(data stored in ACNUC24361 zone)

SWISSPROT: ZSC31_HUMAN

ID   ZSC31_HUMAN             Reviewed;         406 AA.
AC   Q96LW9; Q6P178; Q8WWS5;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   11-DEC-2019, entry version 161.
DE   RecName: Full=Zinc finger and SCAN domain-containing protein 31;
DE   AltName: Full=Zinc finger protein 323;
GN   Name=ZSCAN31; Synonyms=ZNF310P, ZNF323;
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), AND TISSUE SPECIFICITY.
RC   TISSUE=Fetal heart;
RX   PubMed=12147252; DOI=10.1016/s0006-291x(02)00772-6;
RA   Pi H., Li Y., Zhu C., Zhou L., Luo K., Yuan W., Yi Z., Wang Y., Wu X.,
RA   Liu M.;
RT   "A novel human SCAN/(Cys)2(His)2 zinc-finger transcription factor ZNF323 in
RT   early human embryonic development.";
RL   Biochem. Biophys. Res. Commun. 296:206-213(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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   [6]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-149, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [7]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-149, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [8]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14 AND LYS-149, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-149; LYS-191; LYS-205;
RP   LYS-215; LYS-250 AND LYS-358, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: May function as a transcription factor. May be involved in
CC       the development of multiple embryonic organs.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q96LW9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96LW9-2; Sequence=VSP_047105;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in the lung, liver, and
CC       kidney, while weakly expressed in intestine, brain, muscle, cholecyst,
CC       heart, and pancreas. {ECO:0000269|PubMed:12147252}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000305}.
DR   EMBL; AF513019; AAM47006.1; -; mRNA.
DR   EMBL; AK057702; BAB71548.1; -; mRNA.
DR   EMBL; AL021997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03155.1; -; Genomic_DNA.
DR   EMBL; BC065241; AAH65241.1; -; mRNA.
DR   CCDS; CCDS4649.1; -. [Q96LW9-1]
DR   CCDS; CCDS59001.1; -. [Q96LW9-2]
DR   RefSeq; NP_001128687.1; NM_001135215.1. [Q96LW9-1]
DR   RefSeq; NP_001128688.1; NM_001135216.1. [Q96LW9-1]
DR   RefSeq; NP_001230170.1; NM_001243241.1. [Q96LW9-1]
DR   RefSeq; NP_001230171.1; NM_001243242.1. [Q96LW9-2]
DR   RefSeq; NP_001230172.1; NM_001243243.1. [Q96LW9-2]
DR   RefSeq; NP_001230173.1; NM_001243244.1. [Q96LW9-2]
DR   RefSeq; NP_112161.3; NM_030899.4. [Q96LW9-1]
DR   RefSeq; NP_665916.1; NM_145909.2. [Q96LW9-1]
DR   RefSeq; XP_005249352.1; XM_005249295.1. [Q96LW9-1]
DR   RefSeq; XP_005249353.1; XM_005249296.4. [Q96LW9-1]
DR   RefSeq; XP_011513109.1; XM_011514807.2. [Q96LW9-1]
DR   RefSeq; XP_011513110.1; XM_011514808.2. [Q96LW9-1]
DR   RefSeq; XP_011513111.1; XM_011514809.1. [Q96LW9-1]
DR   RefSeq; XP_011513113.1; XM_011514811.2. [Q96LW9-1]
DR   RefSeq; XP_011513114.1; XM_011514812.2. [Q96LW9-1]
DR   RefSeq; XP_011513115.1; XM_011514813.2. [Q96LW9-1]
DR   RefSeq; XP_016866685.1; XM_017011196.1. [Q96LW9-1]
DR   SMR; Q96LW9; -.
DR   BioGrid; 122130; 15.
DR   IntAct; Q96LW9; 11.
DR   STRING; 9606.ENSP00000390076; -.
DR   iPTMnet; Q96LW9; -.
DR   PhosphoSitePlus; Q96LW9; -.
DR   BioMuta; ZSCAN31; -.
DR   DMDM; 23396994; -.
DR   EPD; Q96LW9; -.
DR   jPOST; Q96LW9; -.
DR   MassIVE; Q96LW9; -.
DR   MaxQB; Q96LW9; -.
DR   PaxDb; Q96LW9; -.
DR   PeptideAtlas; Q96LW9; -.
DR   PRIDE; Q96LW9; -.
DR   ProteomicsDB; 66823; -.
DR   ProteomicsDB; 77261; -. [Q96LW9-1]
DR   ABCD; Q96LW9; -.
DR   DNASU; 64288; -.
DR   Ensembl; ENST00000344279; ENSP00000345339; ENSG00000235109. [Q96LW9-1]
DR   Ensembl; ENST00000396838; ENSP00000380050; ENSG00000235109. [Q96LW9-1]
DR   Ensembl; ENST00000414429; ENSP00000390076; ENSG00000235109. [Q96LW9-1]
DR   Ensembl; ENST00000439158; ENSP00000413705; ENSG00000235109. [Q96LW9-1]
DR   Ensembl; ENST00000446474; ENSP00000402937; ENSG00000235109. [Q96LW9-2]
DR   Ensembl; ENST00000611469; ENSP00000480254; ENSG00000235109. [Q96LW9-2]
DR   GeneID; 64288; -.
DR   KEGG; hsa:64288; -.
DR   UCSC; uc003nla.4; human. [Q96LW9-1]
DR   CTD; 64288; -.
DR   DisGeNET; 64288; -.
DR   EuPathDB; HostDB:ENSG00000235109.7; -.
DR   GeneCards; ZSCAN31; -.
DR   HGNC; HGNC:14097; ZSCAN31.
DR   HPA; HPA007124; -.
DR   MIM; 610794; gene.
DR   neXtProt; NX_Q96LW9; -.
DR   OpenTargets; ENSG00000235109; -.
DR   PharmGKB; PA37840; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000163314; -.
DR   HOGENOM; HOG000234619; -.
DR   InParanoid; Q96LW9; -.
DR   KO; K09230; -.
DR   OMA; VEEDPIW; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q96LW9; -.
DR   TreeFam; TF338304; -.
DR   ChiTaRS; ZSCAN31; human.
DR   GenomeRNAi; 64288; -.
DR   Pharos; Q96LW9; Tdark.
DR   PRO; PR:Q96LW9; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q96LW9; protein.
DR   Bgee; ENSG00000235109; Expressed in 188 organ(s), highest expression level in thyroid gland.
DR   ExpressionAtlas; Q96LW9; baseline and differential.
DR   Genevisible; Q96LW9; HS.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd07936; SCAN; 1.
DR   Gene3D; 1.10.4020.10; -; 1.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
DR   PRODOM; Q96LW9.
DR   SWISS-2DPAGE; Q96LW9.
KW   Alternative splicing; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW   Polymorphism; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..406
FT                   /note="Zinc finger and SCAN domain-containing protein 31"
FT                   /id="PRO_0000047532"
FT   DOMAIN          39..121
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00187"
FT   ZN_FING         239..261
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         267..289
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         295..317
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         323..345
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         351..373
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         379..401
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   CROSSLNK        14
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447,
FT                   ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
FT                   ECO:0000244|PubMed:28112733"
FT   CROSSLNK        149
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:25218447,
FT                   ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364,
FT                   ECO:0000244|PubMed:28112733"
FT   CROSSLNK        191
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        205
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        215
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        250
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   CROSSLNK        358
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   VAR_SEQ         1..159
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_047105"
FT   VARIANT         50
FT                   /note="T -> S (in dbSNP:rs853678)"
FT                   /id="VAR_019981"
FT   VARIANT         128
FT                   /note="A -> P (in dbSNP:rs6922302)"
FT                   /id="VAR_052809"
FT   VARIANT         205
FT                   /note="K -> R (in dbSNP:rs853684)"
FT                   /id="VAR_024209"
FT   VARIANT         222
FT                   /note="R -> Q (in dbSNP:rs34223404)"
FT                   /id="VAR_052810"
FT   VARIANT         365
FT                   /note="G -> E (in dbSNP:rs2394051)"
FT                   /id="VAR_059911"
FT   CONFLICT        58
FT                   /note="S -> N (in Ref. 2; BAB71548)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        173
FT                   /note="Q -> R (in Ref. 2; BAB71548)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   406 AA;  47293 MW;  A6082E44F27101E8 CRC64;
     MASTEEQYDL KIVKVEEDPI WDQETHLRGN NFSGQEASRQ LFRQFCYQET PGPREALSRL
     RELCHQWLRP EIHTKEQILE LLVLEQFLTI LPEELQAWVR EHHPESGEEA VAVVEDLEQE
     LSEPGNQAPD HEHGHSEVLL EDVEHLKVKQ EPTDIQLQPM VTQLRYESFC LHQFQEQDGE
     SIPENQELAS KQEILKEMEH LGDSKLQRDV SLDSKYRETC KRDSKAEKQQ AHSTGERRHR
     CNECGKSFTK SSVLIEHQRI HTGEKPYECE ECGKAFSRRS SLNEHRRSHT GEKPYQCKEC
     GKAFSASNGL TRHRRIHTGE KPYECKVCGK AFLLSSCLVQ HQRIHTGEKR YQCRECGKAF
     IQNAGLFQHL RVHTGEKPYQ CSQCSKLFSK RTLLKKHQKI HTGERP
//

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