NYNRI_HUMAN
ID NYNRI_HUMAN Reviewed; 1898 AA.
AC Q9P2P1; Q6P153; Q86TR3; Q9HAC4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Protein NYNRIN;
DE AltName: Full=NYN domain and retroviral integrase catalytic domain-containing protein;
DE AltName: Full=Protein cousin of GIN1;
GN Name=NYNRIN; Synonyms=CGIN1, KIAA1305;
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] (ISOFORM 2).
RC TISSUE=Embryo;
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=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-487 (ISOFORM 1).
RC TISSUE=Eye;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-1898 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [5]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 226-731 (ISOFORM 1).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9P2P1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P2P1-2; Sequence=VSP_030237, VSP_030238, VSP_030239;
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=AAH65283.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AK021873; BAB13925.1; -; mRNA.
DR EMBL; AL132800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065283; AAH65283.1; ALT_SEQ; mRNA.
DR EMBL; AB037726; BAA92543.2; -; mRNA.
DR EMBL; BX248773; CAD66580.1; -; mRNA.
DR CCDS; CCDS45090.1; -. [Q9P2P1-1]
DR RefSeq; NP_079357.2; NM_025081.2. [Q9P2P1-1]
DR AlphaFoldDB; Q9P2P1; -.
DR BioGRID; 121584; 21.
DR IntAct; Q9P2P1; 7.
DR STRING; 9606.ENSP00000371994; -.
DR iPTMnet; Q9P2P1; -.
DR PhosphoSitePlus; Q9P2P1; -.
DR BioMuta; NYNRIN; -.
DR DMDM; 166218833; -.
DR EPD; Q9P2P1; -.
DR jPOST; Q9P2P1; -.
DR MassIVE; Q9P2P1; -.
DR MaxQB; Q9P2P1; -.
DR PaxDb; Q9P2P1; -.
DR PeptideAtlas; Q9P2P1; -.
DR PRIDE; Q9P2P1; -.
DR ProteomicsDB; 83872; -. [Q9P2P1-1]
DR ProteomicsDB; 83873; -. [Q9P2P1-2]
DR Antibodypedia; 57476; 12 antibodies from 7 providers.
DR DNASU; 57523; -.
DR Ensembl; ENST00000382554.4; ENSP00000371994.3; ENSG00000205978.6. [Q9P2P1-1]
DR GeneID; 57523; -.
DR KEGG; hsa:57523; -.
DR MANE-Select; ENST00000382554.4; ENSP00000371994.3; NM_025081.3; NP_079357.2.
DR UCSC; uc001wpf.4; human. [Q9P2P1-1]
DR CTD; 57523; -.
DR DisGeNET; 57523; -.
DR GeneCards; NYNRIN; -.
DR HGNC; HGNC:20165; NYNRIN.
DR HPA; ENSG00000205978; Low tissue specificity.
DR neXtProt; NX_Q9P2P1; -.
DR OpenTargets; ENSG00000205978; -.
DR PharmGKB; PA165479228; -.
DR VEuPathDB; HostDB:ENSG00000205978; -.
DR eggNOG; KOG0017; Eukaryota.
DR eggNOG; KOG3740; Eukaryota.
DR GeneTree; ENSGT00940000161519; -.
DR HOGENOM; CLU_235862_0_0_1; -.
DR InParanoid; Q9P2P1; -.
DR OMA; THMAVAQ; -.
DR OrthoDB; 583605at2759; -.
DR PhylomeDB; Q9P2P1; -.
DR TreeFam; TF351195; -.
DR PathwayCommons; Q9P2P1; -.
DR SignaLink; Q9P2P1; -.
DR BioGRID-ORCS; 57523; 20 hits in 1071 CRISPR screens.
DR GenomeRNAi; 57523; -.
DR Pharos; Q9P2P1; Tdark.
DR PRO; PR:Q9P2P1; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9P2P1; protein.
DR Bgee; ENSG00000205978; Expressed in right hemisphere of cerebellum and 129 other tissues.
DR Genevisible; Q9P2P1; HS.
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:0006281; P:DNA repair; IEA:UniProt.
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 Alternative splicing; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1898
FT /note="Protein NYNRIN"
FT /id="PRO_0000314174"
FT TRANSMEM 1372..1392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1408..1428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 792..942
FT /note="RNase NYN"
FT /evidence="ECO:0000255"
FT DOMAIN 1304..1450
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 1609..1774
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT REGION 289..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..1471
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030237"
FT VAR_SEQ 1606..1621
FT /note="WPLRSTAPWSNLQIEV -> ASVLRGQGVCNRSGTR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030238"
FT VAR_SEQ 1622..1898
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030239"
FT VARIANT 457
FT /note="T -> M (in dbSNP:rs12437434)"
FT /id="VAR_037857"
FT VARIANT 659
FT /note="A -> V (in dbSNP:rs8008203)"
FT /id="VAR_037858"
FT VARIANT 978
FT /note="A -> T (in dbSNP:rs8017377)"
FT /id="VAR_037859"
FT VARIANT 997
FT /note="E -> K (in dbSNP:rs3742518)"
FT /id="VAR_037860"
FT VARIANT 1551
FT /note="I -> V (in dbSNP:rs17103672)"
FT /id="VAR_037861"
FT CONFLICT 1475
FT /note="R -> G (in Ref. 1; BAB13925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1898 AA; 208366 MW; 081533041B25CA08 CRC64;
MLLSGGDPPA QEWFMVQTKS KPRVQRQRLQ VQRIFRVKLN AFQSRPDTPY FWLQLEGPRE
NMGKAKEYLK GLCSPELWKE VRYPPILHCA FLGAQGLFLD CLCWSTLAYL VPGPPGSLMV
GGLTESFIMT QNWLEELVGR LRWGPAPLLT PRGIWEAEVT RAFGALVWIR GDQHAGDLLQ
LPPAVQELLL SLVRDAAGKE DIIEWLSRFG ISDSHSDPEV LICPPQQQKE APAMVSVGES
PGPFVDMGTL QNRGPENSKR LSSLGATGSL ITAQSTPQEA ANQLVRVGSN NQDGMDSAQE
EGTVQATSSQ DSTNHTQALL KQRQVQKIED KLLFQPPVSA LGVCPPWKAW TPGPAFGPLW
PGAIAATFWR INELHSLHLA WLLSQACFNF PFWQRPLGPI QLKLPGQNPL PLNLEWKQKE
LAPLPSAESP AGRPDGGLGG EAALQNCPRP EISPKVTSLL VVPGSSDVKD KVSSDLPQIG
PPLTSTPQLQ AGGEPGDQGS MQLDFKGLEE GPAPVLPTGQ GKPVAQGGLT DQSVPGAQTV
PETLKVPMAA AVPKAENPSR TQVPSAAPKL PTSRMMLAVH TEPAAPEVPL APTKPTAQLM
ATAQKTVVNQ PVLVAQVEPT TPKTPQAQKM PVAKTSPAGP KTPKAQAGPA ATVSKAPAAS
KAPAAPKVPV TPRVSRAPKT PAAQKVPTDA GPTLDVARLL SEVQPTSRAS VSLLKGQGQA
GRQGPQSSGT LALSSKHQFQ MEGLLGAWEG APRQPPRHLQ ANSTVTSFQR YHEALNTPFE
LNLSGEPGNQ GLRRVVIDGS SVAMVHGLQH FFSCRGIAMA VQFFWNRGHR EVTVFVPTWQ
LKKNRRVRES HFLTKLHSLK MLSITPSQLE NGKKITTYDY RFMVKLAEET DGIIVTNEQI
HILMNSSKKL MVKDRLLPFT FAGNLFMVPD DPLGRDGPTL DEFLKKPNRL DTDIGNFLKV
WKTLPPSSAS VTELSDDADS GPLESLPNME EVREEKEERQ DEEQRQGQGT QKAAEEDDLD
SSLASVFRVE CPSLSEEILR CLSLHDPPDG ALDIDLLPGA ASPYLGIPWD GKAPCQQVLA
HLAQLTIPSN FTALSFFMGF MDSHRDAIPD YEALVGPLHS LLKQKPDWQW DQEHEEAFLA
LKRALVSALC LMAPNSQLPF RLEVTVSHVA LTAILHQEHS GRKHPIAYTS KPLLPDEESQ
GPQSGGDSPY AVAWALKHFS RCIGDTPVVL DLSYASRTTA DPEVREGRRV SKAWLIRWSL
LVQDKGKRAL ELALLQGLLG ENRLLTPAAS MPRFFQVLPP FSDLSTFVCI HMSGYCFYRE
DEWCAGFGLY VLSPTSPPVS LSFSCSPYTP TYAHLAAVAC GLERFGQSPL PVVFLTHCNW
IFSLLWELLP LWRARGFLSS DGAPLPHPSL LSYIISLTSG LSSLPFIYRT SYRGSLFAVT
VDTLAKQGAQ GGGQWWSLPK DVPAPTVSPH AMGKRPNLLA LQLSDSTLAD IIARLQAGQK
LSGSSPFSSA FNSLSLDKES GLLMFKGDKK PRVWVVPTQL RRDLIFSVHD IPLGAHQRPE
ETYKKLRLLG WWPGMQEHVK DYCRSCLFCI PRNLIGSELK VIESPWPLRS TAPWSNLQIE
VVGPVTISEE GHKHVLIVAD PNTRWVEAFP LKPYTHTAVA QVLLQHVFAR WGVPVRLEAA
QGPQFARHVL VSCGLALGAQ VASLSRDLQF PCLTSSGAYW EFKRALKEFI FLHGKKWAAS
LPLLHLAFRA SSTDATPFKV LTGGESRLTE PLWWEMSSAN IEGLKMDVFL LQLVGELLEL
HWRVADKASE KAENRRFKRE SQEKEWNVGD QVLLLSLPRN GSSAKWVGPF YIGDRLSLSL
YRIWGFPTPE KLGCIYPSSL MKAFAKSGTP LSFKVLEQ
