRGRSPKGEF KDEEETVTTK HIHITQATET TTTRHKRTAN PSKTIDLGAA AHYTGDKASP
DQNASTHTPQ SSLKTSVPSS KSSGDLVDLF DGTSQSTGGS ADLFGGFADF GSAAASGNFP
SQVTATSGNG DFGDWSAFNQ APSVPVAASG ELFGSASQPA VELVSSSQPA LGPPPAASNS
SDLFDLMGSS QATMTSSQSM NFSMMSTNTV GLGLPMSRSQ PLQNVSTVLQ KPNPLYNQNT
DMVQKSVSKT LPSTWSDPSV NISLDNLLPG MQPSKPQQPS LNTMIQQQNM QQPMNMMTQS
FGAVNLSSPS NMLPVRPQTN PLMGGPMPMS MPNVMTGTMG MAPLGNSPMM NQSMMGMNMN
IGMSTTGMGL TGTMGMGMPN LAMTSGTMQP KQDAFANFAN FSK
