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Protein

RINT1-like protein

Gene

Rint1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

During cytokinesis in male meiotic cells, required for completion of cleavage furrow ingression possibly in conjunction with Zw10. Required for maintenance of Golgi stack number and morphology. Essential for acroblast assembly.1 Publication

GO - Biological processi

  • cleavage furrow ingression Source: FlyBase
  • Golgi organization Source: FlyBase
  • Golgi vesicle transport Source: FlyBase
  • male meiosis cytokinesis Source: FlyBase
  • neurogenesis Source: FlyBase
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-DME-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
RINT1-like protein
Short name:
DmRINT-1
Gene namesi
Name:Rint1Imported
ORF Names:CG8605Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0035762. Rint1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 724724RINT1-like proteinPRO_0000097348Add
BLAST

Proteomic databases

PaxDbiQ9VS46.

Expressioni

Gene expression databases

BgeeiQ9VS46.
ExpressionAtlasiQ9VS46. differential.
GenevisibleiQ9VS46. DM.

Interactioni

Protein-protein interaction databases

BioGridi64247. 2 interactions.
IntActiQ9VS46. 2 interactions.
MINTiMINT-1601225.
STRINGi7227.FBpp0076549.

Structurei

3D structure databases

ProteinModelPortaliQ9VS46.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 724562RINT1/TIP20PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the RINT1 family.Curated
Contains 1 RINT1/TIP20 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2218. Eukaryota.
ENOG410XZD1. LUCA.
GeneTreeiENSGT00390000017006.
InParanoidiQ9VS46.
OMAiIVCQPIN.
OrthoDBiEOG70GMFF.
PhylomeDBiQ9VS46.

Family and domain databases

InterProiIPR007528. RINT1_Tip20.
[Graphical view]
PfamiPF04437. RINT1_TIP1. 1 hit.
[Graphical view]
PROSITEiPS51386. RINT1_TIP20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VS46-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHAELSEMEL RIVARLNEEI GKDASQLHRA SHLVSHYKKH LQVLSQTLDY
60 70 80 90 100
EDPQNVSCYK TAFQCQQQVC ESIDFELEKL AHFEDKLKRK LKECQPVLEG
110 120 130 140 150
VAEDLDKVRQ LQRLQQYLLL VQDIQEISAA LGNAINGKDE DKLVNIYLTL
160 170 180 190 200
YEGNDCEHSV VGRLHAVQAQ SLKSFAERTA IYWHKLLLKR LSSAFEAVLK
210 220 230 240 250
SMRWAHLEQQ ALNYSSARDT AKAQLLAEYM FLIKSPAEER APLQSITPSI
260 270 280 290 300
VCQPINRVVQ LLLAPYRQRF QFHFTGTRQT NRLDKPEWFY TQILNWGKET
310 320 330 340 350
HFFVGKTFQP AAIKAGKLDY NLRLEFIRGL VQLAIEKLAV DIEQIAQDQI
360 370 380 390 400
LFAHLLDETL AFESELRETF GYPASFPSAI SVITQPMYLL RWISLEERFC
410 420 430 440 450
AEKMDDILQA ETPFQLIDPN SFENDLKIPK CADQFMRLLD AIKDRYYGLI
460 470 480 490 500
QPGHQLQFLH LQLELIDSFR QRLVQLHSSG AVPSIPILNA INYLVMVLRE
510 520 530 540 550
WGENVHYLHL HAALAGPNAT EINSVFEHAV AELEHWARQL MRNLATKATN
560 570 580 590 600
EMKAKSMSYR RDAWPTMPEQ NSREPFILSP SGGEMFQVLV TLLHNLEREL
610 620 630 640 650
SANLFTQTLR LIAHQIDDFM LESMVMNTKF SAAGAAQFNY DMTRNLFALF
660 670 680 690 700
GQYTRRPELL FKRTHDACKL LAAARGTALL LLETLRGNQS VEEKTKPLRE
710 720
LHVLSMDSKQ CIEVLERRMD IKMF
Length:724
Mass (Da):83,535
Last modified:October 1, 2002 - v2
Checksum:i7788CD208A44A5BD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti285 – 2851K → N in AAK77245 (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF50583.2.
AY047513 mRNA. Translation: AAK77245.1.
RefSeqiNP_648102.2. NM_139845.3.
UniGeneiDm.36780.

Genome annotation databases

EnsemblMetazoaiFBtr0076838; FBpp0076549; FBgn0035762.
GeneIDi38807.
KEGGidme:Dmel_CG8605.
UCSCiCG8605-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF50583.2.
AY047513 mRNA. Translation: AAK77245.1.
RefSeqiNP_648102.2. NM_139845.3.
UniGeneiDm.36780.

3D structure databases

ProteinModelPortaliQ9VS46.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64247. 2 interactions.
IntActiQ9VS46. 2 interactions.
MINTiMINT-1601225.
STRINGi7227.FBpp0076549.

Proteomic databases

PaxDbiQ9VS46.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076838; FBpp0076549; FBgn0035762.
GeneIDi38807.
KEGGidme:Dmel_CG8605.
UCSCiCG8605-RA. d. melanogaster.

Organism-specific databases

CTDi60561.
FlyBaseiFBgn0035762. Rint1.

Phylogenomic databases

eggNOGiKOG2218. Eukaryota.
ENOG410XZD1. LUCA.
GeneTreeiENSGT00390000017006.
InParanoidiQ9VS46.
OMAiIVCQPIN.
OrthoDBiEOG70GMFF.
PhylomeDBiQ9VS46.

Enzyme and pathway databases

ReactomeiR-DME-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Miscellaneous databases

ChiTaRSiCG8605. fly.
GenomeRNAii38807.
PROiQ9VS46.

Gene expression databases

BgeeiQ9VS46.
ExpressionAtlasiQ9VS46. differential.
GenevisibleiQ9VS46. DM.

Family and domain databases

InterProiIPR007528. RINT1_Tip20.
[Graphical view]
PfamiPF04437. RINT1_TIP1. 1 hit.
[Graphical view]
PROSITEiPS51386. RINT1_TIP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  4. "The Drosophila RZZ complex - roles in membrane trafficking and cytokinesis."
    Wainman A., Giansanti M.G., Goldberg M.L., Gatti M.
    J. Cell Sci. 125:4014-4025(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiRINT1_DROME
AccessioniPrimary (citable) accession number: Q9VS46
Secondary accession number(s): Q961W7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.