SMAL1_RAT
ID SMAL1_RAT Reviewed; 910 AA.
AC B4F769;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 AltName: Full=Sucrose nonfermenting protein 2-like 1;
GN Name=Smarcal1; Synonyms=Harp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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: 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 -!- PTM: DNA damage-regulated phosphorylation by kinases that may include
CC ATM, ATR and PRKDC. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SMARCAL1
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00800}.
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DR EMBL; CH474004; EDL75309.1; -; Genomic_DNA.
DR EMBL; BC168154; AAI68154.1; -; mRNA.
DR RefSeq; NP_001101692.1; NM_001108222.1.
DR RefSeq; XP_006245274.1; XM_006245212.3.
DR RefSeq; XP_006245275.1; XM_006245213.3.
DR RefSeq; XP_008765457.1; XM_008767235.1.
DR RefSeq; XP_017451963.1; XM_017596474.1.
DR AlphaFoldDB; B4F769; -.
DR SMR; B4F769; -.
DR BioGRID; 261356; 1.
DR STRING; 10116.ENSRNOP00000022459; -.
DR PhosphoSitePlus; B4F769; -.
DR PaxDb; B4F769; -.
DR PeptideAtlas; B4F769; -.
DR PRIDE; B4F769; -.
DR Ensembl; ENSRNOT00000022459; ENSRNOP00000022459; ENSRNOG00000016503.
DR GeneID; 316477; -.
DR KEGG; rno:316477; -.
DR UCSC; RGD:1306134; rat.
DR CTD; 50485; -.
DR RGD; 1306134; Smarcal1.
DR eggNOG; KOG1000; Eukaryota.
DR GeneTree; ENSGT00940000157608; -.
DR HOGENOM; CLU_000315_33_1_1; -.
DR InParanoid; B4F769; -.
DR OMA; QEEMPTA; -.
DR OrthoDB; 1082831at2759; -.
DR PhylomeDB; B4F769; -.
DR TreeFam; TF106474; -.
DR PRO; PR:B4F769; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Proteomes; UP000234681; Chromosome 9.
DR Bgee; ENSRNOG00000016503; Expressed in skeletal muscle tissue and 20 other tissues.
DR Genevisible; B4F769; RN.
DR GO; GO:0005662; C:DNA replication factor A complex; IEA:Ensembl.
DR GO; GO:0043596; C:nuclear replication fork; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; ISO:RGD.
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:RGD.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Coiled coil; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; 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_0000361532"
FT DOMAIN 198..268
FT /note="HARP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 284..355
FT /note="HARP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 402..557
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 672..825
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..30
FT /note="Mediates interaction with RPA2"
FT /evidence="ECO:0000250"
FT REGION 865..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3..28
FT /evidence="ECO:0000255"
FT MOTIF 506..509
FT /note="DESH box"
FT COMPBIAS 7..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 415..422
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 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZC9"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZC9"
SQ SEQUENCE 910 AA; 101212 MW; A683FBA1FC495F5F CRC64;
MSLPLTEEQR KKIEENRQKA LARRAEKLWA EQPQSTASGS SAARPSQCKQ NSLLNLPAEP
SKPEGHATIS KGQNLNNSLP AAQRPHSSPC FQPSTAEEAK GLWKSEGKMS AACPNPSPPE
VSNQQLLGSK SSEGHPQATQ DTAASCPRPF PRDPKLEAKA GRPSTSGQSI SDTFYALGEK
TPKTDGRPAK ALQTSPQKAS CLRGMCLRTG DRFRVKIGYN KELIEVFKSL PSRRYDSFTK
TWDFSMSDYR ALMKAVERLS TVSLQPLEEV DGTGGQTSLP SAPSLTFVTG RCMLISRARF
EVDIGYSEVV IALFKQMESR NYDPKTRKWN FLLEEHNKLI ARSRELKQVQ LDPLPKTLTL
AFASQLEKTS LQSKADVPEA DLSGVDAKLV SNLMPFQREG VSFAISKRGR LLLADDMGLG
KTIQAICIAA FYRKEWPLLV VVPSSVRFTW EQAFLRWLPS LSPEDINVVV TGKGRLTAGL
VNIVSFDLLS KLEKQLKTPF KVVIIDESHF LKNIKTARCR AAVPILKVAK RVILLSGTPA
MSRPAELYTQ IIAVKPTFFP QFHAFGLRYC DAKRLPWGWD YSGSSNLGEL KLLLEEAVML
RRLKSDVLSQ LPAKQRKMVV VNPGRISTRA KAALDAAAKE MTKDKTKQQQ KEALLVFFNR
TAEAKIPCVI EYILDLLESG REKFLVFAHH KVLLDAIAKE LERKNVQHIR IDGSTPSADR
EDLCQQFQLS KGHTVAVLSI TAANMGLTFS SADLVVFAEL FWNPGVLIQA EDRVHRIGQT
NSVGIHYLVA KGTADDYLWP LIQEKIKVLG EAGLSETNFS EMTEATDYLY KDPKQKTIYS
LFQQSFEDDG NDMEFLEAAE SFELGSTSGT SGNSSQELGD ITDENALADS PPKKRRFEFF
DNWDSFTSPF
