F111A_MOUSE
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 03-AUG-2022, entry version 129.
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};
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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 AlphaFoldDB; Q9D2L9; -.
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; 48 antibodies from 12 providers.
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 VEuPathDB; HostDB:ENSMUSG00000024691; -.
DR eggNOG; ENOG502QTFX; Eukaryota.
DR GeneTree; ENSGT00390000005182; -.
DR InParanoid; Q9D2L9; -.
DR OMA; YIHAIGK; -.
DR OrthoDB; 470902at2759; -.
DR PhylomeDB; Q9D2L9; -.
DR TreeFam; TF332538; -.
DR BioGRID-ORCS; 107373; 1 hit in 73 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 210 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 Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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
