LUZP1_HUMAN
ID LUZP1_HUMAN Reviewed; 1076 AA.
AC Q86V48; Q5TH93; Q8N4X3; Q8TEH1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Leucine zipper protein 1;
GN Name=LUZP1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 856-1076 (ISOFORM 1), AND VARIANTS SER-458; LYS-461
RP AND ASN-868.
RC TISSUE=Pancreas, and 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 [3]
RP PROTEIN SEQUENCE OF 2-14 AND 673-691, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Dozynkiewicz M., Norman J.C.;
RL Submitted (JUN-2009) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-1076 (ISOFORM 3), AND VARIANTS
RP SER-458; LYS-461 AND ASN-868.
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-659 AND SER-690, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570; SER-659; THR-679 AND
RP SER-690, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-574; SER-659; SER-690 AND
RP SER-745, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-611 AND SER-659, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255; SER-425; SER-440;
RP SER-512; SER-611; SER-659; SER-905; SER-932; THR-958; SER-995 AND SER-1042,
RP AND IDENTIFICATION BY 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Also detected in soma and dendrites
CC of neurons. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86V48-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86V48-2; Sequence=VSP_018351, VSP_018353;
CC Name=3;
CC IsoId=Q86V48-3; Sequence=VSP_018352, VSP_018353;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33219.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL031428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033219; AAH33219.1; ALT_INIT; mRNA.
DR EMBL; BC051733; AAH51733.1; -; mRNA.
DR EMBL; AK074153; BAB84979.1; -; mRNA.
DR CCDS; CCDS30628.1; -. [Q86V48-1]
DR RefSeq; NP_001136018.1; NM_001142546.1. [Q86V48-1]
DR RefSeq; NP_361013.3; NM_033631.3. [Q86V48-1]
DR RefSeq; XP_011540392.1; XM_011542090.2. [Q86V48-1]
DR RefSeq; XP_011540393.1; XM_011542091.2. [Q86V48-1]
DR RefSeq; XP_016857741.1; XM_017002252.1. [Q86V48-1]
DR AlphaFoldDB; Q86V48; -.
DR SMR; Q86V48; -.
DR BioGRID; 113574; 158.
DR DIP; DIP-33113N; -.
DR IntAct; Q86V48; 87.
DR MINT; Q86V48; -.
DR STRING; 9606.ENSP00000303758; -.
DR CarbonylDB; Q86V48; -.
DR GlyGen; Q86V48; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q86V48; -.
DR MetOSite; Q86V48; -.
DR PhosphoSitePlus; Q86V48; -.
DR BioMuta; LUZP1; -.
DR DMDM; 97072093; -.
DR EPD; Q86V48; -.
DR jPOST; Q86V48; -.
DR MassIVE; Q86V48; -.
DR MaxQB; Q86V48; -.
DR PaxDb; Q86V48; -.
DR PeptideAtlas; Q86V48; -.
DR PRIDE; Q86V48; -.
DR ProteomicsDB; 69966; -. [Q86V48-1]
DR ProteomicsDB; 69967; -. [Q86V48-2]
DR ProteomicsDB; 69968; -. [Q86V48-3]
DR Antibodypedia; 30121; 111 antibodies from 23 providers.
DR DNASU; 7798; -.
DR Ensembl; ENST00000302291.8; ENSP00000303758.4; ENSG00000169641.14. [Q86V48-1]
DR Ensembl; ENST00000314174.5; ENSP00000313705.5; ENSG00000169641.14. [Q86V48-2]
DR GeneID; 7798; -.
DR KEGG; hsa:7798; -.
DR UCSC; uc001bgl.4; human. [Q86V48-1]
DR CTD; 7798; -.
DR DisGeNET; 7798; -.
DR GeneCards; LUZP1; -.
DR HGNC; HGNC:14985; LUZP1.
DR HPA; ENSG00000169641; Low tissue specificity.
DR MIM; 601422; gene.
DR neXtProt; NX_Q86V48; -.
DR OpenTargets; ENSG00000169641; -.
DR Orphanet; 1606; 1p36 deletion syndrome.
DR PharmGKB; PA30487; -.
DR VEuPathDB; HostDB:ENSG00000169641; -.
DR eggNOG; ENOG502QV81; Eukaryota.
DR GeneTree; ENSGT00950000182852; -.
DR HOGENOM; CLU_010207_1_0_1; -.
DR InParanoid; Q86V48; -.
DR OMA; NHSAGTE; -.
DR OrthoDB; 176494at2759; -.
DR PhylomeDB; Q86V48; -.
DR TreeFam; TF331399; -.
DR PathwayCommons; Q86V48; -.
DR SignaLink; Q86V48; -.
DR BioGRID-ORCS; 7798; 13 hits in 1081 CRISPR screens.
DR ChiTaRS; LUZP1; human.
DR GenomeRNAi; 7798; -.
DR Pharos; Q86V48; Tbio.
DR PRO; PR:Q86V48; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q86V48; protein.
DR Bgee; ENSG00000169641; Expressed in tendon of biceps brachii and 203 other tissues.
DR ExpressionAtlas; Q86V48; baseline and differential.
DR Genevisible; Q86V48; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0060840; P:artery development; IEA:Ensembl.
DR GO; GO:0021503; P:neural fold bending; IBA:GO_Central.
DR GO; GO:0003281; P:ventricular septum development; IEA:Ensembl.
DR InterPro; IPR026734; Luzp1.
DR PANTHER; PTHR23166:SF7; PTHR23166:SF7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Direct protein sequencing;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT CHAIN 2..1076
FT /note="Leucine zipper protein 1"
FT /id="PRO_0000234550"
FT REGION 246..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1042..1076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 11..359
FT /evidence="ECO:0000255"
FT COMPBIAS 255..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:22814378"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 679
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 905
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 958
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1025
FT /note="E -> SS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018351"
FT VAR_SEQ 1025
FT /note="E -> VSSSLSPLSLFSLPFPSLPFPFSPLLWPV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693554"
FT /id="VSP_018352"
FT VAR_SEQ 1026..1076
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693554,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_018353"
FT VARIANT 317
FT /note="S -> A (in dbSNP:rs12091554)"
FT /id="VAR_056932"
FT VARIANT 458
FT /note="G -> S (in dbSNP:rs477830)"
FT /evidence="ECO:0000269|PubMed:12693554,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_026283"
FT VARIANT 461
FT /note="Q -> K (in dbSNP:rs3765407)"
FT /evidence="ECO:0000269|PubMed:12693554,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_026284"
FT VARIANT 491
FT /note="T -> I (in dbSNP:rs35917050)"
FT /id="VAR_056933"
FT VARIANT 868
FT /note="D -> N (in dbSNP:rs10799790)"
FT /evidence="ECO:0000269|PubMed:12693554,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_026285"
FT VARIANT 1034
FT /note="S -> N (in dbSNP:rs12066671)"
FT /id="VAR_056934"
FT CONFLICT 25
FT /note="R -> P (in Ref. 4; BAB84979)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1076 AA; 120275 MW; 682D8C008BE77F1A CRC64;
MAEFTSYKET ASSRHLRFKL QSLSRRLDEL EEATKNLQKA EDELLDLQDK VIQAEGSNSS
MLAEIEVLRQ RVLRIEGKDE EIKRAEDLCR LMKEKLEEEE NLTRELKSEI ERLQKRMAEL
EKLEEAFSRS KNDCTQLCLS LNEERNLTKK ISSELEMLRV KVKELESSED RLDKTEQSLA
SELEKLKSLT LSFVSERKYL NEKEKENEKL IKELTQKLEQ NKKMNRDYTR NASNLERNDL
RIEDGISSTL PSKESRRKGG LDYLKQVENE TRNKSENEKN RNQEDNKVKD LNQEIEKLKT
QIKHFESLEE ELKKMKSKNN DLQDNYLSEQ NKNKLLASQL EEIKLQIKKQ KELENGEVEG
EDAFLSSKGR HERTKFRGHG SEASVSKHTA RELSPQHKRE RLRNREFALN NENYSLSNRQ
VSSPSFTNRR AAKASHMGVS TDSGTQETKK TEDRFVPGSS QSEGKKSREQ PSVLSRYPPA
AQEHSKAWKG TSKPGTESGL KGKVEKTTRT FSDTTHGSVP SDPLGRADKA SDTSSETVFG
KRGHVLGNGS QVTQAANSGC SKAIGALASS RRSSSEGLSK GKKAANGLEA DNSCPNSKAP
VLSKYPYSCR SQENILQGFS TSHKEGVNQP AAVVMEDSSP HEALRCRVIK SSGREKPDSD
DDLDIASLVT AKLVNTTITP EPEPKPQPNS REKAKTRGAP RTSLFENDKD AGMENESVKS
VRASTNTMEL PDTNGAGVKS QRPFSPREAL RSRAIIKPVI VDKDVKKIMG GSGTETTLEK
QKPVSKPGPN KVTSSITIYP SDSSSPRAAP GEALRERHTS TSNIQVGLAE LTSVSNHVSS
PFELSIHKHD ITLQLAEAER MADGPLKDRP ETVVSRSSII IKPSDPVERN SHAPPAETIR
WKSHSAPSEV GFSDARHVTV RNAWKSRRDL KSLEDPPTRI GKNVESTNSN AYTQRSSTDF
SELEQPRSCL FEQGTRRVGP SSGDAPEPSS RRTQSSLTVS EVLTRRNRVG DTITVAAWNH
SASMEEEGED CTLSVYRQLH NSLDPSELPG KQGLPESGRV RAEERLRPTR PCAEEN
