RBNS5_MOUSE
ID RBNS5_MOUSE Reviewed; 783 AA.
AC Q80Y56; Q8K0L6; Q9CTW0;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Rabenosyn-5 {ECO:0000250|UniProtKB:Q9H1K0};
DE AltName: Full=FYVE finger-containing Rab5 effector protein rabenosyn-5;
DE AltName: Full=RAB effector RBSN {ECO:0000250|UniProtKB:Q9H1K0};
DE AltName: Full=Zinc finger FYVE domain-containing protein 20;
GN Name=Rbsn {ECO:0000250|UniProtKB:Q9H1K0};
GN Synonyms=Zfyve20 {ECO:0000312|MGI:MGI:1925537};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-384.
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-229, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Rab4/Rab5 effector protein acting in early endocytic membrane
CC fusion and membrane trafficking of recycling endosomes. Required for
CC endosome fusion either homotypically or with clathrin coated vesicles.
CC Plays a role in the lysosomal trafficking of CTSD/cathepsin D from the
CC Golgi to lysosomes. Also promotes the recycling of transferrin directly
CC from early endosomes to the plasma membrane. Binds phospholipid
CC vesicles containing phosphatidylinositol 3-phosphate (PtdInsP3). Plays
CC a role in the recycling of transferrin receptor to the plasma membrane
CC (By similarity). {ECO:0000250|UniProtKB:Q9H1K0}.
CC -!- SUBUNIT: Interacts with EHD1, RAB4A, RAB5A, RAB22A, RAB24 and VPS45.
CC Binds simultaneously to RAB4A and RAB5A in vitro. Interacts with RAB4A
CC and RAB5A that has been activated by GTP binding (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q9H1K0}; Lipid-anchor {ECO:0000250}.
CC Note=Enriched in endosomes that are in close proximity to clathrin-
CC enriched regions at the cell surface (By similarity).
CC {ECO:0000250|UniProtKB:Q9H1K0}.
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DR EMBL; BC031135; AAH31135.1; -; mRNA.
DR EMBL; BC049106; AAH49106.1; -; mRNA.
DR EMBL; AK019909; BAB31910.1; -; mRNA.
DR CCDS; CCDS20374.1; -.
DR RefSeq; NP_084357.2; NM_030081.2.
DR RefSeq; XP_006506831.1; XM_006506768.3.
DR AlphaFoldDB; Q80Y56; -.
DR SMR; Q80Y56; -.
DR BioGRID; 219306; 3.
DR STRING; 10090.ENSMUSP00000014694; -.
DR iPTMnet; Q80Y56; -.
DR PhosphoSitePlus; Q80Y56; -.
DR EPD; Q80Y56; -.
DR jPOST; Q80Y56; -.
DR MaxQB; Q80Y56; -.
DR PaxDb; Q80Y56; -.
DR PeptideAtlas; Q80Y56; -.
DR PRIDE; Q80Y56; -.
DR ProteomicsDB; 300276; -.
DR Antibodypedia; 26666; 205 antibodies from 33 providers.
DR DNASU; 78287; -.
DR Ensembl; ENSMUST00000014694; ENSMUSP00000014694; ENSMUSG00000014550.
DR GeneID; 78287; -.
DR KEGG; mmu:78287; -.
DR UCSC; uc009cyv.1; mouse.
DR CTD; 64145; -.
DR MGI; MGI:1925537; Rbsn.
DR VEuPathDB; HostDB:ENSMUSG00000014550; -.
DR eggNOG; KOG1842; Eukaryota.
DR GeneTree; ENSGT00390000007159; -.
DR HOGENOM; CLU_020798_2_0_1; -.
DR InParanoid; Q80Y56; -.
DR OMA; CNDCSKF; -.
DR OrthoDB; 286684at2759; -.
DR PhylomeDB; Q80Y56; -.
DR TreeFam; TF106125; -.
DR Reactome; R-MMU-168138; Toll Like Receptor 9 (TLR9) Cascade.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 78287; 8 hits in 71 CRISPR screens.
DR PRO; PR:Q80Y56; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q80Y56; protein.
DR Bgee; ENSMUSG00000014550; Expressed in ear vesicle and 231 other tissues.
DR ExpressionAtlas; Q80Y56; baseline and differential.
DR Genevisible; Q80Y56; MM.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IPI:MGI.
DR GO; GO:0034498; P:early endosome to Golgi transport; ISO:MGI.
DR GO; GO:0090160; P:Golgi to lysosome transport; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1903358; P:regulation of Golgi organization; ISO:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR021565; Rbsn_Rab-bd.
DR InterPro; IPR036531; Rbsn_Rab-bd_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF11464; Rbsn; 2.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF140125; SSF140125; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Coiled coil; Endosome; Lipoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H1K0"
FT CHAIN 2..783
FT /note="Rabenosyn-5"
FT /id="PRO_0000098712"
FT DOMAIN 495..514
FT /note="UIM"
FT /evidence="ECO:0000305"
FT ZN_FING 14..37
FT /note="C2H2-type"
FT ZN_FING 156..259
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT REGION 99..262
FT /note="Necessary for the correct targeting to endosomes"
FT /evidence="ECO:0000250"
FT REGION 206..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..783
FT /note="Necessary for interaction with EHD1"
FT /evidence="ECO:0000250"
FT REGION 263..499
FT /note="Necessary for interaction with RAB4A"
FT /evidence="ECO:0000250"
FT REGION 387..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..783
FT /note="Necessary for interaction with RAB5A"
FT /evidence="ECO:0000250"
FT REGION 663..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 377..412
FT /evidence="ECO:0000255"
FT COILED 471..531
FT /evidence="ECO:0000255"
FT COMPBIAS 206..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..707
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1K0"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1K0"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1K0"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1K0"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1K0"
FT CONFLICT 227
FT /note="R -> Q (in Ref. 1; AAH31135)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="P -> S (in Ref. 1; AAH31135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 783 AA; 88491 MW; 80103992F296CCD6 CRC64;
MASLDDPGEV REGFLCPLCL KDLQSFYQLQ SHYEEEHLED RDVKGQIKNL VQKARKAKNK
LLKREGDDRV EPGTQGYESF SYGGVDPYMW EPQELGAMRS HLSDFKKHRA ARIDHYVVEV
NKLIIRLEKL TAFDRTNTET SKIRAIEKSV VPWVNDQDVP FCPDCGNKFS IRNRRHHCRL
CGSIMCKKCM ELIGLPLAHK LTSASKDSLS THTSPSQSPN SVHGSRRGSI SSMSSVSSVL
DEKDDDRIRC CTHCKDKLLK REQQMDEKEH TPDIVKLYEK LRLCMEKVDQ KAPEYIRMAA
SLNAGETTYN LEHANDLRVE VQKVYELIDA LSKKILTLGL NQDPSPHPNT LRLQRMIRYS
ATLFVQEKLL GLMSLPTKEQ FEELKKKRKQ DLEQKRTVER QAALESRRKL EERQSGLASH
TANGDVRSLR GIPPPLRKAE GWLPLSEGQG QSEDPDPLLQ QIYNITSFIR QAKAAGRTDE
VRTLQENLRQ LQDEYDQQQT EKAIELSRKQ AEEEELQREQ LQMLRKRELE REQEQFLAAS
LQTRTRVLEL REVIPFQLEA SRGPHIDLSY SLDQDSSPVQ SSTAPDILTP GSALAPMHLW
SGPPALGQET LPQSTMSQQS DKASLNPFDE DDLSSPTEGA ISPAAVEAFL GPPAAVTKEY
NPFEEDAEEE EVAELGAGNP FTDPDSPAPN PFDEDDGPRP ASPAAPGNPF EECPSTNPFE
VDSDSGMEAE EHIEEELLLQ QIDNIKAYIF DAKQCGRMDE VEVLTENLRE LKCTLAKQKG
APN
