NYNRI_MOUSE
ID NYNRI_MOUSE Reviewed; 1840 AA.
AC Q5DTZ0; B9EKP9; Q32KG8; Q3V1I3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein NYNRIN;
DE AltName: Full=NYN domain and retroviral integrase catalytic domain-containing protein;
DE AltName: Full=Pol-like protein;
GN Name=Nynrin; Synonyms=Kiaa1305;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 680-1840.
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1243-1840.
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [5]
RP IDENTIFICATION.
RC STRAIN=C57BL/6J;
RX PubMed=16155747; DOI=10.1007/s00239-004-0332-0;
RA Youngson N.A., Kocialkowski S., Peel N., Ferguson-Smith A.C.;
RT "A small family of sushi-class retrotransposon-derived genes in mammals and
RT their relation to genomic imprinting.";
RL J. Mol. Evol. 61:481-490(2005).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: The gene encoding this protein may have arisen from the
CC fusion of a cellular gene with retroviral sequences prior to the
CC marsupial-eutherian split. Sequence and structural analyses suggest
CC that the integrase catalytic domain is inactive.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI99159.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC098877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151043; AAI51044.1; -; mRNA.
DR EMBL; AK220380; BAD90437.1; -; mRNA.
DR EMBL; AK132435; BAE21168.1; -; mRNA.
DR EMBL; BN000779; CAI99159.1; ALT_SEQ; Genomic_DNA.
DR CCDS; CCDS49501.1; -.
DR RefSeq; NP_001035161.1; NM_001040072.1.
DR AlphaFoldDB; Q5DTZ0; -.
DR BioGRID; 234923; 4.
DR STRING; 10090.ENSMUSP00000129557; -.
DR iPTMnet; Q5DTZ0; -.
DR PhosphoSitePlus; Q5DTZ0; -.
DR MaxQB; Q5DTZ0; -.
DR PaxDb; Q5DTZ0; -.
DR PeptideAtlas; Q5DTZ0; -.
DR PRIDE; Q5DTZ0; -.
DR ProteomicsDB; 294258; -.
DR Antibodypedia; 57476; 12 antibodies from 7 providers.
DR Ensembl; ENSMUST00000100529; ENSMUSP00000098098; ENSMUSG00000075592.
DR Ensembl; ENSMUST00000168479; ENSMUSP00000129557; ENSMUSG00000075592.
DR GeneID; 277154; -.
DR KEGG; mmu:277154; -.
DR UCSC; uc007uaz.2; mouse.
DR CTD; 57523; -.
DR MGI; MGI:2652872; Nynrin.
DR VEuPathDB; HostDB:ENSMUSG00000075592; -.
DR eggNOG; KOG0017; Eukaryota.
DR eggNOG; KOG3740; Eukaryota.
DR GeneTree; ENSGT00940000161519; -.
DR HOGENOM; CLU_235862_0_0_1; -.
DR InParanoid; Q5DTZ0; -.
DR OMA; THMAVAQ; -.
DR OrthoDB; 583605at2759; -.
DR PhylomeDB; Q5DTZ0; -.
DR TreeFam; TF351195; -.
DR BioGRID-ORCS; 277154; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Nynrin; mouse.
DR PRO; PR:Q5DTZ0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q5DTZ0; protein.
DR Bgee; ENSMUSG00000075592; Expressed in yolk sac and 105 other tissues.
DR ExpressionAtlas; Q5DTZ0; baseline and differential.
DR Genevisible; Q5DTZ0; MM.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR021869; RNase_Zc3h12_NYN.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR041577; RT_RNaseH_2.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF11977; RNase_Zc3h12a; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..1840
FT /note="Protein NYNRIN"
FT /id="PRO_0000314175"
FT TRANSMEM 1315..1335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1351..1371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 740..890
FT /note="RNase NYN"
FT /evidence="ECO:0000255"
FT DOMAIN 1247..1393
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1552..1724
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT REGION 249..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1125..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..945
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..962
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 1407
FT /note="V -> M (in Ref. 4; BAE21168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1840 AA; 203068 MW; 9DF479D569C7FBEB CRC64;
MLLSGGKPPA QEWFMVQTKS KPRVHRQRLQ VQRIFRVKVT AFQSRPDTPY FWLQLEGPRE
NTGKAKEYLK GLCNPELWKE VRYPPVLHCA FLGAQGLFLD CLCWSTLAYL VPGPPGSLMV
GGLTESFTMT QNWLEELVAR LRWGPAPMIT PRGVWETEVT RAFGALVWIR CDKYAGDLLQ
LPPAVQELLL SLVRDAAGKE DIIEWLGHFG ISGTCPNPEI LICLARQQKE SASLVTIKES
PGTLQEIGAL NRASENSKKT TSSGAAGSLT QAQSPPAQET ADQLARDQSN KQGDETNSVG
EEGTATQDTS SQDSENPTQA LLQQKQVPKN EERISLLLPV SALSAYTSWK VWAPGTAFGP
SWPGTIAATF WKINELQSLH LAWLLSQACL NFPFWQRPTG PIQLKLPGRN PLPLKLEWKQ
KELVPLSSAG SPACRPGGDL GRETALKHSP RPEIPSKIIS LSVVPGGCGI KEKVSPGLLQ
VGQSSTSVGD KGISLSDCKG LEKPFSLALS TEQGGSTAQE RPLAQVPEAP TVSETLQVAT
AAEVSNVEHP PTGEGLPATP KVPTALKKPA VYTEPTAPKV PSAPTEPAAP ATPTAPQTPT
AQKTPSVKTL AGLQTPKVQS ETIATAGSEV PKAPAASAVA GPTVDVAQLL SEVQASKNRA
IMLKVQGKPG RQGFQPSSTV PSRSKHQFLK EGLLGAWEGS QRLSPHSQGT NIVTSFQRYN
EALNTPFEMN LSEEPGNPGL RRVVIDGSSV AMVHGLQHFF SCRGIAMAVQ YFWNRGHREI
TVFVPTWQLK KNRRVRESHF LTKLHRLKML SITPSQLENG KKITTYDYRF MVKLAEETDG
VIVTNEQIHI LMNNSKKLMV KDRLLPFTFA GSLFMVPDDP LGRDGPTLEE FLKKPNRLDM
DIGNFLKVWK TLPPSSASIS ELSDDADAEP LEDPQDVEEA GKEEGSLEEE PGIPKPDEED
EQDTNPVSVF GVECPSFSEE ILQCLSLHDP SEGTLDIDLL PVVSSPYLDV PWDGKAPCQQ
VLAQLAQLNI PSNFTALSFF MGFMDSHRDV ISDYEDLVGP LHGLLKQKPD WQWNQEHEKS
FLALKRALVC ALCLSTPNPN LPFYLEVTVS QVSLTASLHQ EHSGRKHPIA YTSKPLLPDE
DSEGPQSGGD SPYAVAWALK HFARCVGDNP VVLRLSYASR TTVDNEAWDS RRASKAWLIR
WSLLLQDKGK RELELSLLQG LLGENQLLTP PSSMPRVFQP LPPSSDLSTF ICVHVSGYCF
YRDDELCAGF GLYILSPTSP PVSLAFSCSP YTTTYAHLAA VACGLERFGQ SQHPVVFLTH
CNWIFSVLWE LLPLWRVRGF LSSDGASLPH PSLLSYIISL TSGFSPLPFI YRTSYRGSLF
AVTVDTLAKQ GAQGGGQWWD LPKDVPVPMV TPHPKGRKPN LLALQLSDTT LADIIAKLQA
GQKLSGPSPF SSAFNSLSLD QDSGLLMFKG ERHPRVWVVP RQLRRDLIFS VHDSPIGEHQ
GLEDTYKTVR LLGWWPGMQD HVRDYCRSCL FCIPRNLIGG ELKVIESPWP LRSTAPWSSL
QIEVVGPVTV SEEGHKHVLI VADANTRWVE AFPLKPYTHV AVAQVLLQHV FARWGVPIRL
EAAQGPQFAR HVLVSCGLAL GAQVTTLSRA LQFPCLMSSE AYWEFKRALK EFIFLYGKKW
AASLPLLHLA FRASTTEATP FQVLTGGEMK LMEPVWWEMS RANIEGLKMD AFLLQLMREL
LDLHWRVAEK ASEKAENRRF KRESQENEWS VGDQVLLLSL PRNGSSAKWM GPFYIGDRLS
LSLYRVWGFP VPDKLGCVYP SSLMKAFPKH DTPLSLDVEQ
