AL14E_RAT
ID AL14E_RAT Reviewed; 276 AA.
AC Q5FVK8;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=ARL14 effector protein;
DE AltName: Full=ARF7 effector protein;
GN Name=Arl14ep; Synonyms=Arf7ep;
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 MRNA].
RC TISSUE=Ovary;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, 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: Through its interaction with ARL14 and MYO1E, may connect MHC
CC class II-containing cytoplasmic vesicles to the actin network and hence
CC controls the movement of these vesicles along the actin cytoskeleton in
CC dendritic cells. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ARL14 and MYO1E. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; BC089920; AAH89920.1; -; mRNA.
DR RefSeq; NP_001014067.1; NM_001014045.1.
DR RefSeq; XP_008760314.1; XM_008762092.2.
DR AlphaFoldDB; Q5FVK8; -.
DR STRING; 10116.ENSRNOP00000006481; -.
DR iPTMnet; Q5FVK8; -.
DR PhosphoSitePlus; Q5FVK8; -.
DR PaxDb; Q5FVK8; -.
DR Ensembl; ENSRNOT00000006481; ENSRNOP00000006481; ENSRNOG00000004891.
DR GeneID; 311279; -.
DR KEGG; rno:311279; -.
DR UCSC; RGD:1311463; rat.
DR CTD; 120534; -.
DR RGD; 1311463; Arl14ep.
DR eggNOG; KOG4850; Eukaryota.
DR GeneTree; ENSGT00940000156586; -.
DR HOGENOM; CLU_093502_0_0_1; -.
DR InParanoid; Q5FVK8; -.
DR OMA; CMQIING; -.
DR OrthoDB; 1056242at2759; -.
DR PhylomeDB; Q5FVK8; -.
DR TreeFam; TF333216; -.
DR PRO; PR:Q5FVK8; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000004891; Expressed in cerebellum and 19 other tissues.
DR Genevisible; Q5FVK8; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR InterPro; IPR029264; ARF7EP_C.
DR InterPro; IPR026515; ARL14EP.
DR PANTHER; PTHR46536; PTHR46536; 1.
DR Pfam; PF14949; ARF7EP_C; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..276
FT /note="ARL14 effector protein"
FT /id="PRO_0000251894"
FT REGION 159..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N8R7"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N8R7"
SQ SEQUENCE 276 AA; 31112 MW; A79E194DF5DED2AA CRC64;
MDPCSVGVQL RTTHDCHKTF YTRHTGFKTL KELSSNDMLL LQLRTGMTLS GNNTICLHHV
KIYIERFEEL QKSCCDPFNI HKKLAKKNLH VIDLDDATFL SAKFGRQLVP GWKLCPKCTQ
IINGSVDVDS DDRQRRKPES DGRTAKALRS LQFTNPGKQT EFAPESGKRE KRKLTKNASA
SSDRQIIPAK SKVYDSQGLL IFSGMDLCDC LDEDCLGCFY ACPTCGSTKC GAECRCDRKW
LYEQIEIEGG EIIHNKHAGK AYGLLSPCHP YDILQK