SMAL1_MOUSE
ID SMAL1_MOUSE Reviewed; 910 AA.
AC Q8BJL0; Q3TEQ9; Q3U4W0; Q3V3A8; Q8BVK7; Q8BXW4; Q8K309; Q9EQK8; Q9QYC4;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1;
DE EC=3.6.4.-;
DE AltName: Full=HepA-related protein;
DE Short=mharp;
DE AltName: Full=Sucrose nonfermenting protein 2-like 1;
GN Name=Smarcal1; Synonyms=Harp;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RX PubMed=10857751; DOI=10.1006/geno.2000.6174;
RA Coleman M.A., Eisen J.A., Mohrenweiser H.W.;
RT "Cloning and characterization of HARP/SMARCAL1: a prokaryotic HepA-related
RT SNF2 helicase protein from human and mouse.";
RL Genomics 65:274-282(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Embryo, Testis, and Thymus;
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 MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
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: ATP-dependent annealing helicase that binds selectively to
CC fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the
CC stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably
CC bound by replication protein A (RPA). Acts throughout the genome to
CC reanneal stably unwound DNA, performing the opposite reaction of many
CC enzymes, such as helicases and polymerases, that unwind DNA. May play
CC an important role in DNA damage response by acting at stalled
CC replication forks (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RPA2; the interaction is direct and mediates
CC the recruitment by the RPA complex of SMARCAL1 to sites of DNA damage.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Recruited to damaged
CC DNA regions. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BJL0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BJL0-2; Sequence=VSP_012919, VSP_012920;
CC Name=3;
CC IsoId=Q8BJL0-3; Sequence=VSP_036218, VSP_036219;
CC Name=4;
CC IsoId=Q8BJL0-4; Sequence=VSP_036216, VSP_036217;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with high levels in brain,
CC heart, kidney, liver and testis. {ECO:0000269|PubMed:10857751}.
CC -!- PTM: DNA damage-regulated phosphorylation by kinases that may include
CC ATM, ATR and PRKDC. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SMARCAL1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00800}.
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DR EMBL; AF088884; AAF24985.1; -; mRNA.
DR EMBL; AF209773; AAG47648.1; -; Genomic_DNA.
DR EMBL; AK042332; BAE20630.1; -; mRNA.
DR EMBL; AK043129; BAC31469.1; -; mRNA.
DR EMBL; AK077878; BAC37047.1; -; mRNA.
DR EMBL; AK083488; BAC38933.1; -; mRNA.
DR EMBL; AK154020; BAE32320.1; -; mRNA.
DR EMBL; AK169465; BAE41189.1; -; mRNA.
DR EMBL; BC029078; AAH29078.1; -; mRNA.
DR CCDS; CCDS35609.1; -. [Q8BJL0-1]
DR RefSeq; NP_061287.2; NM_018817.2. [Q8BJL0-1]
DR RefSeq; XP_006496204.1; XM_006496141.3. [Q8BJL0-1]
DR RefSeq; XP_006496205.1; XM_006496142.3. [Q8BJL0-1]
DR RefSeq; XP_006496206.1; XM_006496143.3. [Q8BJL0-1]
DR RefSeq; XP_006496207.1; XM_006496144.1. [Q8BJL0-1]
DR PDB; 4O66; X-ray; 1.90 A; A/B/C/D=197-268.
DR PDBsum; 4O66; -.
DR AlphaFoldDB; Q8BJL0; -.
DR SMR; Q8BJL0; -.
DR BioGRID; 207633; 7.
DR STRING; 10090.ENSMUSP00000047589; -.
DR iPTMnet; Q8BJL0; -.
DR PhosphoSitePlus; Q8BJL0; -.
DR EPD; Q8BJL0; -.
DR MaxQB; Q8BJL0; -.
DR PaxDb; Q8BJL0; -.
DR PeptideAtlas; Q8BJL0; -.
DR PRIDE; Q8BJL0; -.
DR ProteomicsDB; 261515; -. [Q8BJL0-1]
DR ProteomicsDB; 261516; -. [Q8BJL0-2]
DR ProteomicsDB; 261517; -. [Q8BJL0-3]
DR ProteomicsDB; 261518; -. [Q8BJL0-4]
DR Antibodypedia; 34237; 200 antibodies from 31 providers.
DR DNASU; 54380; -.
DR Ensembl; ENSMUST00000047615; ENSMUSP00000047589; ENSMUSG00000039354. [Q8BJL0-1]
DR Ensembl; ENSMUST00000152225; ENSMUSP00000137833; ENSMUSG00000039354. [Q8BJL0-1]
DR GeneID; 54380; -.
DR KEGG; mmu:54380; -.
DR UCSC; uc007bko.2; mouse. [Q8BJL0-4]
DR UCSC; uc007bkq.2; mouse. [Q8BJL0-3]
DR UCSC; uc007bkr.2; mouse. [Q8BJL0-2]
DR UCSC; uc007bks.2; mouse. [Q8BJL0-1]
DR CTD; 50485; -.
DR MGI; MGI:1859183; Smarcal1.
DR VEuPathDB; HostDB:ENSMUSG00000039354; -.
DR eggNOG; KOG1000; Eukaryota.
DR GeneTree; ENSGT00940000157608; -.
DR HOGENOM; CLU_000315_33_1_1; -.
DR InParanoid; Q8BJL0; -.
DR OMA; QEEMPTA; -.
DR OrthoDB; 1082831at2759; -.
DR PhylomeDB; Q8BJL0; -.
DR TreeFam; TF106474; -.
DR BioGRID-ORCS; 54380; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Smarcal1; mouse.
DR PRO; PR:Q8BJL0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BJL0; protein.
DR Bgee; ENSMUSG00000039354; Expressed in primary oocyte and 253 other tissues.
DR ExpressionAtlas; Q8BJL0; baseline and differential.
DR Genevisible; Q8BJL0; MM.
DR GO; GO:0005662; C:DNA replication factor A complex; ISO:MGI.
DR GO; GO:0043596; C:nuclear replication fork; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:MGI.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; ISS:UniProtKB.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR GO; GO:0048478; P:replication fork protection; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030101; HARP(SMARCAL1).
DR InterPro; IPR010003; HARP_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45766:SF3; PTHR45766:SF3; 2.
DR Pfam; PF07443; HARP; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51467; HARP; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Coiled coil;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9NZC9"
FT CHAIN 2..910
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A-like protein 1"
FT /id="PRO_0000074349"
FT DOMAIN 199..269
FT /note="HARP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 286..357
FT /note="HARP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 404..559
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 674..827
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..29
FT /note="Mediates interaction with RPA2"
FT /evidence="ECO:0000250"
FT REGION 868..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3..34
FT /evidence="ECO:0000255"
FT MOTIF 508..511
FT /note="DESH box"
FT COMPBIAS 7..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 417..424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZC9"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZC9"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZC9"
FT VAR_SEQ 404
FT /note="S -> R (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036216"
FT VAR_SEQ 405..910
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036217"
FT VAR_SEQ 508..574
FT /note="DESHFLKNIKTARCRAAVPILKVAKRVILLSGTPAMSRPAELYTQIIAVKPT
FT FFPQFHAFGLRYCDA -> VSNGIALKYFVCLDTRKGSTDLGICVLLGPLWALRREGNR
FT NRCLSFIENDFFIPFLKQPLSLCARLS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036218"
FT VAR_SEQ 575..910
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036219"
FT VAR_SEQ 769..788
FT /note="LIQAEDRVHRIGQTNSVSIH -> GNVARVPLGMPRAEKYKIRK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012919"
FT VAR_SEQ 789..910
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012920"
FT CONFLICT 35
FT /note="A -> T (in Ref. 3; AAH29078)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="F -> L (in Ref. 3; AAH29078)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="K -> N (in Ref. 2; BAE32320)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="K -> R (in Ref. 2; BAC31469)"
FT /evidence="ECO:0000305"
FT CONFLICT 717..725
FT /note="Missing (in Ref. 1; AAG47648)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="T -> R (in Ref. 1; AAF24985)"
FT /evidence="ECO:0000305"
FT CONFLICT 719..721
FT /note="SAD -> TRA (in Ref. 1; AAF24985)"
FT /evidence="ECO:0000305"
FT CONFLICT 724..725
FT /note="AQ -> LK (in Ref. 1; AAF24985)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="T -> P (in Ref. 1; AAF24985)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="D -> A (in Ref. 1; AAF24985)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="Missing (in Ref. 1; AAG47648)"
FT /evidence="ECO:0000305"
FT CONFLICT 866..868
FT /note="LGS -> IKN (in Ref. 1; AAF24985)"
FT /evidence="ECO:0000305"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:4O66"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:4O66"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:4O66"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:4O66"
FT TURN 238..241
FT /evidence="ECO:0007829|PDB:4O66"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4O66"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:4O66"
FT HELIX 250..257
FT /evidence="ECO:0007829|PDB:4O66"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:4O66"
SQ SEQUENCE 910 AA; 100840 MW; F6B28F847BD6FC18 CRC64;
MSLPLTEEQR KKIEENRQKA LARRAEKLSE QPQSAASGSS AAGPSQSKQG SLLNLLAEPS
KPVGHASIFK QQNLSNSFPT DQRPHSSRCS QPSPAEETTG LWKTQGEMST ACPKPNPSPP
GASNQPLLGY KSSEGQPQAT WDTGASSSGP FPRDPELEAK AARPSTSRQS ISDSFYVLGG
KTPRTEGRPP NILQTTPQNT GFLRGACIKT GDRFRVKIGY NQELIAVFKS LPSRHYDSFT
KTWDFSMSDY RALMKAVERL STVSLKPLDE AGGSVGGQTS LPSAPSLTFV TGKCMLISRV
RFEVDIGYSE AVIGLFKQME SRSYDIKTRK WSFLLEEHNK LIARSRELKQ VQLDPLPKTV
TLAFASQLEK TSPKLKADVP EADLSGVDAK LVSSLMPFQR EGVSFAISKR GRLLLADDMG
LGKTVQAICI AAFYRKEWPL LVVVPSSVRF TWEQAFLRWL PSLSPENINV VVTGKGRLTA
GLVNIVSFDL LCKLERQLKT PFKVVIIDES HFLKNIKTAR CRAAVPILKV AKRVILLSGT
PAMSRPAELY TQIIAVKPTF FPQFHAFGLR YCDAKRLPWG WDYSGSSNLG ELKLLLEEAI
MLRRLKSDVL SQLPAKQRKM VVVNPGRISS RAKAALDAAA KEMTKDKTKQ QQKEALLVFF
NRTAEAKIPC VVEYILDLLD SGREKFLVFA HHKVILDAVA KELERKNVQH IRIDGSTPSA
DREAQCQRFQ LSKGHTVALL SITAANMGLT FSTADLVVFA ELFWNPGVLI QAEDRVHRIG
QTNSVSIHYL VAKGTADDYL WPLIQEKIKV LGEAGLSETN FSEMTEATDY VHKDPKQKTI
YDLFQQSFED DGNDMEFLEA AESFELGSTS GTSGNISQDL GDLLDEDEGS PPKKSRFEFF
DNWDSFSSPF
