ID   UBP44_MOUSE             Reviewed;         711 AA.
AC   Q8C2S0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2012, sequence version 3.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 44;
DE            EC=3.4.19.12 {ECO:0000269|PubMed:23187126, ECO:0000269|PubMed:33937266};
DE   AltName: Full=Deubiquitinating enzyme 44;
DE   AltName: Full=Ubiquitin thioesterase 44;
DE   AltName: Full=Ubiquitin-specific-processing protease 44;
GN   Name=Usp44;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND PROTEASOMAL
RP   DEGRADATION.
RC   TISSUE=Kidney;
RX   PubMed=21853124; DOI=10.1371/journal.pone.0023389;
RA   Zhang Y., van Deursen J., Galardy P.J.;
RT   "Overexpression of ubiquitin specific protease 44 (USP44) induces
RT   chromosomal instability and is frequently observed in human T-cell
RT   leukemia.";
RL   PLoS ONE 6:E23389-E23389(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=20402667; DOI=10.1042/cbi20090144;
RA   Suresh B., Ramakrishna S., Lee H.J., Choi J.H., Kim J.Y., Ahn W.S.,
RA   Baek K.H.;
RT   "K48- and K63-linked polyubiquitination of deubiquitinating enzyme USP44.";
RL   Cell Biol. Int. 34:799-808(2010).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-281, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=23187126; DOI=10.1172/jci63084;
RA   Zhang Y., Foreman O., Wigle D.A., Kosari F., Vasmatzis G., Salisbury J.L.,
RA   van Deursen J., Galardy P.J.;
RT   "USP44 regulates centrosome positioning to prevent aneuploidy and suppress
RT   tumorigenesis.";
RL   J. Clin. Invest. 122:4362-4374(2012).
RN   [7]
RP   FUNCTION, MUTAGENESIS OF CYS-281, DISRUPTION PHENOTYPE, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=33937266; DOI=10.3389/fcell.2021.663411;
RA   Zhang Y., Mandemaker I.K., Matsumoto S., Foreman O., Holland C.P.,
RA   Lloyd W.R., Sugasawa K., Vermeulen W., Marteijn J.A., Galardy P.J.;
RT   "USP44 Stabilizes DDB2 to Facilitate Nucleotide Excision Repair and Prevent
RT   Tumors.";
RL   Front. Cell Dev. Biol. 9:663411-663411(2021).
CC   -!- FUNCTION: Deubiquitinase that plays a key regulatory role in the
CC       spindle assembly checkpoint or mitotic checkpoint by preventing
CC       premature anaphase onset (PubMed:23187126). Acts by specifically
CC       mediating deubiquitination of CDC20, a negative regulator of the
CC       anaphase promoting complex/cyclosome (APC/C). Deubiquitination of CDC20
CC       leads to stabilize the MAD2L1-CDC20-APC/C ternary complex (also named
CC       mitotic checkpoint complex), thereby preventing premature activation of
CC       the APC/C. Promotes association of MAD2L1 with CDC20 and reinforces the
CC       spindle assembly checkpoint. Promotes also the deubiquitination of
CC       histone H2A and H2B. Recruited to RNF8/RNF168-ubiquitinated chromatin
CC       surrounding double stranded breaks (DSBs), promotes hydrolysis of such
CC       ubiquitin conjugates, thus negatively regulating protein recruitment to
CC       damaged chromatin (By similarity). Participates in nucleotide excision
CC       repair (NER) pathway by deubiquitinating DDB2 to prevent its premature
CC       degradation so it can remain on damaged chromatin (PubMed:23187126).
CC       Promotes FOXP3 stabilization through 'Lys-48'-linked deubiquitination
CC       leading to increased stability and increased regulatory T-cell lineage
CC       stability. Plays also a positive role in innate immune response to DNA
CC       viruses by deubiquitinating STING1, selectively removing its 'Lys-48'-
CC       linked polyubiquitin chains and stabilizing it (By similarity).
CC       {ECO:0000250|UniProtKB:Q9H0E7, ECO:0000269|PubMed:21853124,
CC       ECO:0000269|PubMed:23187126}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC         and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC         residue protein attached to proteins as an intracellular targeting
CC         signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:23187126,
CC         ECO:0000269|PubMed:33937266};
CC   -!- SUBUNIT: Interacts with the N-CoR components TBL1X and TBL1XR1.
CC       {ECO:0000250|UniProtKB:Q9H0E7}.
CC   -!- INTERACTION:
CC       Q8C2S0; Q99JB6: Foxp3; NbExp=3; IntAct=EBI-26303241, EBI-10956246;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H0E7}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9H0E7}. Note=Peaks in interphase, with
CC       relatively low levels maintained throughout mitosis. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in lung,
CC       pancreas, skin, liver, stomach and intestine.
CC       {ECO:0000269|PubMed:20402667}.
CC   -!- PTM: Dephosphorylated by CTDP1. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
CC       polyubiquitination and is degraded by the proteasome.
CC   -!- DISRUPTION PHENOTYPE: USP44-deficient mice show a significant increase
CC       in skin tumors when compared to wild-type mice (PubMed:33937266). In
CC       addition, they are prone to development of spontaneous tumors,
CC       particularly in the lungs (PubMed:23187126). USP44 loss causes also
CC       chromosome mis-segregation and aneuploidy (PubMed:23187126).
CC       {ECO:0000269|PubMed:23187126, ECO:0000269|PubMed:33937266}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP44 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI11887.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC       Sequence=BAC40148.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AK088109; BAC40148.1; ALT_SEQ; mRNA.
DR   EMBL; CJ236846; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC124686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC111886; AAI11887.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS88075.1; -.
DR   RefSeq; NP_001193780.1; NM_001206851.1.
DR   RefSeq; XP_011241781.1; XM_011243479.2.
DR   RefSeq; XP_011241782.1; XM_011243480.2.
DR   RefSeq; XP_011241783.1; XM_011243481.2.
DR   RefSeq; XP_011241784.1; XM_011243482.2.
DR   RefSeq; XP_011241785.1; XM_011243483.2.
DR   RefSeq; XP_011241786.1; XM_011243484.2.
DR   RefSeq; XP_011241787.1; XM_011243485.2.
DR   RefSeq; XP_011241788.1; XM_011243486.2.
DR   RefSeq; XP_011241789.1; XM_011243487.2.
DR   RefSeq; XP_011241790.1; XM_011243488.2.
DR   RefSeq; XP_011241791.1; XM_011243489.2.
DR   RefSeq; XP_011241792.1; XM_011243490.2.
DR   AlphaFoldDB; Q8C2S0; -.
DR   BioGRID; 236490; 3.
DR   IntAct; Q8C2S0; 1.
DR   MINT; Q8C2S0; -.
DR   STRING; 10090.ENSMUSP00000149020; -.
DR   MEROPS; C19.057; -.
DR   iPTMnet; Q8C2S0; -.
DR   PhosphoSitePlus; Q8C2S0; -.
DR   PaxDb; 10090-ENSMUSP00000092975; -.
DR   ProteomicsDB; 298363; -.
DR   Antibodypedia; 17590; 341 antibodies from 24 providers.
DR   DNASU; 327799; -.
DR   Ensembl; ENSMUST00000216224.2; ENSMUSP00000149020.2; ENSMUSG00000020020.9.
DR   GeneID; 327799; -.
DR   KEGG; mmu:327799; -.
DR   UCSC; uc029rep.1; mouse.
DR   AGR; MGI:3045318; -.
DR   CTD; 84101; -.
DR   MGI; MGI:3045318; Usp44.
DR   VEuPathDB; HostDB:ENSMUSG00000020020; -.
DR   eggNOG; KOG1867; Eukaryota.
DR   GeneTree; ENSGT00940000160526; -.
DR   InParanoid; Q8C2S0; -.
DR   OMA; RYQCNGK; -.
DR   OrthoDB; 227085at2759; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   BioGRID-ORCS; 327799; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Usp44; mouse.
DR   PRO; PR:Q8C2S0; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q8C2S0; Protein.
DR   Bgee; ENSMUSG00000020020; Expressed in spermatid and 27 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISO:MGI.
DR   GO; GO:0101005; F:deubiquitinase activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0140374; P:antiviral innate immune response; ISO:MGI.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IMP:CACAO.
DR   GO; GO:0045841; P:negative regulation of mitotic metaphase/anaphase transition; ISO:MGI.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; IDA:UniProtKB.
DR   GO; GO:0045066; P:regulatory T cell differentiation; ISO:MGI.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF15; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 44; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Hydrolase; Immunity; Innate immunity;
KW   Metal-binding; Mitosis; Nucleus; Protease; Reference proteome;
KW   Thiol protease; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..711
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 44"
FT                   /id="PRO_0000395811"
FT   DOMAIN          272..677
FT                   /note="USP"
FT   ZN_FING         2..99
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   REGION          170..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        281
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        635
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   BINDING         4
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         6
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         53
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   MUTAGEN         281
FT                   /note="C->S: Abolishes deubiquitinase activity."
FT                   /evidence="ECO:0000269|PubMed:23187126,
FT                   ECO:0000269|PubMed:33937266"
SQ   SEQUENCE   711 AA;  80479 MW;  F176DB2BA3C658BE CRC64;
     MDRCKHVEQL QLAQGHSILD PQKWYCMVCN TTESIWACLS CSHVACGKYI QEHALKHFQE
     SSHPVAFEVN DMYAFCYLCN DYVLNDNAAG DLKSLRSTLS TIKSKKYPCV VPSDSVLHPV
     DAQDRVYSLL DGTQSLPGNE DPTCAALWHR RRVLMGKAFR TWFEQSAIGR KGQEPTQERM
     VAKREAKRRQ QQELEQQMKA ELESTPPRKS LRLQGSSEEA ATIEIVPVRA PPPPPASPAK
     DKAALPTSED RTFKKVSDSL IKRRPMVTPG VTGLRNLGNT CYMNSVLQVL SHLLIFRQCF
     LKLDLNQWLA VAASDKARSY KHSAVTEAAA QQMNEGQEKE KGFVCSRHSG LSSGLSGGAS
     KGRNMELIQP REPSSPYSSL CHELHILFQV MWSGEWALVS PFAMLHSVWR LIPAFRGYAQ
     QDAQEFLCEL LDKIQRELET TGTKLPALIP TSQRRLIEQV LNVVNNIFHG QFLSQVTCLA
     CDNKSDTIES FWDLSLEFPE RYQCSGKDAA SQPCLVTDML DKFTETEALE GKIYMCDHCN
     SKRRKFSSKS VVFTEAQKQL MICHLPQVLR LHLKRFRWSG RNNREKIGVH VVFEETLNME
     PYCCRETLNA LRPECFLYNL SAVVIHHGKG FGSGHYTAYC YNSEGGFWVH CNDSKLSMCT
     MEEVRKAQAY ILFYTQRVTE NGHSKLLPPE LLSNSQHPSK ETDASSNEVL S
//