RAB17_HUMAN
ID RAB17_HUMAN Reviewed; 212 AA.
AC Q9H0T7; Q53QV6; Q6IA73; Q6PJZ0; Q9BVU1; Q9H9U9;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Ras-related protein Rab-17;
GN Name=RAB17;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-19.
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, Eye, Ovary, 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 [7]
RP TISSUE SPECIFICITY, AND INDUCTION BY FORSKOLIN.
RX PubMed=21291502; DOI=10.1111/j.1600-0854.2011.01172.x;
RA Beaumont K.A., Hamilton N.A., Moores M.T., Brown D.L., Ohbayashi N.,
RA Cairncross O., Cook A.L., Smith A.G., Misaki R., Fukuda M., Taguchi T.,
RA Sturm R.A., Stow J.L.;
RT "The recycling endosome protein Rab17 regulates melanocytic filopodia
RT formation and melanosome trafficking.";
RL Traffic 12:627-643(2011).
RN [8]
RP FUNCTION IN CELL MIGRATION.
RX PubMed=22328529; DOI=10.1242/jcs.092916;
RA von Thun A., Birtwistle M., Kalna G., Grindlay J., Strachan D., Kolch W.,
RA von Kriegsheim A., Norman J.C.;
RT "ERK2 drives tumour cell migration in three-dimensional microenvironments
RT by suppressing expression of Rab17 and liprin-beta2.";
RL J. Cell Sci. 125:1465-1477(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: The small GTPases Rab are key regulators of intracellular
CC membrane trafficking, from the formation of transport vesicles to their
CC fusion with membranes. Rabs cycle between an inactive GDP-bound form
CC and an active GTP-bound form that is able to recruit to membranes
CC different set of downstream effectors directly responsible for vesicle
CC formation, movement, tethering and fusion. That Rab is involved in
CC transcytosis, the directed movement of endocytosed material through the
CC cell and its exocytosis from the plasma membrane at the opposite side.
CC Mainly observed in epithelial cells, transcytosis mediates for
CC instance, the transcellular transport of immunoglobulins from the
CC basolateral surface to the apical surface. Most probably controls
CC membrane trafficking through apical recycling endosomes in a post-
CC endocytic step of transcytosis. Required for melanosome transport and
CC release from melanocytes, it also regulates dendrite and dendritic
CC spine development (By similarity). May also play a role in cell
CC migration. {ECO:0000250, ECO:0000269|PubMed:22328529}.
CC -!- INTERACTION:
CC Q9H0T7; Q53S33: BOLA3; NbExp=3; IntAct=EBI-721615, EBI-12086950;
CC Q9H0T7; Q9H6J7: C11orf49; NbExp=3; IntAct=EBI-721615, EBI-721300;
CC Q9H0T7; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-721615, EBI-10175124;
CC Q9H0T7; P43355: MAGEA1; NbExp=3; IntAct=EBI-721615, EBI-740978;
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane
CC {ECO:0000250|UniProtKB:P35292}; Lipid-anchor {ECO:0000305}; Cytoplasmic
CC side {ECO:0000305}. Melanosome {ECO:0000250|UniProtKB:P35292}. Cell
CC projection, dendrite {ECO:0000250|UniProtKB:P35292}. Note=May also
CC localize at the basolateral and apical plasma membrane. In neurons,
CC localizes to the cell body and dendritic shaft and spine.
CC {ECO:0000250|UniProtKB:P35292}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0T7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0T7-2; Sequence=VSP_056400;
CC -!- TISSUE SPECIFICITY: Expressed in melanocytes (at protein level).
CC {ECO:0000269|PubMed:21291502}.
CC -!- INDUCTION: Up-regulated by forskolin probably through the transcription
CC factor MITF. {ECO:0000269|PubMed:21291502}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AL136645; CAB66580.1; -; mRNA.
DR EMBL; AK022600; BAB14121.1; -; mRNA.
DR EMBL; CR457282; CAG33563.1; -; mRNA.
DR EMBL; AC104667; AAY24047.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71118.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW71119.1; -; Genomic_DNA.
DR EMBL; BC000929; AAH00929.1; -; mRNA.
DR EMBL; BC050426; AAH50426.1; -; mRNA.
DR EMBL; BC007907; AAH07907.1; -; mRNA.
DR EMBL; BC009827; AAH09827.1; -; mRNA.
DR CCDS; CCDS2520.1; -. [Q9H0T7-1]
DR RefSeq; NP_071894.1; NM_022449.3. [Q9H0T7-1]
DR AlphaFoldDB; Q9H0T7; -.
DR SMR; Q9H0T7; -.
DR BioGRID; 122128; 39.
DR IntAct; Q9H0T7; 12.
DR STRING; 9606.ENSP00000264601; -.
DR iPTMnet; Q9H0T7; -.
DR PhosphoSitePlus; Q9H0T7; -.
DR BioMuta; RAB17; -.
DR DMDM; 37999892; -.
DR EPD; Q9H0T7; -.
DR jPOST; Q9H0T7; -.
DR MassIVE; Q9H0T7; -.
DR MaxQB; Q9H0T7; -.
DR PaxDb; Q9H0T7; -.
DR PeptideAtlas; Q9H0T7; -.
DR PRIDE; Q9H0T7; -.
DR ProteomicsDB; 67228; -.
DR ProteomicsDB; 80323; -. [Q9H0T7-1]
DR Antibodypedia; 34483; 281 antibodies from 31 providers.
DR DNASU; 64284; -.
DR Ensembl; ENST00000264601.8; ENSP00000264601.3; ENSG00000124839.13. [Q9H0T7-1]
DR Ensembl; ENST00000409822.1; ENSP00000386589.1; ENSG00000124839.13. [Q9H0T7-2]
DR GeneID; 64284; -.
DR KEGG; hsa:64284; -.
DR MANE-Select; ENST00000264601.8; ENSP00000264601.3; NM_022449.4; NP_071894.1.
DR UCSC; uc002vwz.3; human. [Q9H0T7-1]
DR CTD; 64284; -.
DR DisGeNET; 64284; -.
DR GeneCards; RAB17; -.
DR HGNC; HGNC:16523; RAB17.
DR HPA; ENSG00000124839; Tissue enhanced (intestine, liver).
DR MIM; 602206; gene.
DR neXtProt; NX_Q9H0T7; -.
DR OpenTargets; ENSG00000124839; -.
DR PharmGKB; PA34105; -.
DR VEuPathDB; HostDB:ENSG00000124839; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000161839; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; Q9H0T7; -.
DR OMA; YDISKRE; -.
DR OrthoDB; 1340129at2759; -.
DR PhylomeDB; Q9H0T7; -.
DR TreeFam; TF300199; -.
DR PathwayCommons; Q9H0T7; -.
DR Reactome; R-HSA-8873719; RAB geranylgeranylation.
DR SignaLink; Q9H0T7; -.
DR BioGRID-ORCS; 64284; 12 hits in 1065 CRISPR screens.
DR ChiTaRS; RAB17; human.
DR GeneWiki; RAB17; -.
DR GenomeRNAi; 64284; -.
DR Pharos; Q9H0T7; Tbio.
DR PRO; PR:Q9H0T7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H0T7; protein.
DR Bgee; ENSG00000124839; Expressed in right lobe of liver and 130 other tissues.
DR ExpressionAtlas; Q9H0T7; baseline and differential.
DR Genevisible; Q9H0T7; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0032401; P:establishment of melanosome localization; ISS:UniProtKB.
DR GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB.
DR GO; GO:0002415; P:immunoglobulin transcytosis in epithelial cells mediated by polymeric immunoglobulin receptor; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0032402; P:melanosome transport; ISS:UniProtKB.
DR GO; GO:0050773; P:regulation of dendrite development; ISS:UniProtKB.
DR GO; GO:0030100; P:regulation of endocytosis; IBA:GO_Central.
DR GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR GO; GO:0051963; P:regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0045056; P:transcytosis; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Endosome; GTP-binding; Lipoprotein;
KW Membrane; Nucleotide-binding; Phosphoprotein; Prenylation;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..212
FT /note="Ras-related protein Rab-17"
FT /id="PRO_0000121191"
FT MOTIF 47..55
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 73..77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 132..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35292"
FT LIPID 209
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 210
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056400"
FT VARIANT 19
FT /note="V -> A (in dbSNP:rs3751112)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_051711"
FT VARIANT 184
FT /note="S -> G (in dbSNP:rs34311889)"
FT /id="VAR_051712"
FT VARIANT 191
FT /note="L -> P (in dbSNP:rs2280289)"
FT /id="VAR_022102"
FT CONFLICT 157
FT /note="L -> P (in Ref. 1; CAB66580)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 212 AA; 23491 MW; 40E8CE5F445E5CF2 CRC64;
MAQAHRTPQP RAAPSQPRVF KLVLLGSGSV GKSSLALRYV KNDFKSILPT VGCAFFTKVV
DVGATSLKLE IWDTAGQEKY HSVCHLYFRG ANAALLVYDI TRKDSFLKAQ QWLKDLEEEL
HPGEVLVMLV GNKTDLSQER EVTFQEGKEF ADSQKLLFME TSAKLNHQVS EVFNTVAQEL
LQRSDEEGQA LRGDAAVALN KGPARQAKCC AH
