KIN17_MOUSE
ID KIN17_MOUSE Reviewed; 391 AA.
AC Q8K339; Q9CV58;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DNA/RNA-binding protein KIN17;
DE AltName: Full=Binding to curved DNA;
DE AltName: Full=KIN, antigenic determinant of recA protein;
GN Name=Kin {ECO:0000312|MGI:MGI:96676}; Synonyms=Btcd, Kin17;
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] {ECO:0000305, ECO:0000312|PIR:S18666}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic brain {ECO:0000269|PubMed:1923796};
RX PubMed=1923796; DOI=10.1093/nar/19.19.5117;
RA Angulo J.F., Rouer E., Mazin A., Mattei M.-G., Tissier A., Horellou P.,
RA Benarous R., Devoret R.;
RT "Identification and expression of the cDNA of KIN17, a zinc-finger gene
RT located on mouse chromosome 2, encoding a new DNA-binding protein.";
RL Nucleic Acids Res. 19:5117-5123(1991).
RN [2] {ECO:0000312|EMBL:BAE39778.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB26281.3}, and
RC DBA/2J {ECO:0000312|EMBL:BAE39778.1};
RC TISSUE=Tongue {ECO:0000312|EMBL:BAB26281.3};
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 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 [4] {ECO:0000312|EMBL:AAH28860.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH28860.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH28860.1};
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 [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-273.
RX PubMed=1715759; DOI=10.1016/0300-9084(91)90210-r;
RA Angulo J.F., Rouer E., Benarous R., Devoret R.;
RT "Identification of a mouse cDNA fragment whose expressed polypeptide reacts
RT with anti-recA antibodies.";
RL Biochimie 73:251-256(1991).
RN [6]
RP FUNCTION.
RX PubMed=8670903; DOI=10.1002/j.1460-2075.1996.tb00772.x;
RA Timchenko T., Bailone A., Devoret R.;
RT "Btcd, a mouse protein that binds to curved DNA, can substitute in
RT Escherichia coli for H-NS, a bacterial nucleoid protein.";
RL EMBO J. 15:3986-3992(1996).
RN [7] {ECO:0000305}
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8954809; DOI=10.1006/geno.1996.0623;
RA Tissier A., Kannouche P., Mauffrey P., Allemand I., Frelat G., Devoret R.,
RA Angulo J.F.;
RT "Molecular cloning and characterization of the mouse Kin17 gene coding for
RT a Zn-finger protein that preferentially recognizes bent DNA.";
RL Genomics 38:238-242(1996).
RN [8] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15252136; DOI=10.1242/jcs.01226;
RA Pinon-Lataillade G., Masson C., Bernardino-Sgherri J., Henriot V.,
RA Mauffrey P., Frobert Y., Araneda S., Angulo J.F.;
RT "KIN17 encodes an RNA-binding protein and is expressed during mouse
RT spermatogenesis.";
RL J. Cell Sci. 117:3691-3702(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 DNA replication and the cellular response to DNA
CC damage. May participate in DNA replication factories and create a
CC bridge between DNA replication and repair mediated by high molecular
CC weight complexes. May play a role in illegitimate recombination and
CC regulation of gene expression. May participate in mRNA processing.
CC Binds, in vitro, to double-stranded DNA. Also shown to bind
CC preferentially to curved DNA in vitro and in vivo. Binds via its C-
CC terminal domain to RNA in vitro. {ECO:0000250|UniProtKB:O60870,
CC ECO:0000269|PubMed:15252136, ECO:0000269|PubMed:1923796,
CC ECO:0000269|PubMed:8670903, ECO:0000269|PubMed:8954809}.
CC -!- SUBUNIT: Associated with DNA polymerase alpha, RFC1 and cyclin A, in
CC multiprotein DNA replication complexes. Also associates with
CC replication origins at the G1/S phase boundary and throughout the S
CC phase in vivo (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15252136}. Cytoplasm
CC {ECO:0000269|PubMed:15252136}. Note=During S phase, strongly associated
CC with the nuclear matrix, and to chromosomal DNA in the presence of DNA
CC damage. Also shows cytoplasmic localization in elongated spermatids.
CC {ECO:0000250|UniProtKB:O60870, ECO:0000269|PubMed:15252136}.
CC -!- TISSUE SPECIFICITY: Highly expressed in transformed mouse AtT20
CC neuroendocrine cells. Expressed at a lower level in testis, kidney,
CC skeletal muscle, liver, lung, spleen, brain and heart and kidney. In
CC testis, expressed at much higher levels in proliferating cells than in
CC differentiating cells. Not detected in embryo.
CC {ECO:0000269|PubMed:15252136, ECO:0000269|PubMed:1923796,
CC ECO:0000269|PubMed:8954809}.
CC -!- DEVELOPMENTAL STAGE: In testis, expression almost doubled from day 5 to
CC days 17-22 postpartum (dpp) and then decreased by 28 dpp to reach a
CC stable level in adult testis. {ECO:0000269|PubMed:15252136}.
CC -!- DOMAIN: The C-terminal domain (268-393) is organized into 2 subdomains
CC that bear structural similarities to SH3-like domains. Both subdomains
CC adopt a similar 5-stranded beta-barrel-like fold and are connected to
CC each other by a short linker of 5 residues. The 5 beta-sheets are
CC packed at approximately right angles against each other. A highly
CC conserved groove formed at the interface between the 2 subdomains,
CC comprised of Lys residues 302 and 391 and other positively charged
CC residues, may possibly be the site of RNA-binding (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Recognized by antibodies directed against the RecA
CC protein. {ECO:0000269|PubMed:1715759, ECO:0000269|PubMed:1923796}.
CC -!- SIMILARITY: Belongs to the KIN17 family. {ECO:0000305}.
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DR EMBL; X58472; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK009429; BAB26281.3; -; mRNA.
DR EMBL; AK167740; BAE39778.1; -; mRNA.
DR EMBL; AL772367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028860; AAH28860.1; -; mRNA.
DR CCDS; CCDS15676.1; -.
DR PIR; S18666; S18666.
DR RefSeq; NP_079556.1; NM_025280.2.
DR AlphaFoldDB; Q8K339; -.
DR BMRB; Q8K339; -.
DR SMR; Q8K339; -.
DR IntAct; Q8K339; 1.
DR MINT; Q8K339; -.
DR STRING; 10090.ENSMUSP00000043614; -.
DR iPTMnet; Q8K339; -.
DR PhosphoSitePlus; Q8K339; -.
DR EPD; Q8K339; -.
DR MaxQB; Q8K339; -.
DR PaxDb; Q8K339; -.
DR PeptideAtlas; Q8K339; -.
DR PRIDE; Q8K339; -.
DR ProteomicsDB; 269220; -.
DR Antibodypedia; 4279; 119 antibodies from 27 providers.
DR DNASU; 16588; -.
DR Ensembl; ENSMUST00000042512; ENSMUSP00000043614; ENSMUSG00000037262.
DR GeneID; 16588; -.
DR KEGG; mmu:16588; -.
DR UCSC; uc008ihp.1; mouse.
DR CTD; 22944; -.
DR MGI; MGI:96676; Kin.
DR VEuPathDB; HostDB:ENSMUSG00000037262; -.
DR eggNOG; KOG2837; Eukaryota.
DR GeneTree; ENSGT00390000005903; -.
DR HOGENOM; CLU_030065_1_0_1; -.
DR InParanoid; Q8K339; -.
DR OMA; DKGHVHM; -.
DR OrthoDB; 1420569at2759; -.
DR PhylomeDB; Q8K339; -.
DR TreeFam; TF314393; -.
DR Reactome; R-MMU-8876725; Protein methylation.
DR BioGRID-ORCS; 16588; 23 hits in 107 CRISPR screens.
DR PRO; PR:Q8K339; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8K339; protein.
DR Bgee; ENSMUSG00000037262; Expressed in granulocyte and 249 other tissues.
DR Genevisible; Q8K339; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd13155; KOW_KIN17; 1.
DR Gene3D; 1.10.10.2030; -; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR InterPro; IPR019447; DNA/RNA-bd_Kin17_WH-like_dom.
DR InterPro; IPR037321; KIN17-like.
DR InterPro; IPR038254; KIN17_WH-like_sf.
DR InterPro; IPR041330; KN17_SH3.
DR InterPro; IPR041995; KOW_KIN17.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR12805; PTHR12805; 1.
DR Pfam; PF10357; Kin17_mid; 1.
DR Pfam; PF18131; KN17_SH3; 1.
DR SMART; SM01253; Kin17_mid; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA replication; DNA-binding; Metal-binding; Methylation; mRNA processing;
KW Nucleus; Reference proteome; RNA-binding; Stress response; Zinc;
KW Zinc-finger.
FT CHAIN 1..391
FT /note="DNA/RNA-binding protein KIN17"
FT /id="PRO_0000289135"
FT ZN_FING 28..50
FT /note="C2H2-type"
FT /evidence="ECO:0000255"
FT REGION 51..160
FT /note="Winged helix-turn-helix (wHTH)"
FT /evidence="ECO:0000250"
FT REGION 206..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..332
FT /note="C-terminal subdomain A"
FT /evidence="ECO:0000250|UniProtKB:O60870"
FT REGION 338..389
FT /note="C-terminal subdomain B"
FT /evidence="ECO:0000250|UniProtKB:O60870"
FT COILED 147..180
FT /evidence="ECO:0000255"
FT COILED 252..275
FT /evidence="ECO:0000255"
FT COMPBIAS 211..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="N6,N6,N6-trimethyllysine; by METTL22; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60870"
FT MOD_RES 135
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O60870"
SQ SEQUENCE 391 AA; 44722 MW; 955BC6A4FF4D3B6E CRC64;
MGKSDFLSPK AIANRIKSKG LQKLRWYCQM CQKQCRDENG FKCHCMSESH QRQLLLASEN
PQQFMDYFSE EFRNDFLELL RRRFGTKRVH NNIVYNEYIS HREHIHMNAT QWETLTDFTK
WLGREGLCKV DETPKGWYIQ YIDRDPETIR RQLELEKKKK QDLDDEEKTA KFIEEQVRRG
LEGKEQETPV FTELSRENEE EKVTFNLNKG AGGSAGATTS KSSSLGPSAL KLLGSAASGK
RKESSQSSAQ PAKKKKSALD EIMELEEEKK RTARTDAWLQ PGIVVKIITK KLGEKYHKKK
GVVKEVIDRY TAVVKMTDSG DRLKLDQTHL ETVIPAPGKR VLVLNGGYRG NEGTLESINE
KAFSATIVIE TGPLKGRRVE GIQYEDISKL A
