ARL4C_MOUSE
ID ARL4C_MOUSE Reviewed; 192 AA.
AC P61208;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ADP-ribosylation factor-like protein 4C;
DE AltName: Full=ADP-ribosylation factor-like 7;
GN Name=Arl4c; Synonyms=Arl7;
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 [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10462049; DOI=10.1016/s0014-5793(99)00759-0;
RA Jacobs S., Schilf C., Fliegert F., Koling S., Weber Y., Schurmann A.,
RA Joost H.-G.;
RT "ADP-ribosylation factor (ARF)-like 4, 6, and 7 represent a subgroup of the
RT ARF family characterization by rapid nucleotide exchange and a nuclear
RT localization signal.";
RL FEBS Lett. 456:384-388(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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).
CC -!- FUNCTION: Small GTP-binding protein which cycles between an inactive
CC GDP-bound and an active GTP-bound form, and the rate of cycling is
CC regulated by guanine nucleotide exchange factors (GEF) and GTPase-
CC activating proteins (GAP). GTP-binding protein that does not act as an
CC allosteric activator of the cholera toxin catalytic subunit. May be
CC involved in transport between a perinuclear compartment and the plasma
CC membrane, apparently linked to the ABCA1-mediated cholesterol secretion
CC pathway. Recruits CYTH1, CYTH2, CYTH3 and CYTH4 to the plasma membrane
CC in the GDP-bound form. Regulates the microtubule-dependent
CC intracellular vesicular transport from early endosome to recycling
CC endosome process (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CYTH2. Interacts with alpha tubulin;
CC interaction is independent on the ARL4C GTP or GDP binding status (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, filopodium {ECO:0000250}. Cell
CC membrane {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; AJ623276; CAF22225.1; -; Genomic_DNA.
DR EMBL; AK080335; BAC37882.1; -; mRNA.
DR EMBL; AK080380; BAC37900.1; -; mRNA.
DR EMBL; BC055769; AAH55769.1; -; mRNA.
DR CCDS; CCDS15146.1; -.
DR RefSeq; NP_796279.2; NM_177305.4.
DR AlphaFoldDB; P61208; -.
DR SMR; P61208; -.
DR BioGRID; 236437; 1.
DR STRING; 10090.ENSMUSP00000124344; -.
DR PhosphoSitePlus; P61208; -.
DR EPD; P61208; -.
DR MaxQB; P61208; -.
DR PaxDb; P61208; -.
DR PeptideAtlas; P61208; -.
DR PRIDE; P61208; -.
DR ProteomicsDB; 265103; -.
DR Antibodypedia; 34460; 92 antibodies from 20 providers.
DR DNASU; 320982; -.
DR Ensembl; ENSMUST00000051236; ENSMUSP00000057085; ENSMUSG00000049866.
DR Ensembl; ENSMUST00000159814; ENSMUSP00000124344; ENSMUSG00000049866.
DR Ensembl; ENSMUST00000187810; ENSMUSP00000139499; ENSMUSG00000049866.
DR GeneID; 320982; -.
DR KEGG; mmu:320982; -.
DR UCSC; uc007byt.1; mouse.
DR CTD; 10123; -.
DR MGI; MGI:2445172; Arl4c.
DR VEuPathDB; HostDB:ENSMUSG00000049866; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000160639; -.
DR HOGENOM; CLU_040729_9_2_1; -.
DR InParanoid; P61208; -.
DR OMA; RVQPACA; -.
DR OrthoDB; 1457094at2759; -.
DR PhylomeDB; P61208; -.
DR TreeFam; TF105464; -.
DR BioGRID-ORCS; 320982; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Arl4c; mouse.
DR PRO; PR:P61208; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P61208; protein.
DR Bgee; ENSMUSG00000049866; Expressed in vestibular membrane of cochlear duct and 228 other tissues.
DR Genevisible; P61208; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cytoplasm; GTP-binding; Lipoprotein;
KW Membrane; Myristate; Nucleotide-binding; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..192
FT /note="ADP-ribosylation factor-like protein 4C"
FT /id="PRO_0000207463"
FT BINDING 20..27
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 68..72
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 127..130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 192 AA; 21487 MW; 389BD49CF9E6D10D CRC64;
MGNISSNISA FQSLHIVMLG LDSAGKTTVL YRLKFNEFVN TVPTIGFNTE KIKLSNGTAK
GISCHFWDVG GQEKLRPLWK SYSRCTDGII YVVDSVDVDR LEEAKTELHK VTKFAENQGT
PLLVIANKQD LPKSLPVAEI EKQLALHELI PATTYHVQPA CAIIGEGLTE GMDKLYEMIL
KRRKSLKQKK KR
