FANCM_MOUSE
ID FANCM_MOUSE Reviewed; 2021 AA.
AC Q8BGE5; Q69ZF5; Q8BKB7; Q8BUA8;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Fanconi anemia group M protein homolog;
DE Short=Protein FACM;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q8IYD8};
DE AltName: Full=ATP-dependent RNA helicase FANCM;
GN Name=Fancm; Synonyms=Kiaa1596;
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] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-1393 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye, Head, Heart, and Liver;
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] (ISOFORM 4).
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP PROTEIN SEQUENCE OF 1424-1438, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: DNA-dependent ATPase component of the Fanconi anemia (FA)
CC core complex. Required for the normal activation of the FA pathway,
CC leading to monoubiquitination of the FANCI-FANCD2 complex in response
CC to DNA damage, cellular resistance to DNA cross-linking drugs, and
CC prevention of chromosomal breakage. In complex with CENPS and CENPX,
CC binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA) and
CC Holliday junction substrates. Its ATP-dependent DNA branch migration
CC activity can process branched DNA structures such as a movable
CC replication fork. This activity is strongly stimulated in the presence
CC of CENPS and CENPX. In complex with FAAP24, efficiently binds to
CC single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In
CC vitro, on its own, strongly binds ssDNA oligomers and weakly fsDNA, but
CC does not bind to dsDNA. {ECO:0000250|UniProtKB:Q8IYD8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:Q8IYD8};
CC -!- SUBUNIT: Component of the Fanconi anemia (FA) core complex, which
CC consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG,
CC FANCL, FANCM, FAAP24 and FAAP100. The FA core complex associates with
CC Bloom syndrome (BLM) complex, which consists of at least BLM, DNA
CC topoisomerase 3-alpha/TOP3A, RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32.
CC This supercomplex between FA and BLM complexes has been called BRAFT.
CC Forms a discrete complex with CENPS and CENPX, called FANCM-MHF; this
CC interaction stimulates DNA binding and replication fork remodeling by
CC FANCM and stabilizes the binding partners. Forms a heterodimer with
CC FAAP24; this interaction increases FANCM single-stranded DNA-binding
CC activity. {ECO:0000250|UniProtKB:Q8IYD8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8IYD8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BGE5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGE5-2; Sequence=VSP_015994, VSP_015995;
CC Name=3;
CC IsoId=Q8BGE5-3; Sequence=VSP_015992, VSP_015993;
CC Name=4;
CC IsoId=Q8BGE5-4; Sequence=VSP_015991;
CC -!- PTM: Phosphorylated; hyperphosphorylated in response to genotoxic
CC stress. {ECO:0000250|UniProtKB:Q8IYD8}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC FANCM sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32489.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK050306; BAC34178.2; -; mRNA.
DR EMBL; AK053715; BAC35487.1; -; mRNA.
DR EMBL; AK084697; BAC39257.2; -; mRNA.
DR EMBL; AK086395; BAC39660.1; -; mRNA.
DR EMBL; AK173211; BAD32489.1; ALT_INIT; mRNA.
DR CCDS; CCDS25941.1; -. [Q8BGE5-1]
DR RefSeq; NP_849243.2; NM_178912.3. [Q8BGE5-1]
DR RefSeq; XP_006515407.1; XM_006515344.3.
DR AlphaFoldDB; Q8BGE5; -.
DR SMR; Q8BGE5; -.
DR BioGRID; 222708; 4.
DR STRING; 10090.ENSMUSP00000054797; -.
DR ChEMBL; CHEMBL2176806; -.
DR iPTMnet; Q8BGE5; -.
DR PhosphoSitePlus; Q8BGE5; -.
DR jPOST; Q8BGE5; -.
DR MaxQB; Q8BGE5; -.
DR PaxDb; Q8BGE5; -.
DR PRIDE; Q8BGE5; -.
DR ProteomicsDB; 271863; -. [Q8BGE5-1]
DR ProteomicsDB; 271864; -. [Q8BGE5-2]
DR ProteomicsDB; 271865; -. [Q8BGE5-3]
DR ProteomicsDB; 271866; -. [Q8BGE5-4]
DR Antibodypedia; 23452; 223 antibodies from 30 providers.
DR DNASU; 104806; -.
DR Ensembl; ENSMUST00000058889; ENSMUSP00000054797; ENSMUSG00000055884. [Q8BGE5-1]
DR GeneID; 104806; -.
DR KEGG; mmu:104806; -.
DR UCSC; uc007nrc.1; mouse. [Q8BGE5-3]
DR UCSC; uc007nrd.1; mouse. [Q8BGE5-2]
DR UCSC; uc007nrf.1; mouse. [Q8BGE5-1]
DR CTD; 57697; -.
DR MGI; MGI:2442306; Fancm.
DR VEuPathDB; HostDB:ENSMUSG00000055884; -.
DR eggNOG; KOG0354; Eukaryota.
DR eggNOG; KOG0442; Eukaryota.
DR GeneTree; ENSGT00940000156480; -.
DR HOGENOM; CLU_000801_1_0_1; -.
DR InParanoid; Q8BGE5; -.
DR OMA; EQPWDRE; -.
DR OrthoDB; 989616at2759; -.
DR PhylomeDB; Q8BGE5; -.
DR TreeFam; TF324610; -.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 104806; 36 hits in 109 CRISPR screens.
DR PRO; PR:Q8BGE5; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BGE5; protein.
DR Bgee; ENSMUSG00000055884; Expressed in embryonic post-anal tail and 152 other tissues.
DR ExpressionAtlas; Q8BGE5; baseline and differential.
DR Genevisible; Q8BGE5; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0071821; C:FANCM-MHF complex; ISS:UniProtKB.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; ISO:MGI.
DR GO; GO:1902527; P:positive regulation of protein monoubiquitination; ISO:MGI.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR GO; GO:0071932; P:replication fork reversal; IBA:GO_Central.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; ISS:UniProtKB.
DR CDD; cd18033; DEXDc_FANCM; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR031879; FANCM-MHF-bd.
DR InterPro; IPR039686; FANCM/Mph1-like.
DR InterPro; IPR044749; FANCM_DEXDc.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR14025:SF20; PTHR14025:SF20; 1.
DR Pfam; PF02732; ERCC4; 1.
DR Pfam; PF16783; FANCM-MHF_bd; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00891; ERCC4; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Direct protein sequencing; DNA damage;
KW DNA repair; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..2021
FT /note="Fanconi anemia group M protein homolog"
FT /id="PRO_0000055177"
FT DOMAIN 86..254
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 437..612
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 638..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1244..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1369..1441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1447..1466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1615..1700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1689..2009
FT /note="Interaction with FAAP24"
FT /evidence="ECO:0000250|UniProtKB:Q8IYD8"
FT REGION 1712..1732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 202..205
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 837..856
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1627..1654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYD8"
FT MOD_RES 1637
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYD8"
FT VAR_SEQ 1..741
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_015991"
FT VAR_SEQ 423..433
FT /note="NKEKKFVYSHP -> LVFQGKLWSFT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015992"
FT VAR_SEQ 434..2021
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015993"
FT VAR_SEQ 651
FT /note="I -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015994"
FT VAR_SEQ 652..2021
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015995"
SQ SEQUENCE 2021 AA; 226018 MW; 8646A4535437A8AF CRC64;
MSGRQRTLFQ TWGPSLVRGS GDSGCGQPRS PAMAEALPEE DDEVLLVAAY EAERQLDPGD
GGFCAAAGAL WIYPTNCPVR DYQLDISRSA LFCNTLVCLP TGLGKTFIAA VVMYNFYRWF
PSGKVVFMAP TKPLVTQQME ACFHVMGIPQ SHMAEMTGST QAVNRKEIWS SRRVLFLTPQ
VMVNDLTRGA VPATHVKCLV VDEAHKALGN YAYCQVVREL VKYTTHFRIL ALSATPGSDI
KAVQQVITNL LIGKIELRSE ESPDILPYSH ERRVEKLVVP LGEELGAIQK TYIQILETFA
SSLIHRNVLM KRDIPNLTKY QIILARDQFR KNPSPNIVGI QQGIIEGEFA LCISLYHGYE
LLQQMGMRSL YFFLSGIMDG TKGMTRARNE LSRNEDFMKL YTHLQSAFAP ASTSDASAFQ
RGNKEKKFVY SHPKLKKLEE VILEHFKSWN AKATTEKKCH ESRVMIFSSF RDSVEEIAEM
LLQHRPVIRV MTFVGHASGK NTKGFTQKEQ LQVVRQFRDG GYNTLVSTCV GEEGLDIGEV
DLIICFDAQK SPIRLIQRMG RTGRKRQGRI VVILAEGREE RTYNQSQSNK KNIYKAISGN
RQVLRLYQGS PRMVPDKINP ELHKMYITHG VYEPEKARSV QRRPFSSRGG IKASKSNKDG
LLSEEEFNLW SRLYRLGDSD QVKGVALPQS HFPSLQEDRV IQDPTTRIHQ LSLSEWSLWQ
DRPLPTHQVD HSDRCHHFIS IMKMIEGMRH EEGECSYELK IRPFLQMEDV CSKYHAPRNG
YNNVASVASS AHQKSSFRPS VDAGGSLTVI ESEEEHADTV KQRDSKWTKI TSLREKPCRA
GRKGQTCEHS EGEGEDGDAG SSDADGQSPA EADSQVDPPS GERMADVGGI SILGAVTEED
NHPGTLQMEC QVTNKSCARY SLDSGYSSFS DEKSVSSNLF LPLEEELFTD RAAEQFYNCR
PMTEDVLANV ERFLSRSPPS LSGLSDLVYD VTQGCEFDNA SCSPYPEHEH SPRPVSPASH
SAGNSQQNLE SNSAKRISHP TEKYCLPGTT HNKVSDRPSF CESDSEGHNI KYQNSGSNSC
AQIQADLENN FVDKNSHDDS EPPVLFTDED ESLLLFEDDF KNIEDGPEEL NGASLPPFNS
ISQPLRVSGK TLTSEMPPVS HFLISDELLL DDDSEPEDQI VCGAKSWKCQ EGVEDGQEEL
RTDGQTFDCS VDLFSVTFDL GFRCSSGSDD EMLAGASDRT RTLGAADVSG RHSDKEIKDA
GGASGPLGRA ISPIPTETAQ WSPWAQNKEY ASFHVASSSP VKQRVRSTPL SKSHASSKTG
AHMLKTLDST KEKAGGQGFK MALNPRLGHL GFSVEETKSS DQVFVHQSPR RTEVEHLTSE
SEDDVFLRKT KKPKRNVLKS PEDQKNNEVD SPIHAVKKPR VLRSELASSD DESENFGRTC
PRLEHFKGRN RNIRKGSAAQ KNRSQVKTMA RRFLDDEAEV SGEDVDCVSA DEEDESENEQ
DSSLLDFVND RTQLSQAIND SEMRAIYMKS VRSPLMSTKY RMVREKRPNM NIFSQIPEQD
ENYLEDSFCV DEEESCKSQS SEEEISVDFN LTKDSFTDED IRYKTRYAVK IKQMNKKQNY
TRPRKKLSRI ILPDDDSSEE ENIPKDREHS VAGGHAAAEH TQQGQLWASG PSGSSVPPQV
LSDPSWNQSS RQRLQVQPSI TDAVPRTLNV KAQSHNKIKS ASPPCTGVES RKEYGNHPVQ
LKADSQEHSD TSAAPCSTSL LHVAEGHTAP RHLQEGNRAC ILVDSREITT GLEVISSLRT
VHGLQVEICP LNGCDYIVSS RMVVVRRSQS EMLSNTSKNK FIEQMQRLQS MFQRICVIVE
KDREKAGDTS KKFRRTKCYD SLLTALVGAG IRILFSSGQE ETADLLKELS LVEQRKNAGI
HIPAVLNTSK LEALPFYLSI PGISYITALN MCHQFSSVKK MANSSPEEIS TCAQVNHQKA
EEIYKYIHYI FDMQMLPNDL NQERQKPDTC LTLGVAMKEL S
