ID RB27B_HUMAN Reviewed; 218 AA. AC O00194; B2RAB0; Q9BZB6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 207. DE RecName: Full=Ras-related protein Rab-27B; DE EC=3.6.5.2 {ECO:0000305|PubMed:30771381}; DE AltName: Full=C25KG; GN Name=RAB27B; 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]. RC TISSUE=Melanocyte; RX PubMed=9066979; DOI=10.1006/bmme.1996.2559; RA Chen D., Guo J., Miki T., Tachibana M., Gahl W.A.; RT "Molecular cloning and characterization of rab27a and rab27b, novel human RT rab proteins shared by melanocytes and platelets."; RL Biochem. Mol. Med. 60:27-37(1997). RN [2] RP SEQUENCE REVISION TO 206. RA Chen D., Gahl W.A.; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=11178108; DOI=10.1186/1471-2156-2-2; RA Ramalho J.S., Tolmachova T., Hume A.N., McGuigan A., Gregory-Evans C.Y., RA Huxley C., Seabra M.C.; RT "Chromosomal mapping, gene structure and characterization of the human and RT murine RAB27B gene."; RL BMC Genet. 2:2-2(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala; 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 [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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; 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 PARTIAL PROTEIN SEQUENCE. RC TISSUE=Platelet; RX PubMed=2507536; DOI=10.1016/s0021-9258(18)71450-6; RA Nagata K., Itoh H., Katada T., Takenaka K., Ui M., Kaziro Y., Nozawa Y.; RT "Purification, identification, and characterization of two GTP-binding RT proteins with molecular weights of 25,000 and 21,000 in human platelet RT cytosol. One is the rap1/smg21/Krev-1 protein and the other is a novel GTP- RT binding protein."; RL J. Biol. Chem. 264:17000-17005(1989). RN [9] RP PROTEIN SEQUENCE OF 2-28; 38-47; 50-64; 68-80 AND 150-184, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Platelet; RA Bienvenut W.V., Claeys D.; RL Submitted (NOV-2005) to UniProtKB. RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP FUNCTION. RX PubMed=21775604; DOI=10.1523/jneurosci.0436-11.2011; RA Huang S.H., Duan S., Sun T., Wang J., Zhao L., Geng Z., Yan J., Sun H.J., RA Chen Z.Y.; RT "JIP3 mediates TrkB axonal anterograde transport and enhances BDNF RT signaling by directly bridging TrkB with kinesin-1."; RL J. Neurosci. 31:10602-10614(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DENND10, ACTIVITY RP REGULATION, AND MUTAGENESIS OF THR-23 AND GLN-78. RX PubMed=30771381; DOI=10.1016/j.bbamcr.2019.02.006; RA Zhang J., Zhang K., Qi L., Hu Q., Shen Z., Liu B., Deng J., Zhang C., RA Zhang Y.; RT "DENN domain-containing protein FAM45A regulates the homeostasis of RT late/multivesicular endosomes."; RL Biochim. Biophys. Acta 1866:916-929(2019). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 4-201 IN COMPLEX WITH GDP, AND RP DISULFIDE BOND. RG Structural genomics consortium (SGC); RT "The crystal structure of human RAB27B."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Small GTPase which cycles between active GTP-bound and CC inactive GDP-bound states. In its active state, binds to a variety of CC effector proteins to regulate homeostasis of late endocytic pathway, CC including endosomal positioning, maturation and secretion CC (PubMed:30771381). Plays a role in NTRK2/TRKB axonal anterograde CC transport by facilitating the association of NTRK2/TRKB with KLC1 CC (PubMed:21775604). May be involved in targeting uroplakins to CC urothelial apical membranes (By similarity). CC {ECO:0000250|UniProtKB:Q8HZJ5, ECO:0000269|PubMed:21775604, CC ECO:0000269|PubMed:30771381}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; CC Evidence={ECO:0000305|PubMed:30771381}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000305|PubMed:30771381}; CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase CC activating proteins (GAPs) which increase the GTP hydrolysis activity, CC and GDP dissociation inhibitors which inhibit the dissociation of the CC nucleotide from the GTPase. Activated by GEFs such as DENND10. CC {ECO:0000305|PubMed:30771381}. CC -!- SUBUNIT: Interacts with SYTL2, SYTL4, MYRIP and MLPH. Interacts with CC RPH3A and RPH3A (By similarity). Interacts (GDP-bound form CC preferentially) with DENND10 (PubMed:30771381). CC {ECO:0000250|UniProtKB:Q99P58, ECO:0000269|PubMed:30771381}. CC -!- INTERACTION: CC O00194; Q03135: CAV1; NbExp=2; IntAct=EBI-10179046, EBI-603614; CC O00194; P49366: DHPS; NbExp=6; IntAct=EBI-10179046, EBI-741925; CC O00194; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-10179046, EBI-739467; CC O00194; Q9BV36: MLPH; NbExp=3; IntAct=EBI-10179046, EBI-7042162; CC O00194; Q8NFW9: MYRIP; NbExp=3; IntAct=EBI-10179046, EBI-1759414; CC O00194; Q9Y2J0-2: RPH3A; NbExp=3; IntAct=EBI-10179046, EBI-16808141; CC O00194; Q9UNE2: RPH3AL; NbExp=3; IntAct=EBI-10179046, EBI-2855824; CC O00194; Q8TDW5: SYTL5; NbExp=5; IntAct=EBI-10179046, EBI-2939487; CC O00194; Q8TDW5-2: SYTL5; NbExp=3; IntAct=EBI-10179046, EBI-12243980; CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Late endosome CC {ECO:0000269|PubMed:30771381}. CC -!- TISSUE SPECIFICITY: Expressed primarily in testis. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {ECO:0000305}. 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; U57093; AAC51194.2; -; mRNA. DR EMBL; AF329499; AAK11243.1; -; mRNA. DR EMBL; AF498954; AAM21102.1; -; mRNA. DR EMBL; AK314115; BAG36807.1; -; mRNA. DR EMBL; CH471096; EAW63010.1; -; Genomic_DNA. DR EMBL; BC027474; AAH27474.1; -; mRNA. DR CCDS; CCDS11958.1; -. DR RefSeq; NP_004154.2; NM_004163.4. DR RefSeq; XP_005266790.1; XM_005266733.1. DR RefSeq; XP_016881402.1; XM_017025913.1. DR RefSeq; XP_016881403.1; XM_017025914.1. DR PDB; 2F7S; X-ray; 2.70 A; A/B=4-201. DR PDBsum; 2F7S; -. DR AlphaFoldDB; O00194; -. DR SMR; O00194; -. DR BioGRID; 111812; 41. DR DIP; DIP-48948N; -. DR IntAct; O00194; 19. DR STRING; 9606.ENSP00000262094; -. DR GlyGen; O00194; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O00194; -. DR PhosphoSitePlus; O00194; -. DR SwissPalm; O00194; -. DR BioMuta; RAB27B; -. DR OGP; O00194; -. DR EPD; O00194; -. DR jPOST; O00194; -. DR MassIVE; O00194; -. DR MaxQB; O00194; -. DR PaxDb; 9606-ENSP00000262094; -. DR PeptideAtlas; O00194; -. DR ProteomicsDB; 47773; -. DR Pumba; O00194; -. DR Antibodypedia; 4487; 312 antibodies from 32 providers. DR DNASU; 5874; -. DR Ensembl; ENST00000262094.10; ENSP00000262094.4; ENSG00000041353.10. DR GeneID; 5874; -. DR KEGG; hsa:5874; -. DR MANE-Select; ENST00000262094.10; ENSP00000262094.4; NM_004163.4; NP_004154.2. DR UCSC; uc002lfr.4; human. DR AGR; HGNC:9767; -. DR CTD; 5874; -. DR DisGeNET; 5874; -. DR GeneCards; RAB27B; -. DR HGNC; HGNC:9767; RAB27B. DR HPA; ENSG00000041353; Tissue enhanced (stomach). DR MIM; 603869; gene. DR neXtProt; NX_O00194; -. DR OpenTargets; ENSG00000041353; -. DR PharmGKB; PA34118; -. DR VEuPathDB; HostDB:ENSG00000041353; -. DR eggNOG; KOG0081; Eukaryota. DR GeneTree; ENSGT00940000157449; -. DR HOGENOM; CLU_041217_10_1_1; -. DR InParanoid; O00194; -. DR OMA; TEKKCAC; -. DR OrthoDB; 8685at2759; -. DR PhylomeDB; O00194; -. DR TreeFam; TF312895; -. DR PathwayCommons; O00194; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-8873719; RAB geranylgeranylation. DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs. DR SignaLink; O00194; -. DR BioGRID-ORCS; 5874; 7 hits in 1154 CRISPR screens. DR ChiTaRS; RAB27B; human. DR EvolutionaryTrace; O00194; -. DR GenomeRNAi; 5874; -. DR Pharos; O00194; Tbio. DR PRO; PR:O00194; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; O00194; Protein. DR Bgee; ENSG00000041353; Expressed in esophagus squamous epithelium and 182 other cell types or tissues. DR ExpressionAtlas; O00194; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC. DR GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0005795; C:Golgi stack; IDA:UniProtKB. DR GO; GO:0005770; C:late endosome; IDA:UniProtKB. DR GO; GO:0042470; C:melanosome; IDA:UniProtKB. DR GO; GO:0032585; C:multivesicular body membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0031088; C:platelet dense granule membrane; TAS:Reactome. DR GO; GO:0030141; C:secretory granule; IBA:GO_Central. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl. DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:UniProtKB. DR GO; GO:0042589; C:zymogen granule membrane; IEA:Ensembl. DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC. DR GO; GO:0019003; F:GDP binding; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:UniProtKB. DR GO; GO:0006887; P:exocytosis; IBA:GO_Central. DR GO; GO:0071985; P:multivesicular body sorting pathway; IMP:UniProtKB. DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl. DR CDD; cd04127; Rab27A; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR041837; Rab27a/b. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47977; RAS-RELATED PROTEIN RAB; 1. DR PANTHER; PTHR47977:SF33; RAS-RELATED PROTEIN RAB-27B; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. DR Genevisible; O00194; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Disulfide bond; KW Endosome; GTP-binding; Hydrolase; Lipoprotein; Membrane; Methylation; KW Nucleotide-binding; Prenylation; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.9" FT CHAIN 2..218 FT /note="Ras-related protein Rab-27B" FT /id="PRO_0000121224" FT REGION 194..218 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 38..46 FT /note="Effector region" FT /evidence="ECO:0000250" FT BINDING 16..24 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT BINDING 74..78 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 133..136 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT BINDING 163..165 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT MOD_RES 2 FT /note="N-acetylthreonine" FT /evidence="ECO:0000269|Ref.9" FT MOD_RES 218 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000250" FT LIPID 216 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT LIPID 218 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT DISULFID 123..188 FT /evidence="ECO:0000269|Ref.14" FT VARIANT 92 FT /note="A -> T (in dbSNP:rs9966265)" FT /id="VAR_051714" FT MUTAGEN 23 FT /note="T->N: GDP-locked. Increases interaction with FT DENND10. Disrupts late endocytic pathway homeostasis." FT /evidence="ECO:0000269|PubMed:30771381" FT MUTAGEN 78 FT /note="Q->L: GTP-locked. decreases interaction with FT DENND10." FT /evidence="ECO:0000269|PubMed:30771381" FT STRAND 7..16 FT /evidence="ECO:0007829|PDB:2F7S" FT HELIX 22..30 FT /evidence="ECO:0007829|PDB:2F7S" FT STRAND 37..54 FT /evidence="ECO:0007829|PDB:2F7S" FT STRAND 65..77 FT /evidence="ECO:0007829|PDB:2F7S" FT HELIX 78..89 FT /evidence="ECO:0007829|PDB:2F7S" FT STRAND 94..100 FT /evidence="ECO:0007829|PDB:2F7S" FT HELIX 104..115 FT /evidence="ECO:0007829|PDB:2F7S" FT TURN 122..124 FT /evidence="ECO:0007829|PDB:2F7S" FT STRAND 127..133 FT /evidence="ECO:0007829|PDB:2F7S" FT HELIX 138..140 FT /evidence="ECO:0007829|PDB:2F7S" FT HELIX 145..154 FT /evidence="ECO:0007829|PDB:2F7S" FT STRAND 159..162 FT /evidence="ECO:0007829|PDB:2F7S" FT TURN 164..166 FT /evidence="ECO:0007829|PDB:2F7S" FT HELIX 170..188 FT /evidence="ECO:0007829|PDB:2F7S" SQ SEQUENCE 218 AA; 24608 MW; 8ED640F0C15EDCD3 CRC64; MTDGDYDYLI KLLALGDSGV GKTTFLYRYT DNKFNPKFIT TVGIDFREKR VVYNAQGPNG SSGKAFKVHL QLWDTAGQER FRSLTTAFFR DAMGFLLMFD LTSQQSFLNV RNWMSQLQAN AYCENPDIVL IGNKADLPDQ REVNERQARE LADKYGIPYF ETSAATGQNV EKAVETLLDL IMKRMEQCVE KTQIPDTVNG GNSGNLDGEK PPEKKCIC //