ARFRP_HUMAN
ID ARFRP_HUMAN Reviewed; 201 AA.
AC Q13795; A0A087WY13; B7ZKX7; E1P5J9; Q6IBQ0; V9GYH4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=ADP-ribosylation factor-related protein 1;
DE Short=ARF-related protein 1;
DE Short=ARP;
GN Name=ARFRP1; Synonyms=ARP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8530503; DOI=10.1074/jbc.270.51.30657;
RA Schuermann A., Massmann S., Joost H.-G.;
RT "ARP is a plasma membrane-associated Ras-related GTPase with remote
RT similarity to the family of ADP-ribosylation factors.";
RL J. Biol. Chem. 270:30657-30663(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10655513; DOI=10.1073/pnas.97.3.1230;
RA Bai C., Connolly B., Metzker M.L., Hilliard C.A., Liu X., Sandig V.,
RA Soderman A., Galloway S.M., Liu Q., Austin C.P., Caskey C.T.;
RT "Overexpression of M68/DcR3 in human gastrointestinal tract tumors
RT independent of gene amplification and its location in a four-gene
RT cluster.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1230-1235(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and 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).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SYS1.
RX PubMed=15077113; DOI=10.1038/ncb1120;
RA Behnia R., Panic B., Whyte J.R.C., Munro S.;
RT "Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal
RT acetylation and the membrane protein Sys1p.";
RL Nat. Cell Biol. 6:405-413(2004).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-108.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Trans-Golgi-associated GTPase that regulates protein sorting.
CC Controls the targeting of ARL1 and its effector to the trans-Golgi.
CC Required for the lipidation of chylomicrons in the intestine and
CC required for VLDL lipidation in the liver.
CC {ECO:0000250|UniProtKB:Q8BXL7}.
CC -!- SUBUNIT: Interacts with SYS1. {ECO:0000269|PubMed:15077113}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:15077113}.
CC Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q8BXL7}.
CC Note=Located in the trans-Golgi in the GTP-bound active state.
CC {ECO:0000250|UniProtKB:Q8BXL7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q13795-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13795-2; Sequence=VSP_043531;
CC Name=3;
CC IsoId=Q13795-3; Sequence=VSP_057570;
CC Name=4;
CC IsoId=Q13795-4; Sequence=VSP_057571, VSP_057572;
CC -!- TISSUE SPECIFICITY: Found in most tissues.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; X91504; CAA62804.1; -; mRNA.
DR EMBL; AF217796; AAF35246.1; -; Genomic_DNA.
DR EMBL; CR456752; CAG33033.1; -; mRNA.
DR EMBL; BT019624; AAV38430.1; -; mRNA.
DR EMBL; BT019663; AAV38469.1; -; mRNA.
DR EMBL; AL121845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF511326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75231.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75232.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75235.1; -; Genomic_DNA.
DR EMBL; BC092480; AAH92480.1; -; mRNA.
DR EMBL; BC093967; AAH93967.1; -; mRNA.
DR EMBL; BC143447; AAI43448.1; -; mRNA.
DR EMBL; BC143448; AAI43449.1; -; mRNA.
DR CCDS; CCDS13533.1; -. [Q13795-1]
DR CCDS; CCDS46630.1; -. [Q13795-2]
DR CCDS; CCDS68172.1; -. [Q13795-3]
DR CCDS; CCDS68173.1; -. [Q13795-4]
DR RefSeq; NP_001128230.1; NM_001134758.3. [Q13795-2]
DR RefSeq; NP_001254474.1; NM_001267545.2. [Q13795-4]
DR RefSeq; NP_001254475.1; NM_001267546.2. [Q13795-3]
DR RefSeq; NP_001254476.1; NM_001267547.2. [Q13795-1]
DR RefSeq; NP_001254477.1; NM_001267548.2. [Q13795-1]
DR RefSeq; NP_001254478.1; NM_001267549.2. [Q13795-2]
DR RefSeq; NP_003215.1; NM_003224.5. [Q13795-1]
DR RefSeq; XP_011526784.1; XM_011528482.2. [Q13795-1]
DR RefSeq; XP_011526785.1; XM_011528483.1. [Q13795-1]
DR RefSeq; XP_016883065.1; XM_017027576.1. [Q13795-1]
DR AlphaFoldDB; Q13795; -.
DR SMR; Q13795; -.
DR BioGRID; 115442; 8.
DR IntAct; Q13795; 1.
DR STRING; 9606.ENSP00000483486; -.
DR iPTMnet; Q13795; -.
DR PhosphoSitePlus; Q13795; -.
DR BioMuta; ARFRP1; -.
DR DMDM; 2492927; -.
DR EPD; Q13795; -.
DR jPOST; Q13795; -.
DR MassIVE; Q13795; -.
DR MaxQB; Q13795; -.
DR PaxDb; Q13795; -.
DR PeptideAtlas; Q13795; -.
DR PRIDE; Q13795; -.
DR ProteomicsDB; 59685; -. [Q13795-1]
DR ProteomicsDB; 59686; -. [Q13795-2]
DR Antibodypedia; 29845; 124 antibodies from 24 providers.
DR DNASU; 10139; -.
DR Ensembl; ENST00000607873.1; ENSP00000476756.1; ENSG00000101246.20. [Q13795-3]
DR Ensembl; ENST00000612157.4; ENSP00000479058.1; ENSG00000101246.20. [Q13795-2]
DR Ensembl; ENST00000612256.4; ENSP00000484109.1; ENSG00000101246.20. [Q13795-3]
DR Ensembl; ENST00000614942.4; ENSP00000483130.1; ENSG00000101246.20. [Q13795-4]
DR Ensembl; ENST00000618568.4; ENSP00000481446.1; ENSG00000101246.20. [Q13795-4]
DR Ensembl; ENST00000618838.4; ENSP00000479616.1; ENSG00000101246.20. [Q13795-1]
DR Ensembl; ENST00000619493.4; ENSP00000479940.1; ENSG00000101246.20. [Q13795-1]
DR Ensembl; ENST00000622789.5; ENSP00000483486.1; ENSG00000101246.20. [Q13795-1]
DR GeneID; 10139; -.
DR KEGG; hsa:10139; -.
DR MANE-Select; ENST00000622789.5; ENSP00000483486.1; NM_001267547.3; NP_001254476.1.
DR UCSC; uc032ppa.2; human.
DR UCSC; uc032ppb.2; human. [Q13795-1]
DR UCSC; uc032ppd.2; human.
DR CTD; 10139; -.
DR DisGeNET; 10139; -.
DR GeneCards; ARFRP1; -.
DR HGNC; HGNC:662; ARFRP1.
DR HPA; ENSG00000101246; Low tissue specificity.
DR MIM; 604699; gene.
DR neXtProt; NX_Q13795; -.
DR OpenTargets; ENSG00000101246; -.
DR PharmGKB; PA24946; -.
DR VEuPathDB; HostDB:ENSG00000101246; -.
DR eggNOG; KOG0076; Eukaryota.
DR GeneTree; ENSGT00940000156407; -.
DR HOGENOM; CLU_040729_7_2_1; -.
DR InParanoid; Q13795; -.
DR OMA; QCHGIIF; -.
DR OrthoDB; 1271528at2759; -.
DR PhylomeDB; Q13795; -.
DR TreeFam; TF105788; -.
DR PathwayCommons; Q13795; -.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; Q13795; -.
DR BioGRID-ORCS; 10139; 539 hits in 1078 CRISPR screens.
DR ChiTaRS; ARFRP1; human.
DR GeneWiki; ARFRP1; -.
DR GenomeRNAi; 10139; -.
DR Pharos; Q13795; Tbio.
DR PRO; PR:Q13795; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q13795; protein.
DR Bgee; ENSG00000101246; Expressed in type B pancreatic cell and 201 other tissues.
DR ExpressionAtlas; Q13795; baseline and differential.
DR Genevisible; Q13795; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0007369; P:gastrulation; IEA:Ensembl.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR Pfam; PF00025; Arf; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Golgi apparatus; GTP-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..201
FT /note="ADP-ribosylation factor-related protein 1"
FT /id="PRO_0000207487"
FT BINDING 24..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 134..137
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..47
FT /note="Missing (in isoform 3)"
FT /id="VSP_057570"
FT VAR_SEQ 116..121
FT /note="EKVVTS -> DVPLNP (in isoform 4)"
FT /id="VSP_057571"
FT VAR_SEQ 122..201
FT /note="Missing (in isoform 4)"
FT /id="VSP_057572"
FT VAR_SEQ 174..201
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043531"
FT VARIANT 108
FT /note="L -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036559"
SQ SEQUENCE 201 AA; 22614 MW; 8A75CF7A3B268158 CRC64;
MYTLLSGLYK YMFQKDEYCI LILGLDNAGK TTFLEQSKTR FNKNYKGMSL SKITTTVGLN
IGTVDVGKAR LMFWDLGGQE ELQSLWDKYY AECHGVIYVI DSTDEERLAE SKQAFEKVVT
SEALCGVPVL VLANKQDVET CLSIPDIKTA FSDCTSKIGR RDCLTQACSA LTGKGVREGI
EWMVKCVVRN VHRPPRQRDI T
