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   27-MAR-2024, entry version 157.
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;
RC   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}.
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; 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; 10090-ENSMUSP00000047589; -.
DR   PeptideAtlas; Q8BJL0; -.
DR   ProteomicsDB; 261515; -. [Q8BJL0-1]
DR   ProteomicsDB; 261516; -. [Q8BJL0-2]
DR   ProteomicsDB; 261517; -. [Q8BJL0-3]
DR   ProteomicsDB; 261518; -. [Q8BJL0-4]
DR   Pumba; Q8BJL0; -.
DR   Antibodypedia; 34237; 221 antibodies from 31 providers.
DR   DNASU; 54380; -.
DR   Ensembl; ENSMUST00000047615.15; ENSMUSP00000047589.9; ENSMUSG00000039354.17. [Q8BJL0-1]
DR   Ensembl; ENSMUST00000152225.2; ENSMUSP00000137833.2; ENSMUSG00000039354.17. [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   AGR; MGI:1859183; -.
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; WNFSMAD; -.
DR   OrthoDB; 318617at2759; -.
DR   PhylomeDB; Q8BJL0; -.
DR   TreeFam; TF106474; -.
DR   BioGRID-ORCS; 54380; 3 hits in 80 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 256 other cell types or tissues.
DR   ExpressionAtlas; Q8BJL0; baseline and differential.
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; 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:DNA damage response; 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   CDD; cd18010; DEXHc_HARP_SMARCAL1; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
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; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45766:SF3; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1; 1.
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; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51467; HARP; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   Genevisible; Q8BJL0; MM.
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
//