ID F111A_MOUSE Reviewed; 613 AA. AC Q9D2L9; Q3T9N2; Q8BLH2; Q8CI07; Q8VE75; Q9CU11; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 02-JUN-2021, entry version 125. DE RecName: Full=Serine protease FAM111A {ECO:0000305}; DE EC=3.4.21.- {ECO:0000250|UniProtKB:Q96PZ2}; GN Name=Fam111a {ECO:0000312|MGI:MGI:1915508}; 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]. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Embryo, Placenta, Skin, Spleen, and Stomach; 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]. RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor; 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). CC -!- FUNCTION: Single-stranded DNA-binding serine protease that mediates the CC proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during CC DNA synthesis, thereby playing a key role in maintaining genomic CC integrity. DPCs are highly toxic DNA lesions that interfere with CC essential chromatin transactions, such as replication and CC transcription, and which are induced by reactive agents, such as UV CC light or formaldehyde. Protects replication fork from stalling by CC removing DPCs, such as covalently trapped topoisomerase 1 (TOP1) CC adducts on DNA lesion, or poly(ADP-ribose) polymerase 1 (PARP1)-DNA CC complexes trapped by PARP inhibitors. Required for PCNA loading on CC replication sites. Promotes S-phase entry and DNA synthesis. CC {ECO:0000250|UniProtKB:Q96PZ2}. CC -!- SUBUNIT: Interacts (via PIP-box) with PCNA; this interaction is direct. CC {ECO:0000250|UniProtKB:Q96PZ2}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96PZ2}. CC Chromosome {ECO:0000250|UniProtKB:Q96PZ2}. Cytoplasm CC {ECO:0000250|UniProtKB:Q96PZ2}. Note=Mainly localizes to nucleus: CC colocalizes with PCNA on replication sites. CC {ECO:0000250|UniProtKB:Q96PZ2}. CC -!- DOMAIN: The PIP-box mediates the interaction with PCNA. CC {ECO:0000250|UniProtKB:Q96PZ2}. CC -!- PTM: Autocatalytically cleaved; autocatalytic cleavage takes place in CC trans. {ECO:0000250|UniProtKB:Q96PZ2}. CC -!- SIMILARITY: Belongs to the FAM111 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH38020.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK018830; BAB31452.3; -; mRNA. DR EMBL; AK019499; BAB31763.1; -; mRNA. DR EMBL; AK045189; BAC32254.1; -; mRNA. DR EMBL; AK172402; BAE42988.1; -; mRNA. DR EMBL; BC019638; AAH19638.1; -; mRNA. DR EMBL; BC038020; AAH38020.1; ALT_FRAME; mRNA. DR CCDS; CCDS29632.1; -. DR RefSeq; NP_001333474.1; NM_001346545.1. DR RefSeq; NP_080916.1; NM_026640.2. DR STRING; 10090.ENSMUSP00000119518; -. DR iPTMnet; Q9D2L9; -. DR PhosphoSitePlus; Q9D2L9; -. DR EPD; Q9D2L9; -. DR MaxQB; Q9D2L9; -. DR PaxDb; Q9D2L9; -. DR PRIDE; Q9D2L9; -. DR ProteomicsDB; 275813; -. DR Antibodypedia; 27720; 42 antibodies. DR DNASU; 107373; -. DR Ensembl; ENSMUST00000025595; ENSMUSP00000025595; ENSMUSG00000024691. DR Ensembl; ENSMUST00000144662; ENSMUSP00000119518; ENSMUSG00000024691. DR GeneID; 107373; -. DR KEGG; mmu:107373; -. DR UCSC; uc008guf.1; mouse. DR CTD; 63901; -. DR MGI; MGI:1915508; Fam111a. DR eggNOG; ENOG502QTFX; Eukaryota. DR GeneTree; ENSGT00390000005182; -. DR InParanoid; Q9D2L9; -. DR OrthoDB; 470902at2759; -. DR PhylomeDB; Q9D2L9; -. DR TreeFam; TF332538; -. DR BioGRID-ORCS; 107373; 1 hit in 52 CRISPR screens. DR ChiTaRS; Fam111a; mouse. DR PRO; PR:Q9D2L9; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; Q9D2L9; protein. DR Bgee; ENSMUSG00000024691; Expressed in granulocyte and 241 other tissues. DR ExpressionAtlas; Q9D2L9; baseline and differential. DR Genevisible; Q9D2L9; MM. DR GO; GO:0000785; C:chromatin; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0001650; C:fibrillar center; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB. DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB. DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI. DR GO; GO:0016540; P:protein autoprocessing; ISS:UniProtKB. DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB. DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB. DR InterPro; IPR009003; Peptidase_S1_PA. DR SUPFAM; SSF50494; SSF50494; 1. PE 2: Evidence at transcript level; KW Autocatalytic cleavage; Chromosome; Cytoplasm; DNA damage; DNA repair; KW DNA replication; DNA-binding; Hydrolase; Isopeptide bond; Nucleus; KW Phosphoprotein; Protease; Reference proteome; Ubl conjugation. FT CHAIN 1..613 FT /note="Serine protease FAM111A" FT /id="PRO_0000274408" FT REGION 1..72 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 15..61 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 383 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P06681" FT ACT_SITE 437 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:P06681" FT ACT_SITE 543 FT /note="Charge relay system" FT /evidence="ECO:0000250|UniProtKB:Q96PZ2" FT SITE 331..332 FT /note="Cleavage; by autolysis" FT /evidence="ECO:0000250|UniProtKB:Q96PZ2" FT MOD_RES 25 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96PZ2" FT CROSSLNK 19 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q96PZ2" FT CROSSLNK 29 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q96PZ2" FT CROSSLNK 62 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q96PZ2" FT CONFLICT 227..228 FT /note="CT -> RS (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 239..240 FT /note="ND -> GN (in Ref. 2; AAH19638)" FT /evidence="ECO:0000305" FT CONFLICT 243 FT /note="T -> S (in Ref. 2; AAH19638)" FT /evidence="ECO:0000305" FT CONFLICT 272 FT /note="V -> A (in Ref. 2; AAH19638)" FT /evidence="ECO:0000305" FT CONFLICT 282 FT /note="N -> K (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 293 FT /note="V -> M (in Ref. 2; AAH19638)" FT /evidence="ECO:0000305" FT CONFLICT 301 FT /note="E -> K (in Ref. 2; AAH19638)" FT /evidence="ECO:0000305" FT CONFLICT 304 FT /note="K -> E (in Ref. 2; AAH19638)" FT /evidence="ECO:0000305" FT CONFLICT 325 FT /note="K -> E (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 330 FT /note="H -> Q (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 335..336 FT /note="TR -> KS (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 342..346 FT /note="KVVKH -> TVHEN (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 342 FT /note="K -> Q (in Ref. 2; AAH19638)" FT /evidence="ECO:0000305" FT CONFLICT 352 FT /note="D -> A (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 356 FT /note="F -> Y (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 360 FT /note="N -> D (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 400 FT /note="N -> S (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 413..419 FT /note="EELLPTG -> KDFPLTK (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 435 FT /note="H -> D (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 456..459 FT /note="HRIR -> NGIG (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 463..464 FT /note="HS -> LG (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 463 FT /note="H -> P (in Ref. 2; AAH19638)" FT /evidence="ECO:0000305" FT CONFLICT 476 FT /note="E -> G (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 480..482 FT /note="IDC -> SDG (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 489 FT /note="S -> G (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 507 FT /note="F -> C (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 532 FT /note="V -> I (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 572 FT /note="N -> S (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 579 FT /note="I -> T (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 584..586 FT /note="DDH -> LAN (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 592 FT /note="Y -> H (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 599..600 FT /note="IS -> VF (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 604 FT /note="Q -> E (in Ref. 2; AAH19638)" FT /evidence="ECO:0000305" FT CONFLICT 605 FT /note="N -> D (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" FT CONFLICT 611..613 FT /note="IDF -> TDS (in Ref. 1; BAE42988)" FT /evidence="ECO:0000305" SQ SEQUENCE 613 AA; 69949 MW; F926114F705A639B CRC64; MSCKKRKSQI SFNPRKNKKI KDYFSQVPKE EQNDPNTVKV DSKKMPRDIT NTRDQRPLSP RKTRQDQTPP LNKKITVTLG VNSRKHKNMK YELTCRETSS LYAALNTLSA VREEVESQKG REMLVCGKEG IEGYLNLGMP VCCIPEGSHV VITFCQCKSK TQENKQFFES QDQASTNYVR FCIHAVGSKR KKILKCGELQ KEGNKLCVYG FKGETIRDTL RKDGRFCTFI ESDDWKLIND LDTIIENTQP VDELEGKLFQ VAAELPKNPR VVSVTQNSGS ENRNFHKLEE YIVNEYTTLK EEGKKLRAYI KEKSEKRKKK ASLFKVHKEH FGKMTRNSTP VKVVKHLSRV SDSVGFLWWN NNGNAGCATC FVFKELYILT CQHVIASIVG EGIDSSEWAN IISQCVKVTF DYEELLPTGD KFFMVKPWFE ISDKHLDYAV LELKENGQEV PAGLYHRIRP VPHSGLIYII GHPEGEKKSI DCCTVVPQSS RRKKCQENFQ AREEAGFCFS TSFIHMYTQR SFQEMLHNSD VVTYDTSFFG GSSGSPVFDS NGSLVAMHAA GITCTYQAGV SNIIEFGSIM ESIDDHMKQD KYKEWYNTIS GNVQNVEMLS IDF //