ARL5A_RAT
ID ARL5A_RAT Reviewed; 179 AA.
AC P51646; Q4V8N2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ADP-ribosylation factor-like protein 5A;
GN Name=Arl5a; Synonyms=Arl5;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Adipose tissue;
RX PubMed=8765741; DOI=10.1016/0167-4781(96)00081-4;
RA Breiner M., Schuermann A., Becker W., Joost H.-G.;
RT "Cloning of a novel member (ARL5) of the ARF-family of Ras-related
RT GTPases.";
RL Biochim. Biophys. Acta 1308:1-6(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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: Lacks ADP-ribosylation enhancing activity.
CC -!- TISSUE SPECIFICITY: Low amounts were found in most tissues examined
CC with highest levels in brain, intestine and thymus.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; X78604; CAA55338.1; -; mRNA.
DR EMBL; BC097294; AAH97294.1; -; mRNA.
DR PIR; S72161; S72161.
DR RefSeq; NP_446431.1; NM_053979.2.
DR AlphaFoldDB; P51646; -.
DR SMR; P51646; -.
DR STRING; 10116.ENSRNOP00000009181; -.
DR PhosphoSitePlus; P51646; -.
DR PaxDb; P51646; -.
DR Ensembl; ENSRNOT00000009181; ENSRNOP00000009181; ENSRNOG00000006839.
DR GeneID; 117050; -.
DR KEGG; rno:117050; -.
DR UCSC; RGD:621327; rat.
DR CTD; 26225; -.
DR RGD; 621327; Arl5a.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00940000154714; -.
DR HOGENOM; CLU_040729_9_1_1; -.
DR InParanoid; P51646; -.
DR OMA; IWRLFSH; -.
DR OrthoDB; 1417432at2759; -.
DR PhylomeDB; P51646; -.
DR TreeFam; TF105465; -.
DR PRO; PR:P51646; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000006839; Expressed in jejunum and 19 other tissues.
DR Genevisible; P51646; RN.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1903292; P:protein localization to Golgi membrane; ISO:RGD.
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 GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..179
FT /note="ADP-ribosylation factor-like protein 5A"
FT /id="PRO_0000207469"
FT BINDING 23..30
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 159
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 179 AA; 20714 MW; 518CCBCF928CB9D5 CRC64;
MGILFTRIWR LFNHQEHKVI IVGLDNAGKT TILYQFSMNE VVHTSPTIGS NVEEIVVNNT
RFLMWDIGGQ ESLRSSWNTY YTNTEFVIVV VDSTDRERIS VTREELYKML AHEDLRKAGL
LIFANKQDVK ECMTVAEISQ FLKLTSIKDH QWHIQACCAL TGEGLCQGLE WMMSRLKIR