AP4AT_RAT
ID AP4AT_RAT Reviewed; 569 AA.
AC G3V8Y7; Q5EB78;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=AP-4 complex accessory subunit Tepsin {ECO:0000305};
DE AltName: Full=ENTH domain-containing protein 2 {ECO:0000312|RGD:1307410};
DE AltName: Full=Tetra-epsin {ECO:0000303|PubMed:22472443};
GN Name=Tepsin {ECO:0000303|PubMed:22472443, ECO:0000312|RGD:1307410};
GN Synonyms=Enthd2 {ECO:0000312|RGD:1307410};
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].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 332-569.
RC TISSUE=Brain;
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 SUBCELLULAR LOCATION.
RX PubMed=22472443; DOI=10.1083/jcb.201111049;
RA Borner G.H., Antrobus R., Hirst J., Bhumbra G.S., Kozik P., Jackson L.P.,
RA Sahlender D.A., Robinson M.S.;
RT "Multivariate proteomic profiling identifies novel accessory proteins of
RT coated vesicles.";
RL J. Cell Biol. 197:141-160(2012).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400, AND IDENTIFICATION BY
RP 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: Associates with the adapter-like complex 4 (AP-4) and may
CC therefore play a role in vesicular trafficking of proteins at the
CC trans-Golgi network. {ECO:0000250|UniProtKB:Q96N21}.
CC -!- SUBUNIT: Interacts with AP4B1 and AP4E1; the interaction is direct and
CC mediates the association of TEPSIN with the adapter-like complex 4 (AP-
CC 4), a heterotetramer composed of AP4B1, AP4E1, AP4M1 and AP4S1.
CC {ECO:0000250|UniProtKB:Q96N21}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:22472443}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96N21}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:22472443}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q96N21}. Note=Extensively colocalizes with AP-4
CC which mediates the recruitment of TEPSIN to the trans-Golgi network.
CC {ECO:0000269|PubMed:22472443}.
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DR EMBL; CH473948; EDM06814.1; -; Genomic_DNA.
DR EMBL; BC089956; AAH89956.1; -; mRNA.
DR RefSeq; NP_001094199.1; NM_001100729.1.
DR AlphaFoldDB; G3V8Y7; -.
DR SMR; G3V8Y7; -.
DR STRING; 10116.ENSRNOP00000031142; -.
DR iPTMnet; G3V8Y7; -.
DR PhosphoSitePlus; G3V8Y7; -.
DR PaxDb; G3V8Y7; -.
DR PRIDE; G3V8Y7; -.
DR GeneID; 360673; -.
DR KEGG; rno:360673; -.
DR CTD; 146705; -.
DR RGD; 1307410; Tepsin.
DR VEuPathDB; HostDB:ENSRNOG00000028161; -.
DR eggNOG; ENOG502QV38; Eukaryota.
DR HOGENOM; CLU_030958_0_0_1; -.
DR InParanoid; G3V8Y7; -.
DR OMA; SHCLLEY; -.
DR OrthoDB; 433095at2759; -.
DR TreeFam; TF331354; -.
DR PRO; PR:G3V8Y7; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000028161; Expressed in pancreas and 20 other tissues.
DR Genevisible; G3V8Y7; RN.
DR GO; GO:0030662; C:coated vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0031312; C:extrinsic component of organelle membrane; ISO:RGD.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:RGD.
DR CDD; cd03572; ENTH_like_Tepsin; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR035802; ENTH/VHS_tepsin.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR039273; TEPSIN.
DR PANTHER; PTHR21514; PTHR21514; 1.
DR Pfam; PF01417; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..569
FT /note="AP-4 complex accessory subunit Tepsin"
FT /id="PRO_0000418126"
FT DOMAIN 8..141
FT /note="ENTH"
FT REGION 196..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..535
FT /note="Interaction with AP4B1"
FT /evidence="ECO:0000250|UniProtKB:Q96N21"
FT REGION 559..569
FT /note="Interaction with AP4E1"
FT /evidence="ECO:0000250|UniProtKB:Q96N21"
FT COMPBIAS 257..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 569 AA; 60281 MW; BCFE523992D97CCA CRC64;
MAAVPPLRDR LSFLHRLPIL LKGTSDDDIP CPGYLFEEIA KISHESLGSS QCLLEYLLNR
LDSSSGHVKL KVLKILLYLC SHGSSSFMLI LRRNSALIQE ATAFAGPPDP LHGNSLYQKV
RAAAQDLGST LFSDALPQPP SQPPQILPPA GMGAQARPHS ALQGFGYTKE SSRTGSAGET
FLSTIQRAAE VVVNAVRPGP DNPCTKGPLP HGDAYQPAVT PSASHTHPNP GNLLPAAIQG
TRAVKHQPGQ AGGGWDEMDS SPSSQNSSCT SNLSRASDSV SRSGSDSHSG ASREPGDLAE
RAEGMAPNDC QQELNLVRTV TQGPRVFLSR EETQHFIKEC GLLNCEAVLE LLLQQLVGTS
ECEQMRALCA IASFGSADLL PQEHILLLCR QQLQELGAGS PGPVTNKATK ILRHLEASCG
QQFPTLRPCA QPNSAAAVVG PADLLTSPVP PPGSQVFLQP LSSTAVVPRS PVPTPSPDTL
PPALQDPGEL RTQLVCSSEP GTGSEQRLEN TDTPKDSSSP CPWSPNSLFA GMELVACTRL
PCPSFQADLQ KVTTEPPVSE PSAFAFLNM
