RT4I1_MOUSE
ID RT4I1_MOUSE Reviewed; 396 AA.
AC Q924D0; Q8R1T0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Reticulon-4-interacting protein 1, mitochondrial;
DE AltName: Full=NOGO-interacting mitochondrial protein;
DE Flags: Precursor;
GN Name=Rtn4ip1; Synonyms=Nimp;
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 [MRNA], FUNCTION, INTERACTION WITH RTN4; UQCRC1 AND
RP UQCRC2, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=12067236; DOI=10.1046/j.1471-4159.2002.00788.x;
RA Hu W.-H., Hausmann O.N., Yan M.-S., Walters W.M., Wong P.K.Y., Bethea J.R.;
RT "Identification and characterization of a novel Nogo-interacting
RT mitochondrial protein (NIMP).";
RL J. Neurochem. 81:36-45(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Heart, Liver, and Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
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).
RN [5]
RP FUNCTION.
RX PubMed=26593267; DOI=10.1016/j.ajhg.2015.09.012;
RA Angebault C., Guichet P.O., Talmat-Amar Y., Charif M., Gerber S.,
RA Fares-Taie L., Gueguen N., Halloy F., Moore D., Amati-Bonneau P., Manes G.,
RA Hebrard M., Bocquet B., Quiles M., Piro-Megy C., Teigell M., Delettre C.,
RA Rossel M., Meunier I., Preising M., Lorenz B., Carelli V., Chinnery P.F.,
RA Yu-Wai-Man P., Kaplan J., Roubertie A., Barakat A., Bonneau D., Reynier P.,
RA Rozet J.M., Bomont P., Hamel C.P., Lenaers G.;
RT "Recessive mutations in RTN4IP1 cause isolated and syndromic optic
RT neuropathies.";
RL Am. J. Hum. Genet. 97:754-760(2015).
CC -!- FUNCTION: Plays a role in the regulation of retinal ganglion cell (RGC)
CC neurite outgrowth, and hence in the development of the inner retina and
CC optic nerve (PubMed:26593267). Appears to be a potent inhibitor of
CC regeneration following spinal cord injury (PubMed:12067236).
CC {ECO:0000269|PubMed:12067236, ECO:0000269|PubMed:26593267}.
CC -!- SUBUNIT: Interacts with RTN4, UQCRC1 and UQCRC2.
CC {ECO:0000269|PubMed:12067236}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12067236}.
CC Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8WWV3}.
CC Note=Colocalizes with the endoplasmic reticulum HSPA5 at spots
CC corresponding to contacts with mitochondria.
CC {ECO:0000250|UniProtKB:Q8WWV3}.
CC -!- TISSUE SPECIFICITY: Widely expressed in mitochondria-enriched tissues.
CC Found in heart, kidney, liver, brain and spinal cord.
CC {ECO:0000269|PubMed:12067236}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. Quinone oxidoreductase subfamily. {ECO:0000305}.
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DR EMBL; AF336862; AAK64604.1; -; mRNA.
DR EMBL; AK050324; BAC34189.1; -; mRNA.
DR EMBL; AK085858; BAC39556.1; -; mRNA.
DR EMBL; AK088029; BAC40106.1; -; mRNA.
DR EMBL; BC024116; AAH24116.1; -; mRNA.
DR CCDS; CCDS23823.1; -.
DR RefSeq; NP_570962.2; NM_130892.4.
DR AlphaFoldDB; Q924D0; -.
DR SMR; Q924D0; -.
DR BioGRID; 228396; 12.
DR STRING; 10090.ENSMUSP00000060940; -.
DR iPTMnet; Q924D0; -.
DR PhosphoSitePlus; Q924D0; -.
DR EPD; Q924D0; -.
DR jPOST; Q924D0; -.
DR MaxQB; Q924D0; -.
DR PaxDb; Q924D0; -.
DR PeptideAtlas; Q924D0; -.
DR PRIDE; Q924D0; -.
DR ProteomicsDB; 260864; -.
DR DNASU; 170728; -.
DR GeneID; 170728; -.
DR KEGG; mmu:170728; -.
DR UCSC; uc007ezp.1; mouse.
DR CTD; 84816; -.
DR MGI; MGI:2178759; Rtn4ip1.
DR eggNOG; KOG1198; Eukaryota.
DR InParanoid; Q924D0; -.
DR OrthoDB; 727365at2759; -.
DR PhylomeDB; Q924D0; -.
DR TreeFam; TF313919; -.
DR BioGRID-ORCS; 170728; 17 hits in 73 CRISPR screens.
DR PRO; PR:Q924D0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q924D0; protein.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0050773; P:regulation of dendrite development; IMP:UniProtKB.
DR CDD; cd08248; RTN4I1; 1.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR InterPro; IPR037397; RTN4I1.
DR Pfam; PF08240; ADH_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Neurogenesis;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..40
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 41..396
FT /note="Reticulon-4-interacting protein 1, mitochondrial"
FT /id="PRO_0000042115"
FT CONFLICT 201
FT /note="K -> R (in Ref. 2; BAC34189/BAC39556/BAC40106 and 3;
FT AAH24116)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="K -> E (in Ref. 1; AAK64604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 43371 MW; A426344D4216D84A CRC64;
MGVLKTCVLR RSACAAACFW RRTVIPKPPF RGISTTSARS TVMPAWVIDK YGKNEVLRFT
QNMMLPIIHY PNEVIIKVHA ASVNPIDVNM RSGYGATALN MKRDPLHMKT KGEEFPLTLG
RDVSGVVMEC GLDVKYFQPG DEVWAAVPPW KQGTLSEFVV VSGNEVSHKP KSLTHTQAAS
LPYVALTAWS AINKVGGLSD KNCKGKRALI LGASGGVGTF AIQVMKAWGA HVTAVCSKDA
SELVRKLGAD EVIDYTLGSV EEQLKSLKLF DFILDNVGGS TETWALNFLK KWSGATYVTL
VTPFLLNMDR LGVADGMLQT GVTVGTKALK HLWQGVHYRW AFFMASGPYL DEIAELVDAG
KIRPVIERTF PFSEVPEAFL KVERGHARGK TVVNVV
