SMAL1_BOVIN
ID SMAL1_BOVIN Reviewed; 940 AA.
AC Q9TTA5; F1MDP3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 03-AUG-2022, entry version 130.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=10713074; DOI=10.1074/jbc.275.11.7648;
RA Muthuswami R., Truman P.A., Mesner L.D., Hockensmith J.W.;
RT "A eukaryotic SWI2/SNF2 domain, an exquisite detector of double-stranded to
RT single-stranded DNA transition elements.";
RL J. Biol. Chem. 275:7648-7655(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [3]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PHYLOGENY.
RX PubMed=19393058; DOI=10.1186/1471-2164-10-183;
RA Uzun A., Rodriguez-Osorio N., Kaya A., Wang H., Parrish J.J., Ilyin V.A.,
RA Memili E.;
RT "Functional genomics of HMGN3a and SMARCAL1 in early mammalian
RT embryogenesis.";
RL BMC Genomics 10:183-183(2009).
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 -!- TISSUE SPECIFICITY: Expressed in mature oocytes, 2-4 cell stage embryos
CC and 8-16 cell stage embryos. Expressed at lower levels in morulae and
CC blastocysts. {ECO:0000269|PubMed:19393058}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early embryogenesis.
CC {ECO:0000269|PubMed:19393058}.
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; AF173643; AAF22285.1; -; mRNA.
DR EMBL; DAAA02005900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_788839.1; NM_176666.1.
DR AlphaFoldDB; Q9TTA5; -.
DR SMR; Q9TTA5; -.
DR STRING; 9913.ENSBTAP00000005013; -.
DR PaxDb; Q9TTA5; -.
DR PRIDE; Q9TTA5; -.
DR GeneID; 338072; -.
DR KEGG; bta:338072; -.
DR CTD; 50485; -.
DR eggNOG; KOG1000; Eukaryota.
DR HOGENOM; CLU_000315_33_1_1; -.
DR InParanoid; Q9TTA5; -.
DR OrthoDB; 1082831at2759; -.
DR TreeFam; TF106474; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0043596; C:nuclear replication fork; IBA:GO_Central.
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: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: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..940
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A-like protein 1"
FT /id="PRO_0000074347"
FT DOMAIN 229..299
FT /note="HARP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 325..396
FT /note="HARP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00800"
FT DOMAIN 442..597
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 708..864
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..36
FT /note="Mediates interaction with RPA2"
FT /evidence="ECO:0000250"
FT REGION 662..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 18..40
FT /evidence="ECO:0000255"
FT MOTIF 546..549
FT /note="DESH box"
FT COMPBIAS 18..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 455..462
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 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZC9"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZC9"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZC9"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZC9"
FT CONFLICT 17
FT /note="G -> GK (in Ref. 1; AAF22285)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="S -> P (in Ref. 1; AAF22285)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="P -> L (in Ref. 1; AAF22285)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="A -> T (in Ref. 1; AAF22285)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="A -> R (in Ref. 1; AAF22285)"
FT /evidence="ECO:0000305"
FT CONFLICT 196..197
FT /note="MA -> IG (in Ref. 1; AAF22285)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="L -> P (in Ref. 1; AAF22285)"
FT /evidence="ECO:0000305"
FT CONFLICT 558..560
FT /note="RCR -> VC (in Ref. 1; AAF22285)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="A -> P (in Ref. 1; AAF22285)"
FT /evidence="ECO:0000305"
FT CONFLICT 667
FT /note="T -> M (in Ref. 1; AAF22285)"
FT /evidence="ECO:0000305"
FT CONFLICT 678..679
FT /note="PR -> AKE (in Ref. 1; AAF22285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 940 AA; 104776 MW; AB29A63444B23C95 CRC64;
MSISPLKCPC LLQRSRGKIE ANRQKALARR AEKLLAEQHQ KPAQSKQGPS QNLPRDPSKS
GSHGIFFKQQ NPSSSSHGDQ RPQNPHSFSP NTSEQAKGMW QRPEEMPTAC PSYRPPNQVT
VAGISPPLAN SPPGVPSQQL WGCELGQGHP QASLETQSTP FANTTHEPLA KVKNFQETAA
SSCGQPPRDP ELEARMARPS TSGQNISGSV MPRTEGRLQQ KAGTPLHRVV GSQQGRCIRN
GERFQVKIGY NEALIAVFKS LPSRSYDPAT KTWNFSMTDY GPLMKAAQRL PGITLQPLEG
AEGHMESPST SSGIIAKTGL PAAPSLAFVK GQCVLISRAR FEADISYSED LIALFKQMDS
RKYDVKTRKW SFLLEEYSKL MERVRGLPQV QLDPLPKTLT LFRAQLQKTS LSPVADIPEA
DLSRVDSKLV SSLLPFQRAG VNFAIAQRGR LLLADDMGLG KTIQAICIAA YYRKEWPLLV
VVPSSVRFTW EQAFCRWLPS LNPLDINVVV TGKDRLTDGL VNIVSFDLLS KLEKQLKPPF
KVVIIDESHF LKNIKTARCR AAMPLLKVAK RVILLSGTPA MSRPAELYTQ ILAVRPTFFP
QFHAFGLRYC GAKRQPWGWD YSGSSNLGEL KLLLEEAVML RRLKGDVLSQ LPAKQARWWW
SPQARSTPGP EPPWMPPPRM TTKDKTKQQQ KEALILFFNR TAEAKIPSII EYILDLLESG
REKFLVFAHH KVVLDAITKE LERKRVQHIR IDGSTSSADR ETSASSFSCP RALRGVLSIT
AANMGLTFSS ADLVVFGELF WNPGVLMQAE DRVHRIGQLS SVSIHYLVAR GTADDYLWPL
IQEKIKVLGE AGLSETNFSE MTEATDYFSK DSKQQKIYNL FQKSFEEDGN DMELLEAAES
FDPGSQDTGD KLDESTLTGS PVKKKRFEFF DNWDSFTSPL
