RINL_HUMAN
ID RINL_HUMAN Reviewed; 566 AA.
AC Q6ZS11; B4DPG5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ras and Rab interactor-like protein;
GN Name=RINL;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB5A and RAB22A
CC that activates RAB5A and RAB22A by exchanging bound GDP for free GTP.
CC Plays a role in endocytosis via its role in activating Rab family
CC members (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RAB5A, RAB22A and MUSK. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle {ECO:0000250}.
CC Cytoplasmic vesicle {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZS11-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZS11-2; Sequence=VSP_046909;
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; AK127808; BAC87145.1; -; mRNA.
DR EMBL; AK298327; BAG60577.1; -; mRNA.
DR EMBL; AC011455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS12522.1; -. [Q6ZS11-2]
DR CCDS; CCDS59386.1; -. [Q6ZS11-1]
DR RefSeq; NP_001182762.1; NM_001195833.1. [Q6ZS11-1]
DR RefSeq; NP_940847.1; NM_198445.3. [Q6ZS11-2]
DR AlphaFoldDB; Q6ZS11; -.
DR BioGRID; 125991; 14.
DR IntAct; Q6ZS11; 2.
DR STRING; 9606.ENSP00000467107; -.
DR iPTMnet; Q6ZS11; -.
DR PhosphoSitePlus; Q6ZS11; -.
DR BioMuta; RINL; -.
DR DMDM; 519668657; -.
DR EPD; Q6ZS11; -.
DR jPOST; Q6ZS11; -.
DR MassIVE; Q6ZS11; -.
DR MaxQB; Q6ZS11; -.
DR PaxDb; Q6ZS11; -.
DR PeptideAtlas; Q6ZS11; -.
DR PRIDE; Q6ZS11; -.
DR ProteomicsDB; 68181; -. [Q6ZS11-1]
DR Antibodypedia; 47998; 82 antibodies from 16 providers.
DR DNASU; 126432; -.
DR Ensembl; ENST00000591812.2; ENSP00000467107.1; ENSG00000187994.14. [Q6ZS11-1]
DR Ensembl; ENST00000598904.5; ENSP00000469568.1; ENSG00000187994.14. [Q6ZS11-2]
DR Ensembl; ENST00000635328.1; ENSP00000488992.1; ENSG00000282895.2. [Q6ZS11-2]
DR Ensembl; ENST00000635542.2; ENSP00000489071.1; ENSG00000282895.2. [Q6ZS11-1]
DR GeneID; 126432; -.
DR KEGG; hsa:126432; -.
DR MANE-Select; ENST00000591812.2; ENSP00000467107.1; NM_001195833.2; NP_001182762.1.
DR UCSC; uc010xuo.3; human. [Q6ZS11-1]
DR CTD; 126432; -.
DR DisGeNET; 126432; -.
DR GeneCards; RINL; -.
DR HGNC; HGNC:24795; RINL.
DR HPA; ENSG00000187994; Low tissue specificity.
DR neXtProt; NX_Q6ZS11; -.
DR OpenTargets; ENSG00000187994; -.
DR PharmGKB; PA162401347; -.
DR VEuPathDB; HostDB:ENSG00000187994; -.
DR eggNOG; KOG2320; Eukaryota.
DR GeneTree; ENSGT00940000162381; -.
DR HOGENOM; CLU_038657_0_0_1; -.
DR InParanoid; Q6ZS11; -.
DR OMA; GVWHVPE; -.
DR OrthoDB; 251004at2759; -.
DR PhylomeDB; Q6ZS11; -.
DR TreeFam; TF331067; -.
DR PathwayCommons; Q6ZS11; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q6ZS11; -.
DR BioGRID-ORCS; 126432; 10 hits in 1081 CRISPR screens.
DR ChiTaRS; RINL; human.
DR GenomeRNAi; 126432; -.
DR Pharos; Q6ZS11; Tdark.
DR PRO; PR:Q6ZS11; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6ZS11; protein.
DR Bgee; ENSG00000187994; Expressed in granulocyte and 104 other tissues.
DR ExpressionAtlas; Q6ZS11; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1050.80; -; 1.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR045046; Vps9-like.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR23101; PTHR23101; 1.
DR Pfam; PF02204; VPS9; 1.
DR SMART; SM00167; VPS9; 1.
DR SUPFAM; SSF109993; SSF109993; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell projection; Cytoplasmic vesicle; Endocytosis;
KW GTPase activation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..566
FT /note="Ras and Rab interactor-like protein"
FT /id="PRO_0000318973"
FT DOMAIN 370..515
FT /note="VPS9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550"
FT REGION 182..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046909"
FT VARIANT 402
FT /note="P -> L (in dbSNP:rs8110393)"
FT /id="VAR_038926"
SQ SEQUENCE 566 AA; 62466 MW; AEC0D6D4521E5481 CRC64;
MAQPEDKAPE VPTEGVRLVP PQVNKADRTP LGVLSTLEPL TRLQRTWGVW HVPELDTQDA
EALVGLWPLG SFLVTGRDPS QALVLRSGPL PGEVNTYQIQ KIPRGVSLES SNLCMPDLPH
LLAFLSASRD VLPRTLLLPP PTLGPRDEHT DPVQIGRVQQ DTPGKVLSIV NQLYLETHRG
WGREQTPQET EPEAAQRHDP APRNPAPHGV SWVKGPLSPE VDHPGPALAS LLEEEEEDLE
GKEEGREDDP EEEGPEDVLT IHVQSLVRAR SSYVARQYRS LRVRIASDSG GPHGSGDPAT
ELLQDVRHLL TDLQDHLAKD SYIRAVFGSR GPGLPKKDED PGPALETAVC QAVLAPLKPA
LWTRLRTLRA PELRRLRRRQ TALRAGAGPP GAQGPGPEGQ SPAPALRSRI HERLAHLHAA
CAPRRKVALL LEVCRDVYAG LARGENQDPL GADAFLPALT EELIWSPDIG DTQLDVEFLM
ELLDPDELRG EAGYYLTTWF GALHHIAHYQ PETDRAPRGL SSEARASLHQ WHRRRTLHRK
DHPRAQANLP FKEPWAEETV TGTSDN
