ID AR13B_HUMAN Reviewed; 428 AA. AC Q3SXY8; D3DN29; G3V1S8; Q504W8; Q8TCL5; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 27-MAR-2024, entry version 150. DE RecName: Full=ADP-ribosylation factor-like protein 13B; DE AltName: Full=ADP-ribosylation factor-like protein 2-like 1; DE Short=ARL2-like protein 1; GN Name=ARL13B; Synonyms=ARL2L1; 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 3). RC TISSUE=Amygdala; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC 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). RN [5] RP IDENTIFICATION. RX PubMed=15314642; DOI=10.1038/ng1414; RA Fan Y., Esmail M.A., Ansley S.J., Blacque O.E., Boroevich K., Ross A.J., RA Moore S.J., Badano J.L., May-Simera H., Compton D.S., Green J.S., RA Lewis R.A., van Haelst M.M., Parfrey P.S., Baillie D.L., Beales P.L., RA Katsanis N., Davidson W.S., Leroux M.R.; RT "Mutations in a member of the Ras superfamily of small GTP-binding proteins RT causes Bardet-Biedl syndrome."; RL Nat. Genet. 36:989-993(2004). RN [6] RP SUBCELLULAR LOCATION, GTP-BINDING, AND MUTAGENESIS OF THR-35 AND ASN-130. RX PubMed=18554500; DOI=10.1016/j.bbrc.2008.06.001; RA Hori Y., Kobayashi T., Kikko Y., Kontani K., Katada T.; RT "Domain architecture of the atypical Arf-family GTPase Arl13b involved in RT cilia formation."; RL Biochem. Biophys. Res. Commun. 373:119-124(2008). RN [7] RP INTERACTION WITH CIMAP3. RX PubMed=20643351; DOI=10.1016/j.devcel.2010.06.005; RA Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., RA Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.; RT "Pitchfork regulates primary cilia disassembly and left-right asymmetry."; RL Dev. Cell 19:66-77(2010). RN [8] RP SUMOYLATION AT LYS-329, AND MUTAGENESIS OF LYS-231; LYS-270; LYS-275; RP LYS-276; LYS-279 AND LYS-329. RX PubMed=23128241; DOI=10.1083/jcb.201203150; RA Li Y., Zhang Q., Wei Q., Zhang Y., Ling K., Hu J.; RT "SUMOylation of the small GTPase ARL-13 promotes ciliary targeting of RT sensory receptors."; RL J. Cell Biol. 199:589-598(2012). RN [9] RP INTERACTION WITH IFT46 AND IFT74. RX PubMed=24339792; DOI=10.1371/journal.pgen.1003977; RA Cevik S., Sanders A.A., Van Wijk E., Boldt K., Clarke L., van Reeuwijk J., RA Hori Y., Horn N., Hetterschijt L., Wdowicz A., Mullins A., Kida K., RA Kaplan O.I., van Beersum S.E., Man Wu K., Letteboer S.J., Mans D.A., RA Katada T., Kontani K., Ueffing M., Roepman R., Kremer H., Blacque O.E.; RT "Active transport and diffusion barriers restrict Joubert syndrome- RT associated ARL13B/ARL-13 to an inv-like ciliary membrane subdomain."; RL PLoS Genet. 9:E1003977-E1003977(2013). RN [10] RP FUNCTION. RX PubMed=23150559; DOI=10.1073/pnas.1210916109; RA Humbert M.C., Weihbrecht K., Searby C.C., Li Y., Pope R.M., Sheffield V.C., RA Seo S.; RT "ARL13B, PDE6D, and CEP164 form a functional network for INPP5E ciliary RT targeting."; RL Proc. Natl. Acad. Sci. U.S.A. 109:19691-19696(2012). RN [11] RP POSSIBLE FUNCTION. RX PubMed=23223633; DOI=10.1073/pnas.1218272110; RA Barral D.C., Garg S., Casalou C., Watts G.F., Sandoval J.L., Ramalho J.S., RA Hsu V.W., Brenner M.B.; RT "Arl13b regulates endocytic recycling traffic."; RL Proc. Natl. Acad. Sci. U.S.A. 109:21354-21359(2012). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=24120134; DOI=10.1016/j.cell.2013.08.060; RA Paridaen J.T., Wilsch-Brauninger M., Huttner W.B.; RT "Asymmetric inheritance of centrosome-associated primary cilium membrane RT directs ciliogenesis after cell division."; RL Cell 155:333-344(2013). RN [13] RP INVOLVEMENT IN JBTS8, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT RP JBTS8 CYS-86, AND CHARACTERIZATION OF VARIANT JBTS8 CYS-86. RX PubMed=25138100; DOI=10.1038/ejhg.2014.156; RA Thomas S., Cantagrel V., Mariani L., Serre V., Lee J.E., Elkhartoufi N., RA de Lonlay P., Desguerre I., Munnich A., Boddaert N., Lyonnet S., RA Vekemans M., Lisgo S.N., Caspary T., Gleeson J., Attie-Bitach T.; RT "Identification of a novel ARL13B variant in a Joubert syndrome-affected RT patient with retinal impairment and obesity."; RL Eur. J. Hum. Genet. 23:621-627(2015). RN [14] RP VARIANTS JBTS8 GLN-79 AND CYS-200, AND CHARACTERIZATION OF VARIANT JBTS8 RP GLN-79. RX PubMed=18674751; DOI=10.1016/j.ajhg.2008.06.023; RG The international Joubert syndrome related disorders (JSRD) study group; RA Cantagrel V., Silhavy J.L., Bielas S.L., Swistun D., Marsh S.E., RA Bertrand J.Y., Audollent S., Attie-Bitach T., Holden K.R., Dobyns W.B., RA Traver D., Al-Gazali L., Ali B.R., Lindner T.H., Caspary T., Otto E.A., RA Hildebrandt F., Glass I.A., Logan C.V., Johnson C.A., Bennett C., RA Brancati F., Valente E.M., Woods C.G., Gleeson J.G.; RT "Mutations in the cilia gene ARL13B lead to the classical form of Joubert RT syndrome."; RL Am. J. Hum. Genet. 83:170-179(2008). RN [15] RP VARIANT LEU-390. RX PubMed=21068128; DOI=10.1136/jmg.2010.082552; RA Otto E.A., Ramaswami G., Janssen S., Chaki M., Allen S.J., Zhou W., RA Airik R., Hurd T.W., Ghosh A.K., Wolf M.T., Hoppe B., Neuhaus T.J., RA Bockenhauer D., Milford D.V., Soliman N.A., Antignac C., Saunier S., RA Johnson C.A., Hildebrandt F.; RT "Mutation analysis of 18 nephronophthisis associated ciliopathy disease RT genes using a DNA pooling and next generation sequencing strategy."; RL J. Med. Genet. 48:105-116(2011). CC -!- FUNCTION: Cilium-specific protein required to control the microtubule- CC based, ciliary axoneme structure. May act by maintaining the CC association between IFT subcomplexes A and B. Binds GTP but is not able CC to hydrolyze it; the GTPase activity remains unclear. Required to CC pattern the neural tube. Involved in cerebral cortex development: CC required for the initial formation of a polarized radial glial CC scaffold, the first step in the construction of the cerebral cortex, by CC regulating ciliary signaling. Regulates the migration and placement of CC postmitotic interneurons in the developing cerebral cortex. May CC regulate endocytic recycling traffic; however, additional evidence is CC required to confirm these data. {ECO:0000269|PubMed:23150559}. CC -!- SUBUNIT: Monomer (By similarity). Interacts with CIMAP3. Interacts with CC IFT complex B components IFT46 and IFT74 (By similarity) CC (PubMed:20643351, PubMed:24339792). Interacts with EXOC2; regulates CC ARL13B localization to the cilium membrane. CC {ECO:0000250|UniProtKB:Q640N2, ECO:0000269|PubMed:20643351, CC ECO:0000269|PubMed:24339792}. CC -!- INTERACTION: CC Q3SXY8; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-11343438, EBI-2876502; CC Q3SXY8; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-11343438, EBI-11957045; CC Q3SXY8; Q92685: ALG3; NbExp=3; IntAct=EBI-11343438, EBI-2848814; CC Q3SXY8; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-11343438, EBI-12109402; CC Q3SXY8; Q16853: AOC3; NbExp=3; IntAct=EBI-11343438, EBI-3921628; CC Q3SXY8; Q96PS8: AQP10; NbExp=3; IntAct=EBI-11343438, EBI-12820279; CC Q3SXY8; Q8NHY0: B4GALNT2; NbExp=3; IntAct=EBI-11343438, EBI-1042940; CC Q3SXY8; O95393: BMP10; NbExp=3; IntAct=EBI-11343438, EBI-3922513; CC Q3SXY8; Q12983: BNIP3; NbExp=3; IntAct=EBI-11343438, EBI-749464; CC Q3SXY8; Q6PL45-2: BRICD5; NbExp=3; IntAct=EBI-11343438, EBI-12244618; CC Q3SXY8; O14523: C2CD2L; NbExp=3; IntAct=EBI-11343438, EBI-12822627; CC Q3SXY8; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-11343438, EBI-12003442; CC Q3SXY8; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-11343438, EBI-9083477; CC Q3SXY8; P13236: CCL4; NbExp=3; IntAct=EBI-11343438, EBI-2873970; CC Q3SXY8; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-11343438, EBI-10271156; CC Q3SXY8; P48509: CD151; NbExp=3; IntAct=EBI-11343438, EBI-10210332; CC Q3SXY8; Q8IX05: CD302; NbExp=3; IntAct=EBI-11343438, EBI-14259393; CC Q3SXY8; P19397: CD53; NbExp=3; IntAct=EBI-11343438, EBI-6657396; CC Q3SXY8; O14735: CDIPT; NbExp=3; IntAct=EBI-11343438, EBI-358858; CC Q3SXY8; Q9BXR6: CFHR5; NbExp=3; IntAct=EBI-11343438, EBI-11579371; CC Q3SXY8; O14493: CLDN4; NbExp=3; IntAct=EBI-11343438, EBI-9316372; CC Q3SXY8; P56748: CLDN8; NbExp=3; IntAct=EBI-11343438, EBI-10215641; CC Q3SXY8; Q6UXB4: CLEC4G; NbExp=3; IntAct=EBI-11343438, EBI-2114729; CC Q3SXY8; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-11343438, EBI-11989440; CC Q3SXY8; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-11343438, EBI-6165897; CC Q3SXY8; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-11343438, EBI-7247651; CC Q3SXY8; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-11343438, EBI-2807956; CC Q3SXY8; Q4VAQ0: COL8A2; NbExp=3; IntAct=EBI-11343438, EBI-10241815; CC Q3SXY8; Q8N6G5: CSGALNACT2; NbExp=3; IntAct=EBI-11343438, EBI-10267100; CC Q3SXY8; O14569: CYB561D2; NbExp=3; IntAct=EBI-11343438, EBI-717654; CC Q3SXY8; Q15125: EBP; NbExp=3; IntAct=EBI-11343438, EBI-3915253; CC Q3SXY8; P54849: EMP1; NbExp=3; IntAct=EBI-11343438, EBI-4319440; CC Q3SXY8; O75355-2: ENTPD3; NbExp=3; IntAct=EBI-11343438, EBI-12279764; CC Q3SXY8; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-11343438, EBI-12142299; CC Q3SXY8; P37268: FDFT1; NbExp=3; IntAct=EBI-11343438, EBI-714550; CC Q3SXY8; Q14318: FKBP8; NbExp=3; IntAct=EBI-11343438, EBI-724839; CC Q3SXY8; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-11343438, EBI-714482; CC Q3SXY8; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-11343438, EBI-713304; CC Q3SXY8; Q05329: GAD2; NbExp=3; IntAct=EBI-11343438, EBI-9304251; CC Q3SXY8; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-11343438, EBI-11991950; CC Q3SXY8; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-11343438, EBI-6166686; CC Q3SXY8; P29033: GJB2; NbExp=3; IntAct=EBI-11343438, EBI-3905204; CC Q3SXY8; O14653: GOSR2; NbExp=3; IntAct=EBI-11343438, EBI-4401517; CC Q3SXY8; O60883: GPR37L1; NbExp=3; IntAct=EBI-11343438, EBI-2927498; CC Q3SXY8; P09601: HMOX1; NbExp=3; IntAct=EBI-11343438, EBI-2806151; CC Q3SXY8; P30519: HMOX2; NbExp=3; IntAct=EBI-11343438, EBI-712096; CC Q3SXY8; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-11343438, EBI-748420; CC Q3SXY8; O60725: ICMT; NbExp=3; IntAct=EBI-11343438, EBI-11721771; CC Q3SXY8; P11215: ITGAM; NbExp=3; IntAct=EBI-11343438, EBI-2568251; CC Q3SXY8; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-11343438, EBI-10266796; CC Q3SXY8; P63252: KCNJ2; NbExp=4; IntAct=EBI-11343438, EBI-703457; CC Q3SXY8; Q96E93: KLRG1; NbExp=3; IntAct=EBI-11343438, EBI-750770; CC Q3SXY8; O95214: LEPROTL1; NbExp=3; IntAct=EBI-11343438, EBI-750776; CC Q3SXY8; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-11343438, EBI-12033434; CC Q3SXY8; Q969L2: MAL2; NbExp=3; IntAct=EBI-11343438, EBI-944295; CC Q3SXY8; Q13021: MALL; NbExp=3; IntAct=EBI-11343438, EBI-750078; CC Q3SXY8; Q15546: MMD; NbExp=3; IntAct=EBI-11343438, EBI-17873222; CC Q3SXY8; O75425: MOSPD3; NbExp=3; IntAct=EBI-11343438, EBI-12179105; CC Q3SXY8; Q96DR8: MUCL1; NbExp=3; IntAct=EBI-11343438, EBI-9056153; CC Q3SXY8; A6NDP7: MYADML2; NbExp=3; IntAct=EBI-11343438, EBI-17641390; CC Q3SXY8; Q9UHE5: NAT8; NbExp=3; IntAct=EBI-11343438, EBI-2863634; CC Q3SXY8; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-11343438, EBI-10317425; CC Q3SXY8; Q16617: NKG7; NbExp=3; IntAct=EBI-11343438, EBI-3919611; CC Q3SXY8; Q8IXM6: NRM; NbExp=3; IntAct=EBI-11343438, EBI-10262547; CC Q3SXY8; Q9P0S3: ORMDL1; NbExp=3; IntAct=EBI-11343438, EBI-1054848; CC Q3SXY8; Q8N138: ORMDL3; NbExp=3; IntAct=EBI-11343438, EBI-721750; CC Q3SXY8; P09466: PAEP; NbExp=3; IntAct=EBI-11343438, EBI-465167; CC Q3SXY8; Q13113: PDZK1IP1; NbExp=3; IntAct=EBI-11343438, EBI-716063; CC Q3SXY8; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-11343438, EBI-12092917; CC Q3SXY8; P26678: PLN; NbExp=3; IntAct=EBI-11343438, EBI-692836; CC Q3SXY8; P60201-2: PLP1; NbExp=3; IntAct=EBI-11343438, EBI-12188331; CC Q3SXY8; Q5VZY2: PLPP4; NbExp=3; IntAct=EBI-11343438, EBI-10485931; CC Q3SXY8; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-11343438, EBI-12955265; CC Q3SXY8; Q01453: PMP22; NbExp=3; IntAct=EBI-11343438, EBI-2845982; CC Q3SXY8; Q59EV6: PPGB; NbExp=3; IntAct=EBI-11343438, EBI-14210385; CC Q3SXY8; A5D903: PRB1; NbExp=3; IntAct=EBI-11343438, EBI-10173935; CC Q3SXY8; P43378: PTPN9; NbExp=3; IntAct=EBI-11343438, EBI-742898; CC Q3SXY8; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-11343438, EBI-10244780; CC Q3SXY8; P29034: S100A2; NbExp=3; IntAct=EBI-11343438, EBI-752230; CC Q3SXY8; Q9NTJ5: SACM1L; NbExp=3; IntAct=EBI-11343438, EBI-3917235; CC Q3SXY8; Q9NTN9-2: SEMA4G; NbExp=3; IntAct=EBI-11343438, EBI-12913124; CC Q3SXY8; Q8WWT9: SLC13A3; NbExp=3; IntAct=EBI-11343438, EBI-12938720; CC Q3SXY8; P22732: SLC2A5; NbExp=3; IntAct=EBI-11343438, EBI-2825135; CC Q3SXY8; P78382: SLC35A1; NbExp=3; IntAct=EBI-11343438, EBI-12870360; CC Q3SXY8; P78383: SLC35B1; NbExp=3; IntAct=EBI-11343438, EBI-12147661; CC Q3SXY8; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-11343438, EBI-10314552; CC Q3SXY8; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-11343438, EBI-12898013; CC Q3SXY8; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-11343438, EBI-10226799; CC Q3SXY8; P16150: SPN; NbExp=3; IntAct=EBI-11343438, EBI-10049055; CC Q3SXY8; P0DN84: STRIT1; NbExp=3; IntAct=EBI-11343438, EBI-12200293; CC Q3SXY8; Q16623: STX1A; NbExp=3; IntAct=EBI-11343438, EBI-712466; CC Q3SXY8; O15400: STX7; NbExp=3; IntAct=EBI-11343438, EBI-3221827; CC Q3SXY8; Q9NZ01: TECR; NbExp=3; IntAct=EBI-11343438, EBI-2877718; CC Q3SXY8; Q9Y6I9: TEX264; NbExp=3; IntAct=EBI-11343438, EBI-10329860; CC Q3SXY8; P02786: TFRC; NbExp=3; IntAct=EBI-11343438, EBI-355727; CC Q3SXY8; Q9UPZ6: THSD7A; NbExp=3; IntAct=EBI-11343438, EBI-310962; CC Q3SXY8; Q9C0I4: THSD7B; NbExp=3; IntAct=EBI-11343438, EBI-311394; CC Q3SXY8; Q9BZW4: TM6SF2; NbExp=3; IntAct=EBI-11343438, EBI-13082040; CC Q3SXY8; P17152: TMEM11; NbExp=3; IntAct=EBI-11343438, EBI-723946; CC Q3SXY8; Q9BTD3: TMEM121; NbExp=3; IntAct=EBI-11343438, EBI-12155101; CC Q3SXY8; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-11343438, EBI-10694905; CC Q3SXY8; Q9P0S9: TMEM14C; NbExp=3; IntAct=EBI-11343438, EBI-2339195; CC Q3SXY8; Q14656: TMEM187; NbExp=3; IntAct=EBI-11343438, EBI-13046724; CC Q3SXY8; Q8WZ59: TMEM190; NbExp=3; IntAct=EBI-11343438, EBI-10278423; CC Q3SXY8; A2RU14: TMEM218; NbExp=3; IntAct=EBI-11343438, EBI-10173151; CC Q3SXY8; Q8NBD8: TMEM229B; NbExp=3; IntAct=EBI-11343438, EBI-12195227; CC Q3SXY8; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-11343438, EBI-11956809; CC Q3SXY8; Q9BTV4: TMEM43; NbExp=3; IntAct=EBI-11343438, EBI-721293; CC Q3SXY8; Q969K7: TMEM54; NbExp=3; IntAct=EBI-11343438, EBI-3922833; CC Q3SXY8; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-11343438, EBI-6656213; CC Q3SXY8; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-11343438, EBI-8649725; CC Q3SXY8; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-11343438, EBI-2548832; CC Q3SXY8; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-11343438, EBI-12111910; CC Q3SXY8; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-11343438, EBI-2820477; CC Q3SXY8; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-11343438, EBI-717441; CC Q3SXY8; Q9H2S6-2: TNMD; NbExp=3; IntAct=EBI-11343438, EBI-12003398; CC Q3SXY8; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-11343438, EBI-12195249; CC Q3SXY8; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-11343438, EBI-11988865; CC Q3SXY8; P23763-3: VAMP1; NbExp=3; IntAct=EBI-11343438, EBI-12097582; CC Q3SXY8; P63027: VAMP2; NbExp=3; IntAct=EBI-11343438, EBI-520113; CC Q3SXY8; Q15836: VAMP3; NbExp=3; IntAct=EBI-11343438, EBI-722343; CC Q3SXY8; O75379: VAMP4; NbExp=3; IntAct=EBI-11343438, EBI-744953; CC Q3SXY8; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-11343438, EBI-12190699; CC Q3SXY8; Q14508: WFDC2; NbExp=3; IntAct=EBI-11343438, EBI-723529; CC Q3SXY8; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-11343438, EBI-751210; CC Q3SXY8; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-11343438, EBI-12837904; CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane CC {ECO:0000269|PubMed:18554500, ECO:0000269|PubMed:24120134}; Lipid- CC anchor {ECO:0000269|PubMed:18554500, ECO:0000269|PubMed:24120134}. Cell CC projection, cilium {ECO:0000269|PubMed:25138100}. Note=Associates to CC the cilium membrane via palmitoylation. Localizes to proximal ciliary CC membranes, to an inversin-like subciliary membrane compartment, CC excluding the transition zone. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q3SXY8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3SXY8-2; Sequence=VSP_020733; CC Name=3; CC IsoId=Q3SXY8-3; Sequence=VSP_045421; CC -!- TISSUE SPECIFICITY: Expressed in the developing brain. CC {ECO:0000269|PubMed:25138100}. CC -!- PTM: Sumoylation is required for PKD2 entry into cilium. CC {ECO:0000269|PubMed:23128241}. CC -!- DISEASE: Joubert syndrome 8 (JBTS8) [MIM:612291]: A disorder presenting CC with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal CC breathing abnormalities and psychomotor delay. Neuroradiologically, it CC is characterized by cerebellar vermian hypoplasia/aplasia, thickened CC and reoriented superior cerebellar peduncles, and an abnormally large CC interpeduncular fossa, giving the appearance of a molar tooth on CC transaxial slices (molar tooth sign). Additional variable features CC include retinal dystrophy and renal disease. CC {ECO:0000269|PubMed:18674751, ECO:0000269|PubMed:25138100}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: Used as a ciliary marker because of its specific CC localization to microtubule doublets of the ciliary axoneme. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC {ECO:0000305}. CC -!- CAUTION: Was initially thought to form a homodimer (PubMed:18554500). CC However, 3D structure of C.reinhardtii ortholog showed that it is CC probably not the case. {ECO:0000305|PubMed:18554500}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL713789; CAD28544.2; -; mRNA. DR EMBL; AC117474; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC130896; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW79897.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79901.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79898.1; -; Genomic_DNA. DR EMBL; BC094725; AAH94725.1; -; mRNA. DR EMBL; BC104035; AAI04036.1; -; mRNA. DR EMBL; BC104036; AAI04037.1; -; mRNA. DR CCDS; CCDS2924.1; -. [Q3SXY8-2] DR CCDS; CCDS2925.1; -. [Q3SXY8-1] DR CCDS; CCDS54615.1; -. [Q3SXY8-3] DR RefSeq; NP_001167621.1; NM_001174150.1. [Q3SXY8-1] DR RefSeq; NP_001167622.1; NM_001174151.1. [Q3SXY8-3] DR RefSeq; NP_659433.2; NM_144996.3. [Q3SXY8-2] DR RefSeq; NP_878899.1; NM_182896.2. [Q3SXY8-1] DR RefSeq; XP_016861342.1; XM_017005853.1. [Q3SXY8-3] DR AlphaFoldDB; Q3SXY8; -. DR SMR; Q3SXY8; -. DR BioGRID; 128353; 303. DR IntAct; Q3SXY8; 149. DR MINT; Q3SXY8; -. DR STRING; 9606.ENSP00000377769; -. DR iPTMnet; Q3SXY8; -. DR PhosphoSitePlus; Q3SXY8; -. DR SwissPalm; Q3SXY8; -. DR BioMuta; ARL13B; -. DR DMDM; 115503786; -. DR EPD; Q3SXY8; -. DR jPOST; Q3SXY8; -. DR MassIVE; Q3SXY8; -. DR MaxQB; Q3SXY8; -. DR PaxDb; 9606-ENSP00000377769; -. DR PeptideAtlas; Q3SXY8; -. DR ProteomicsDB; 32429; -. DR ProteomicsDB; 61823; -. [Q3SXY8-1] DR ProteomicsDB; 61824; -. [Q3SXY8-2] DR Pumba; Q3SXY8; -. DR Antibodypedia; 32073; 151 antibodies from 28 providers. DR DNASU; 200894; -. DR Ensembl; ENST00000303097.11; ENSP00000306225.7; ENSG00000169379.17. [Q3SXY8-2] DR Ensembl; ENST00000394222.8; ENSP00000377769.3; ENSG00000169379.17. [Q3SXY8-1] DR Ensembl; ENST00000471138.5; ENSP00000420780.1; ENSG00000169379.17. [Q3SXY8-1] DR Ensembl; ENST00000535334.5; ENSP00000445145.1; ENSG00000169379.17. [Q3SXY8-3] DR GeneID; 200894; -. DR KEGG; hsa:200894; -. DR MANE-Select; ENST00000394222.8; ENSP00000377769.3; NM_001174150.2; NP_001167621.1. DR UCSC; uc003drc.4; human. [Q3SXY8-1] DR AGR; HGNC:25419; -. DR CTD; 200894; -. DR DisGeNET; 200894; -. DR GeneCards; ARL13B; -. DR GeneReviews; ARL13B; -. DR HGNC; HGNC:25419; ARL13B. DR HPA; ENSG00000169379; Tissue enhanced (retina). DR MalaCards; ARL13B; -. DR MIM; 608922; gene. DR MIM; 612291; phenotype. DR neXtProt; NX_Q3SXY8; -. DR OpenTargets; ENSG00000169379; -. DR Orphanet; 475; Joubert syndrome. DR PharmGKB; PA134975272; -. DR VEuPathDB; HostDB:ENSG00000169379; -. DR eggNOG; KOG0074; Eukaryota. DR eggNOG; KOG0076; Eukaryota. DR GeneTree; ENSGT00940000156365; -. DR HOGENOM; CLU_040729_3_0_1; -. DR InParanoid; Q3SXY8; -. DR OMA; QKMEHEQ; -. DR OrthoDB; 5483033at2759; -. DR PhylomeDB; Q3SXY8; -. DR TreeFam; TF105476; -. DR PathwayCommons; Q3SXY8; -. DR Reactome; R-HSA-5624958; ARL13B-mediated ciliary trafficking of INPP5E. DR Reactome; R-HSA-9013406; RHOQ GTPase cycle. DR Reactome; R-HSA-9013409; RHOJ GTPase cycle. DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy. DR Reactome; R-HSA-9615710; Late endosomal microautophagy. DR Reactome; R-HSA-9646399; Aggrephagy. DR SignaLink; Q3SXY8; -. DR BioGRID-ORCS; 200894; 18 hits in 1156 CRISPR screens. DR ChiTaRS; ARL13B; human. DR GeneWiki; ARL13B; -. DR GenomeRNAi; 200894; -. DR Pharos; Q3SXY8; Tbio. DR PRO; PR:Q3SXY8; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q3SXY8; Protein. DR Bgee; ENSG00000169379; Expressed in secondary oocyte and 168 other cell types or tissues. DR ExpressionAtlas; Q3SXY8; baseline and differential. DR GO; GO:0005930; C:axoneme; IEA:Ensembl. DR GO; GO:0060170; C:ciliary membrane; ISS:UniProtKB. DR GO; GO:0005929; C:cilium; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0031514; C:motile cilium; IBA:GO_Central. DR GO; GO:0097730; C:non-motile cilium; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB. DR GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl. DR GO; GO:0021943; P:formation of radial glial scaffolds; ISS:UniProtKB. DR GO; GO:0001947; P:heart looping; IEA:Ensembl. DR GO; GO:0021830; P:interneuron migration from the subpallium to the cortex; ISS:UniProtKB. DR GO; GO:0070986; P:left/right axis specification; IEA:Ensembl. DR GO; GO:0021532; P:neural tube patterning; ISS:UniProtKB. DR GO; GO:1905515; P:non-motile cilium assembly; ISS:UniProtKB. DR GO; GO:0097500; P:receptor localization to non-motile cilium; IBA:GO_Central. DR GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB. DR CDD; cd04161; Arl2l1_Arl13_like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR006689; Small_GTPase_ARF/SAR. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR46090; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 13B; 1. DR PANTHER; PTHR46090:SF3; ADP-RIBOSYLATION FACTOR-LIKE PROTEIN 13B; 1. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR SMART; SM00178; SAR; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51417; ARF; 1. DR Genevisible; Q3SXY8; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cell projection; Ciliopathy; Cilium; KW Coiled coil; Disease variant; GTP-binding; Isopeptide bond; KW Joubert syndrome; Lipoprotein; Membrane; Nucleotide-binding; Palmitate; KW Reference proteome; Ubl conjugation. FT CHAIN 1..428 FT /note="ADP-ribosylation factor-like protein 13B" FT /id="PRO_0000251137" FT REGION 207..287 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 318..428 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 192..245 FT /evidence="ECO:0000255" FT COMPBIAS 207..237 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 267..287 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 325..346 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 368..385 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 28..35 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 71..75 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 130..133 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT LIPID 8 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT LIPID 9 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CROSSLNK 329 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000305" FT VAR_SEQ 1..103 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_045421" FT VAR_SEQ 21..127 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020733" FT VARIANT 79 FT /note="R -> Q (in JBTS8; reduces binding to GTP; FT dbSNP:rs121912606)" FT /evidence="ECO:0000269|PubMed:18674751" FT /id="VAR_054371" FT VARIANT 86 FT /note="Y -> C (in JBTS8; the patient also manifests obesity FT as a feature; decreased localization to cilium; FT dbSNP:rs863225430)" FT /evidence="ECO:0000269|PubMed:25138100" FT /id="VAR_077496" FT VARIANT 200 FT /note="R -> C (in JBTS8; dbSNP:rs121912608)" FT /evidence="ECO:0000269|PubMed:18674751" FT /id="VAR_054372" FT VARIANT 348 FT /note="T -> S (in dbSNP:rs33944211)" FT /id="VAR_048319" FT VARIANT 390 FT /note="R -> L (in a nephronophthisis (NPHP) patient)" FT /evidence="ECO:0000269|PubMed:21068128" FT /id="VAR_069190" FT MUTAGEN 35 FT /note="T->N: Does not affect localization to cilia." FT /evidence="ECO:0000269|PubMed:18554500" FT MUTAGEN 130 FT /note="N->I: Does not affect localization to cilia." FT /evidence="ECO:0000269|PubMed:18554500" FT MUTAGEN 231 FT /note="K->R: No effect. Abolishes sumoylation; when FT associated with R-270; R-275; R-276; R-279 and R-329." FT /evidence="ECO:0000269|PubMed:23128241" FT MUTAGEN 270 FT /note="K->R: No effect. Abolishes sumoylation; when FT associated with R-231; R-275; R-276; R-279 and R-329." FT /evidence="ECO:0000269|PubMed:23128241" FT MUTAGEN 275 FT /note="K->R: No effect. Abolishes sumoylation; when FT associated with R-231; R-270; R-276; R-279 and R-329." FT /evidence="ECO:0000269|PubMed:23128241" FT MUTAGEN 276 FT /note="K->R: No effect. Abolishes sumoylation; when FT associated with R-231; R-270; R-275; R-279 and R-329." FT /evidence="ECO:0000269|PubMed:23128241" FT MUTAGEN 279 FT /note="K->R: No effect. Abolishes sumoylation; when FT associated with R-231; R-270; R-275; R-276 and R-329." FT /evidence="ECO:0000269|PubMed:23128241" FT MUTAGEN 329 FT /note="K->R: Abolishes sumoylation. Abolishes sumoylation; FT when associated with R-231; R-270; R-275; R-276 and R-279." FT /evidence="ECO:0000269|PubMed:23128241" FT CONFLICT 275 FT /note="K -> KK (in Ref. 1; CAD28544)" FT /evidence="ECO:0000305" SQ SEQUENCE 428 AA; 48643 MW; 002B38A38D1F7BDD CRC64; MFSLMASCCG WFKRWREPVR KVTLLMVGLD NAGKTATAKG IQGEYPEDVA PTVGFSKINL RQGKFEVTIF DLGGGIRIRG IWKNYYAESY GVIFVVDSSD EERMEETKEA MSEMLRHPRI SGKPILVLAN KQDKEGALGE ADVIECLSLE KLVNEHKCLC QIEPCSAISG YGKKIDKSIK KGLYWLLHVI ARDFDALNER IQKETTEQRA LEEQEKQERA ERVRKLREER KQNEQEQAEL DGTSGLAELD PEPTNPFQPI ASVIIENEGK LEREKKNQKM EKDSDGCHLK HKMEHEQIET QGQVNHNGQK NNEFGLVENY KEALTQQLKN EDETDRPSLE SANGKKKTKK LRMKRNHRVE PLNIDDCAPE SPTPPPPPPP VGWGTPKVTR LPKLEPLGET HHNDFYRKPL PPLAVPQRPN SDAHDVIS //