ID   USPL1_HUMAN             Reviewed;        1092 AA.
AC   Q5W0Q7; Q14109; Q6AI45; Q8IY30; Q8IYE8;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=SUMO-specific isopeptidase USPL1;
DE            EC=3.4.22.-;
DE   AltName: Full=Ubiquitin-specific peptidase-like protein 1;
DE            Short=USP-like 1;
GN   Name=USPL1; Synonyms=C13orf22, D13S106;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Melanoma;
RA   Wilton A.N., Zehavi-Feferman T., Fleming J., Baker E., Chen L.Z.,
RA   Cooper D.W.;
RT   "A unique intronless gene or gene segment on chromosome 13 specifying a
RT   highly charged amino acid sequence.";
RL   Cytogenet. Cell Genet. 58:1985-1985(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Semen;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLY-173;
RP   SER-531; ASN-950 AND SER-1043.
RC   TISSUE=Testis;
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   FUNCTION IN PROTEIN DESUMOYLATION, NON-CATALYTIC FUNCTION, CATALYTIC
RP   ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-229; CYS-236;
RP   TRP-237; HIS-421; 340-LEU-LEU-341 AND 494-ILE-VAL-495.
RX   PubMed=22878415; DOI=10.1038/embor.2012.125;
RA   Schulz S., Chachami G., Kozaczkiewicz L., Winter U., Stankovic-Valentin N.,
RA   Haas P., Hofmann K., Urlaub H., Ovaa H., Wittbrodt J., Meulmeester E.,
RA   Melchior F.;
RT   "Ubiquitin-specific protease-like 1 (USPL1) is a SUMO isopeptidase with
RT   essential, non-catalytic functions.";
RL   EMBO Rep. 13:930-938(2012).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-909, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [7]
RP   FUNCTION IN RNAPII-MEDIATED SNRNA TRANSCRIPTION, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH ELL.
RX   PubMed=24413172; DOI=10.1242/jcs.141788;
RA   Hutten S., Chachami G., Winter U., Melchior F., Lamond A.I.;
RT   "A role for the Cajal-body-associated SUMO isopeptidase USPL1 in snRNA
RT   transcription mediated by RNA polymerase II.";
RL   J. Cell Sci. 127:1065-1078(2014).
CC   -!- FUNCTION: SUMO-specific isopeptidase involved in protein desumoylation.
CC       Specifically binds SUMO proteins with a higher affinity for SUMO2 and
CC       SUMO3 which it cleaves more efficiently. Also able to process full-
CC       length SUMO proteins to their mature forms (PubMed:22878415). Plays a
CC       key role in RNA polymerase-II-mediated snRNA transcription in the Cajal
CC       bodies (PubMed:24413172). Is a component of complexes that can bind to
CC       U snRNA genes (PubMed:24413172). {ECO:0000269|PubMed:22878415,
CC       ECO:0000269|PubMed:24413172}.
CC   -!- SUBUNIT: Interacts with ELL. {ECO:0000269|PubMed:24413172}.
CC   -!- INTERACTION:
CC       Q5W0Q7; P63165: SUMO1; NbExp=5; IntAct=EBI-2513899, EBI-80140;
CC       Q5W0Q7; P61956: SUMO2; NbExp=2; IntAct=EBI-2513899, EBI-473220;
CC       Q5W0Q7; P55854: SUMO3; NbExp=17; IntAct=EBI-2513899, EBI-474067;
CC   -!- SUBCELLULAR LOCATION: Nucleus, Cajal body {ECO:0000269|PubMed:22878415,
CC       ECO:0000269|PubMed:24413172}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5W0Q7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5W0Q7-2; Sequence=VSP_023479;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR   EMBL; X59131; CAA41848.1; -; mRNA.
DR   EMBL; CR627370; CAH10469.1; -; mRNA.
DR   EMBL; AL138681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC036027; AAH36027.1; -; mRNA.
DR   EMBL; BC038103; AAH38103.1; -; mRNA.
DR   CCDS; CCDS81760.1; -. [Q5W0Q7-2]
DR   CCDS; CCDS9336.1; -. [Q5W0Q7-1]
DR   PIR; I37273; I37273.
DR   RefSeq; NP_001308461.1; NM_001321532.1.
DR   RefSeq; NP_001308462.1; NM_001321533.1. [Q5W0Q7-2]
DR   RefSeq; NP_001308463.1; NM_001321534.1. [Q5W0Q7-2]
DR   RefSeq; NP_005791.3; NM_005800.4. [Q5W0Q7-1]
DR   RefSeq; XP_005266270.1; XM_005266213.3.
DR   PDB; 7P99; X-ray; 1.80 A; A=213-516.
DR   PDB; 7ZJU; X-ray; 2.17 A; A/C=218-502.
DR   PDB; 7ZJV; X-ray; 2.40 A; A=218-502.
DR   PDBsum; 7P99; -.
DR   PDBsum; 7ZJU; -.
DR   PDBsum; 7ZJV; -.
DR   AlphaFoldDB; Q5W0Q7; -.
DR   SMR; Q5W0Q7; -.
DR   BioGRID; 115503; 37.
DR   DIP; DIP-47278N; -.
DR   IntAct; Q5W0Q7; 22.
DR   MINT; Q5W0Q7; -.
DR   STRING; 9606.ENSP00000255304; -.
DR   MEROPS; C98.001; -.
DR   GlyGen; Q5W0Q7; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5W0Q7; -.
DR   PhosphoSitePlus; Q5W0Q7; -.
DR   BioMuta; USPL1; -.
DR   DMDM; 74747969; -.
DR   EPD; Q5W0Q7; -.
DR   jPOST; Q5W0Q7; -.
DR   MassIVE; Q5W0Q7; -.
DR   MaxQB; Q5W0Q7; -.
DR   PaxDb; 9606-ENSP00000255304; -.
DR   PeptideAtlas; Q5W0Q7; -.
DR   ProteomicsDB; 65772; -. [Q5W0Q7-1]
DR   ProteomicsDB; 65773; -. [Q5W0Q7-2]
DR   Antibodypedia; 22766; 22 antibodies from 10 providers.
DR   DNASU; 10208; -.
DR   Ensembl; ENST00000255304.9; ENSP00000255304.4; ENSG00000132952.12. [Q5W0Q7-1]
DR   Ensembl; ENST00000614860.1; ENSP00000480656.1; ENSG00000132952.12. [Q5W0Q7-2]
DR   GeneID; 10208; -.
DR   KEGG; hsa:10208; -.
DR   MANE-Select; ENST00000255304.9; ENSP00000255304.4; NM_005800.5; NP_005791.3.
DR   UCSC; uc001utc.3; human. [Q5W0Q7-1]
DR   AGR; HGNC:20294; -.
DR   CTD; 10208; -.
DR   DisGeNET; 10208; -.
DR   GeneCards; USPL1; -.
DR   HGNC; HGNC:20294; USPL1.
DR   HPA; ENSG00000132952; Low tissue specificity.
DR   MIM; 617470; gene.
DR   neXtProt; NX_Q5W0Q7; -.
DR   OpenTargets; ENSG00000132952; -.
DR   PharmGKB; PA134872379; -.
DR   VEuPathDB; HostDB:ENSG00000132952; -.
DR   eggNOG; ENOG502QRFM; Eukaryota.
DR   GeneTree; ENSGT00390000002316; -.
DR   HOGENOM; CLU_009764_0_0_1; -.
DR   InParanoid; Q5W0Q7; -.
DR   OMA; NANALCW; -.
DR   OrthoDB; 3740838at2759; -.
DR   PhylomeDB; Q5W0Q7; -.
DR   TreeFam; TF350670; -.
DR   BRENDA; 3.4.22.B70; 2681.
DR   PathwayCommons; Q5W0Q7; -.
DR   SignaLink; Q5W0Q7; -.
DR   BioGRID-ORCS; 10208; 773 hits in 1160 CRISPR screens.
DR   ChiTaRS; USPL1; human.
DR   GenomeRNAi; 10208; -.
DR   Pharos; Q5W0Q7; Tbio.
DR   PRO; PR:Q5W0Q7; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q5W0Q7; Protein.
DR   Bgee; ENSG00000132952; Expressed in sperm and 200 other cell types or tissues.
DR   GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0016929; F:deSUMOylase activity; IDA:UniProtKB.
DR   GO; GO:0032183; F:SUMO binding; IDA:UniProtKB.
DR   GO; GO:0030576; P:Cajal body organization; IMP:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR   GO; GO:0016926; P:protein desumoylation; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0009301; P:snRNA transcription; IMP:UniProtKB.
DR   InterPro; IPR029388; DUF4650.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR028890; Peptidase_C98.
DR   InterPro; IPR028889; USP_dom.
DR   InterPro; IPR033505; USPL1.
DR   PANTHER; PTHR15294; RETINOVIN-RELATED; 1.
DR   PANTHER; PTHR15294:SF3; SUMO-SPECIFIC ISOPEPTIDASE USPL1; 1.
DR   Pfam; PF15509; DUF4650; 1.
DR   Pfam; PF15499; Peptidase_C98; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q5W0Q7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Hydrolase; Nucleus; Phosphoprotein;
KW   Protease; Reference proteome; Thiol protease.
FT   CHAIN           1..1092
FT                   /note="SUMO-specific isopeptidase USPL1"
FT                   /id="PRO_0000279526"
FT   DOMAIN          227..500
FT                   /note="USP"
FT   REGION          145..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..495
FT                   /note="SUMO-binding"
FT   REGION          713..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          797..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          904..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..207
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        907..929
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        236
FT                   /note="Nucleophile"
FT   ACT_SITE        456
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         909
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..329
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_023479"
FT   VARIANT         173
FT                   /note="E -> G (in dbSNP:rs17853512)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_030916"
FT   VARIANT         384
FT                   /note="P -> S (in dbSNP:rs3742303)"
FT                   /id="VAR_030917"
FT   VARIANT         522
FT                   /note="A -> P (in dbSNP:rs17609459)"
FT                   /id="VAR_030918"
FT   VARIANT         531
FT                   /note="L -> S (in dbSNP:rs7984952)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_030919"
FT   VARIANT         583
FT                   /note="I -> V (in dbSNP:rs41412648)"
FT                   /id="VAR_051542"
FT   VARIANT         739
FT                   /note="S -> C (in dbSNP:rs9578190)"
FT                   /id="VAR_030920"
FT   VARIANT         786
FT                   /note="L -> I (in dbSNP:rs35371042)"
FT                   /id="VAR_051543"
FT   VARIANT         950
FT                   /note="S -> N (in dbSNP:rs3742302)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_030921"
FT   VARIANT         1043
FT                   /note="T -> S (in dbSNP:rs17857086)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_030922"
FT   MUTAGEN         229
FT                   /note="W->L: Altered SUMO-binding and SUMO-specific
FT                   isopeptidase activity."
FT                   /evidence="ECO:0000269|PubMed:22878415"
FT   MUTAGEN         236
FT                   /note="C->S: Abolishes the SUMO-specific isopeptidase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:22878415"
FT   MUTAGEN         237
FT                   /note="W->F: Altered SUMO-binding and SUMO-specific
FT                   isopeptidase activity."
FT                   /evidence="ECO:0000269|PubMed:22878415"
FT   MUTAGEN         340..341
FT                   /note="LL->AA: Altered SUMO-binding and SUMO-specific
FT                   isopeptidase activity."
FT                   /evidence="ECO:0000269|PubMed:22878415"
FT   MUTAGEN         421
FT                   /note="H->A: Altered SUMO-binding and SUMO-specific
FT                   isopeptidase activity."
FT                   /evidence="ECO:0000269|PubMed:22878415"
FT   MUTAGEN         494..495
FT                   /note="IV->AA: Loss of SUMO-binding and catalytic
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:22878415"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   HELIX           236..246
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   HELIX           249..256
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   HELIX           261..263
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   HELIX           265..283
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   HELIX           297..323
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   HELIX           333..342
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   HELIX           345..348
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   TURN            349..351
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   STRAND          353..360
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   TURN            362..364
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   STRAND          367..375
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   STRAND          377..379
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   STRAND          390..395
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   TURN            398..400
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   STRAND          403..413
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   STRAND          416..422
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   HELIX           431..434
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   STRAND          436..438
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   STRAND          441..452
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   TURN            453..455
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   STRAND          456..462
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   STRAND          468..471
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   HELIX           473..475
FT                   /evidence="ECO:0007829|PDB:7ZJU"
FT   STRAND          480..484
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   HELIX           489..491
FT                   /evidence="ECO:0007829|PDB:7P99"
FT   STRAND          492..500
FT                   /evidence="ECO:0007829|PDB:7P99"
SQ   SEQUENCE   1092 AA;  120440 MW;  FBE4626FC311E706 CRC64;
     MMDSPKIGNG LPVIGPGTDI GISSLHMVGY LGKNFDSAKV PSDEYCPACR EKGKLKALKT
     YRISFQESIF LCEDLQCIYP LGSKSLNNLI SPDLEECHTP HKPQKRKSLE SSYKDSLLLA
     NSKKTRNYIA IDGGKVLNSK HNGEVYDETS SNLPDSSGQQ NPIRTADSLE RNEILEADTV
     DMATTKDPAT VDVSGTGRPS PQNEGCTSKL EMPLESKCTS FPQALCVQWK NAYALCWLDC
     ILSALVHSEE LKNTVTGLCS KEESIFWRLL TKYNQANTLL YTSQLSGVKD GDCKKLTSEI
     FAEIETCLNE VRDEIFISLQ PQLRCTLGDM ESPVFAFPLL LKLETHIEKL FLYSFSWDFE
     CSQCGHQYQN RHMKSLVTFT NVIPEWHPLN AAHFGPCNNC NSKSQIRKMV LEKVSPIFML
     HFVEGLPQND LQHYAFHFEG CLYQITSVIQ YRANNHFITW ILDADGSWLE CDDLKGPCSE
     RHKKFEVPAS EIHIVIWERK ISQVTDKEAA CLPLKKTNDQ HALSNEKPVS LTSCSVGDAA
     SAETASVTHP KDISVAPRTL SQDTAVTHGD HLLSGPKGLV DNILPLTLEE TIQKTASVSQ
     LNSEAFLLEN KPVAENTGIL KTNTLLSQES LMASSVSAPC NEKLIQDQFV DISFPSQVVN
     TNMQSVQLNT EDTVNTKSVN NTDATGLIQG VKSVEIEKDA QLKQFLTPKT EQLKPERVTS
     QVSNLKKKET TADSQTTTSK SLQNQSLKEN QKKPFVGSWV KGLISRGASF MPLCVSAHNR
     NTITDLQPSV KGVNNFGGFK TKGINQKASH VSKKARKSAS KPPPISKPPA GPPSSNGTAA
     HPHAHAASEV LEKSGSTSCG AQLNHSSYGN GISSANHEDL VEGQIHKLRL KLRKKLKAEK
     KKLAALMSSP QSRTVRSENL EQVPQDGSPN DCESIEDLLN ELPYPIDIAS ESACTTVPGV
     SLYSSQTHEE ILAELLSPTP VSTELSENGE GDFRYLGMGD SHIPPPVPSE FNDVSQNTHL
     RQDHNYCSPT KKNPCEVQPD SLTNNACVRT LNLESPMKTD IFDEFFSSSA LNALANDTLD
     LPHFDEYLFE NY
//