EPN4_MOUSE
ID EPN4_MOUSE Reviewed; 631 AA.
AC Q99KN9; Q8CFH4;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Clathrin interactor 1;
DE AltName: Full=Enthoprotin;
DE AltName: Full=Epsin-4;
DE AltName: Full=Epsin-related protein;
DE Short=EpsinR;
GN Name=Clint1; Synonyms=Enth, Epn4, Epnr, Kiaa0171;
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] (ISOFORM 2).
RC TISSUE=Embryonic intestine;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-631 (ISOFORM 1).
RC 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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: 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99KN9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99KN9-2; Sequence=VSP_009162, VSP_009163, VSP_009164;
CC -!- SIMILARITY: Belongs to the epsin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41396.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB093212; BAC41396.1; ALT_INIT; mRNA.
DR EMBL; BC004080; AAH04080.1; -; mRNA.
DR AlphaFoldDB; Q99KN9; -.
DR SMR; Q99KN9; -.
DR STRING; 10090.ENSMUSP00000104883; -.
DR iPTMnet; Q99KN9; -.
DR PhosphoSitePlus; Q99KN9; -.
DR SwissPalm; Q99KN9; -.
DR EPD; Q99KN9; -.
DR jPOST; Q99KN9; -.
DR MaxQB; Q99KN9; -.
DR PaxDb; Q99KN9; -.
DR PeptideAtlas; Q99KN9; -.
DR PRIDE; Q99KN9; -.
DR ProteomicsDB; 275637; -. [Q99KN9-1]
DR ProteomicsDB; 275638; -. [Q99KN9-2]
DR UCSC; uc007inr.1; mouse. [Q99KN9-2]
DR MGI; MGI:2144243; Clint1.
DR eggNOG; KOG2057; Eukaryota.
DR InParanoid; Q99KN9; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR ChiTaRS; Clint1; mouse.
DR PRO; PR:Q99KN9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99KN9; protein.
DR GO; GO:0030125; C:clathrin vesicle coat; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030276; F:clathrin binding; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Endocytosis;
KW Lipid-binding; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..631
FT /note="Clathrin interactor 1"
FT /id="PRO_0000074522"
FT DOMAIN 24..157
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 60..62
FT /note="Interaction with VTI1B"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT REGION 102..104
FT /note="Interaction with VTI1B"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT REGION 150..161
FT /note="Interaction with VTI1B"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT REGION 227..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 37
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 75
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 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 316
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT MOD_RES 630
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14677"
FT VAR_SEQ 346..370
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_009162"
FT VAR_SEQ 467..489
FT /note="NTDMVQKSASKTLPSTWSDPSVN -> VSCLFPLGIGAYTSTRRSNSMMS
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_009163"
FT VAR_SEQ 490..631
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_009164"
SQ SEQUENCE 631 AA; 68513 MW; 370711BBCA59CC17 CRC64;
MLIFMYLYVC VCTCTCAFSL CSTNVVMNYS EIESKVREAT NDDPWGPSGQ LMGEIAKATF
MYEQFPELMN MLWSRMLKDN KKNWRRVYKS LLLLAYLIRN GSERVVTSAR EHIYDLRSLE
NYHFVDEHGK DQGINIRQKV KELVEFAQDD DRLREERKKA KKNKDKYVGV SSDSVGGFRY
NERYDPEPKS KWDEEWDKNK SAFPFSDKLG ELSDKIGSTI DDTISKFRRK DREDSPERCS
DSDEEKKARR GRSPKGEFKD EEETVTTKHI HITQATETTT TRHKRTANPS KTIDLGAAAH
YTGDKASPDQ NASTHTPQSS AKPSVPSSKS SGDLVDLFDG SSQSAGGSAD LFGGFADFGS
AAASGNFPSQ ATSGNGDFGD WSAFNQAPSG PVASGGELFG SAPQSAVELI SASQPALGPP
PAASNSADLF DLMGSSQATM TSSQSMNFSL MSTNTVGLGL PMSRSQNTDM VQKSASKTLP
STWSDPSVNI SLDNLLPGMQ PSKPQQPSLN TMIQQQNMQQ PLNVMTQSFG AVNLSSPSNM
LPVRPQTNPL LGGPMPMNMP GVMTGTMGMA PLGNSAGMSQ GMVGMNMNMG MSASGMGLSG
TMGMGMPSMA MPSGTVQPKQ DAFANFANFS K
