RINT1_MOUSE
ID RINT1_MOUSE Reviewed; 792 AA.
AC Q8BZ36; Q3UXS1; Q6P1I2; Q8C193;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=RAD50-interacting protein 1;
DE AltName: Full=RAD50 interactor 1;
DE Short=RINT-1;
GN Name=Rint1;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Skin, Vagina, and Wolffian duct;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryonic 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Pancreas, Spleen, 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: Involved in regulation of membrane traffic between the Golgi
CC and the endoplasmic reticulum; the function is proposed to depend on
CC its association in the NRZ complex which is believed to play a role in
CC SNARE assembly at the ER. May play a role in cell cycle checkpoint
CC control. Essential for telomere length control (By similarity).
CC {ECO:0000250|UniProtKB:Q6NUQ1}.
CC -!- SUBUNIT: Component of the NRZ complex composed of NBAS, ZW10 and
CC RINT1/TIP20L; NRZ associates with SNAREs STX18, USE1L, BNIP1/SEC20L and
CC SEC22B (the assembly has been described as syntaxin 18 complex).
CC Interacts directly with BNIP1/SEC20L and ZW10. Interacts with RAD50
CC during late S and G2/M phases. Interacts with RBL2, preferentially with
CC the active, hypophosphorylated form (By similarity).
CC {ECO:0000250|UniProtKB:Q6NUQ1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6NUQ1}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6NUQ1};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q6NUQ1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BZ36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BZ36-2; Sequence=VSP_012658;
CC -!- SIMILARITY: Belongs to the RINT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC29582.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK028707; BAC26077.1; -; mRNA.
DR EMBL; AK036805; BAC29582.1; ALT_FRAME; mRNA.
DR EMBL; AK135334; BAE22492.1; -; mRNA.
DR EMBL; BC065059; AAH65059.2; -; mRNA.
DR CCDS; CCDS39025.1; -. [Q8BZ36-1]
DR CCDS; CCDS80220.1; -. [Q8BZ36-2]
DR RefSeq; NP_001297396.1; NM_001310467.1. [Q8BZ36-2]
DR RefSeq; NP_796297.2; NM_177323.4. [Q8BZ36-1]
DR AlphaFoldDB; Q8BZ36; -.
DR SMR; Q8BZ36; -.
DR IntAct; Q8BZ36; 1.
DR MINT; Q8BZ36; -.
DR STRING; 10090.ENSMUSP00000030852; -.
DR iPTMnet; Q8BZ36; -.
DR PhosphoSitePlus; Q8BZ36; -.
DR EPD; Q8BZ36; -.
DR MaxQB; Q8BZ36; -.
DR PaxDb; Q8BZ36; -.
DR PeptideAtlas; Q8BZ36; -.
DR PRIDE; Q8BZ36; -.
DR ProteomicsDB; 253243; -. [Q8BZ36-1]
DR ProteomicsDB; 253244; -. [Q8BZ36-2]
DR Antibodypedia; 17090; 112 antibodies from 23 providers.
DR DNASU; 72772; -.
DR Ensembl; ENSMUST00000030852; ENSMUSP00000030852; ENSMUSG00000028999. [Q8BZ36-1]
DR Ensembl; ENSMUST00000115113; ENSMUSP00000110766; ENSMUSG00000028999. [Q8BZ36-2]
DR GeneID; 72772; -.
DR KEGG; mmu:72772; -.
DR UCSC; uc008wqq.1; mouse. [Q8BZ36-1]
DR UCSC; uc012dsx.1; mouse. [Q8BZ36-2]
DR CTD; 60561; -.
DR MGI; MGI:1916233; Rint1.
DR VEuPathDB; HostDB:ENSMUSG00000028999; -.
DR eggNOG; KOG2218; Eukaryota.
DR GeneTree; ENSGT00390000017006; -.
DR HOGENOM; CLU_020201_0_0_1; -.
DR InParanoid; Q8BZ36; -.
DR OMA; WPFVGPP; -.
DR OrthoDB; 1393136at2759; -.
DR PhylomeDB; Q8BZ36; -.
DR TreeFam; TF324274; -.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR BioGRID-ORCS; 72772; 20 hits in 71 CRISPR screens.
DR ChiTaRS; Rint1; mouse.
DR PRO; PR:Q8BZ36; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BZ36; protein.
DR Bgee; ENSMUSG00000028999; Expressed in rostral migratory stream and 214 other tissues.
DR ExpressionAtlas; Q8BZ36; baseline and differential.
DR Genevisible; Q8BZ36; MM.
DR GO; GO:0070939; C:Dsl1/NZR complex; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:HGNC.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR Gene3D; 1.20.58.670; -; 1.
DR InterPro; IPR042044; EXOC6PINT-1/Sec15/Tip20_C_dom2.
DR InterPro; IPR007528; RINT1_Tip20.
DR PANTHER; PTHR13520; PTHR13520; 1.
DR Pfam; PF04437; RINT1_TIP1; 1.
DR PROSITE; PS51386; RINT1_TIP20; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Coiled coil; Cytoplasm;
KW Endoplasmic reticulum; ER-Golgi transport; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..792
FT /note="RAD50-interacting protein 1"
FT /id="PRO_0000097350"
FT DOMAIN 220..792
FT /note="RINT1/TIP20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00717"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 71..123
FT /evidence="ECO:0000255"
FT COMPBIAS 29..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 172..229
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012658"
FT CONFLICT 24
FT /note="K -> N (in Ref. 1; BAC29582)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="V -> D (in Ref. 1; BAC26077)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="S -> C (in Ref. 1; BAC29582)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 792 AA; 90094 MW; B1E104125538F6D1 CRC64;
MLAADDIGEV PAAPCCPESG DETKNTDVKS DVNTAAPAGS EQLSQGGSDD ALLSYVSAFI
EKEVGSDLKS LKTLGKLIEQ MTESKVKLEE QVLTISSEIP KRIQSALKDA EESKQLLDEF
LEQEAPLFSS ISSHLLMAQP WMDDLGAMIT QMEEIERHLA YLKWVSQTEE LSDNIQQYLM
TNSVPEAASL LVTMTELDIQ LQESSCTHLL SFMRATVKFW HKILKDKLTS DFEEVLAQLH
WPFTSHTQSQ TVGGSRPAGT PELYSSLDTL FCQLLKLQAS DELLTEPKQL PEKYCLPASP
PVTLPIQVML APLQKRFRYH FRGSRQTNVM SKPEWYLAQV LMWIGNHTQF LDEKIQPILD
KVGSAVNARL EFSRGLVMLI LEKLASDIPC LLYDDSLFCH LVDEVLLFER ELHTVHGYPS
TFASCMHILS EETCFQRWLT VERKFALQKM DSMLSSEAAW VSQYKDISDV DEMKVPDCAE
VFMTLLLVIT DRYKNLPTAS RKLQFLELQK DLVDDFRIRL TQVMKEETRA ALGFRYCAIL
NAVNYISAVL ADWADNVFFL QLQQAALEVF AENNVLSKLQ LGQLASMESS VFDDMINLLE
RLKLDMLTRQ VDHVFREVKD SAKLYKKERW LSLPSQSEQA VMSLSSSACP LLLTLRDRLL
QLEQQLCFSL FRIFWQMLAE KLDLYIYQEI ILANHFNEGG AAQLQFDMTR NLFPLFSHYC
KRPENYFKHV KEACIILNLN IGSALLLKDV LQSVSEHIPA TAALNEVGVY KLAQQDVEIL
LNLRTNWPNT GK
