ID   NAB1_HUMAN              Reviewed;         487 AA.
AC   Q13506; O75383; O75384; Q6GTU1; Q9UEV1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=NGFI-A-binding protein 1;
DE   AltName: Full=EGR-1-binding protein 1;
DE   AltName: Full=Transcriptional regulatory protein p54;
GN   Name=NAB1;
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 LONG).
RC   TISSUE=Brain;
RX   PubMed=8668170; DOI=10.1128/mcb.16.7.3545;
RA   Svaren J., Sevetson B.R., Apel E.D., Zimonjic D.B., Popescu N.C.,
RA   Milbrandt J.;
RT   "NAB2, a corepressor of NGFI-A (Egr-1) and Krox20, is induced by
RT   proliferative and differentiative stimuli.";
RL   Mol. Cell. Biol. 16:3545-3553(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RA   Fan W.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103.
RA   Cao J., Fan W.;
RT   "Cloning and characterization of the 5' promoter region of human p54, a
RT   transcriptional repressor.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP   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   [7]
RP   SUMOYLATION AT LYS-333 AND LYS-480 BY EGR2.
RX   PubMed=21836637; DOI=10.1038/embor.2011.152;
RA   Garcia-Gutierrez P., Juarez-Vicente F., Gallardo-Chamizo F., Charnay P.,
RA   Garcia-Dominguez M.;
RT   "The transcription factor Krox20 is an E3 ligase that sumoylates its Nab
RT   coregulators.";
RL   EMBO Rep. 12:1018-1023(2011).
RN   [8]
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   [9]
RP   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   [10]
RP   IDENTIFICATION BY 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).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-333; LYS-355 AND LYS-480, 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   [12]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-129; LYS-333 AND LYS-480, 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   [13]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-333, AND IDENTIFICATION BY MASS
RP   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   [14]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-126; LYS-129; LYS-143; LYS-212;
RP   LYS-333; LYS-355; LYS-369; LYS-373; LYS-454; LYS-465; LYS-477 AND LYS-480,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [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).
RN   [15]
RP   STRUCTURE BY NMR OF 183-317.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the NCD2 domain in human transcriptional repressor
RT   NAB1 protein.";
RL   Submitted (APR-2008) to the PDB data bank.
CC   -!- FUNCTION: Acts as a transcriptional repressor for zinc finger
CC       transcription factors EGR1 and EGR2. {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimers may associate with EGR1 bound to DNA.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q13506-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q13506-2; Sequence=VSP_003384;
CC   -!- TISSUE SPECIFICITY: Isoform Short is found in myeloid leukemia cell
CC       line KG-1.
CC   -!- DOMAIN: The NAB conserved domain 1 (NCD1) interacts with EGR1
CC       inhibitory domain and mediates multimerization.
CC   -!- DOMAIN: The NAB conserved domain 2 (NCD2) is necessary for
CC       transcriptional repression.
CC   -!- SIMILARITY: Belongs to the NAB family. {ECO:0000305}.
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DR   EMBL; U47007; AAC50588.1; -; mRNA.
DR   EMBL; AF045451; AAC25085.1; -; mRNA.
DR   EMBL; AF045452; AAC25086.1; -; mRNA.
DR   EMBL; AC006460; AAX93076.1; -; Genomic_DNA.
DR   EMBL; BC035724; AAH35724.1; -; mRNA.
DR   EMBL; AF052744; AAC28325.1; -; Genomic_DNA.
DR   CCDS; CCDS2307.1; -. [Q13506-1]
DR   RefSeq; NP_001308241.1; NM_001321312.1. [Q13506-1]
DR   RefSeq; NP_001308242.1; NM_001321313.1. [Q13506-1]
DR   RefSeq; NP_001308243.1; NM_001321314.1.
DR   RefSeq; NP_001308244.1; NM_001321315.1.
DR   RefSeq; NP_005957.2; NM_005966.3. [Q13506-1]
DR   RefSeq; XP_005246639.1; XM_005246582.1. [Q13506-1]
DR   RefSeq; XP_005246640.1; XM_005246583.1. [Q13506-1]
DR   RefSeq; XP_011509521.1; XM_011511219.2. [Q13506-1]
DR   RefSeq; XP_016859659.1; XM_017004170.1. [Q13506-1]
DR   RefSeq; XP_016859665.1; XM_017004176.1. [Q13506-1]
DR   PDB; 2YUF; NMR; -; A=189-317.
DR   PDBsum; 2YUF; -.
DR   AlphaFoldDB; Q13506; -.
DR   SMR; Q13506; -.
DR   BioGRID; 110746; 27.
DR   IntAct; Q13506; 10.
DR   STRING; 9606.ENSP00000336894; -.
DR   GlyGen; Q13506; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q13506; -.
DR   PhosphoSitePlus; Q13506; -.
DR   BioMuta; NAB1; -.
DR   DMDM; 90109928; -.
DR   EPD; Q13506; -.
DR   jPOST; Q13506; -.
DR   MassIVE; Q13506; -.
DR   MaxQB; Q13506; -.
DR   PaxDb; 9606-ENSP00000336894; -.
DR   PeptideAtlas; Q13506; -.
DR   ProteomicsDB; 59502; -. [Q13506-1]
DR   ProteomicsDB; 59503; -. [Q13506-2]
DR   Pumba; Q13506; -.
DR   Antibodypedia; 1209; 385 antibodies from 27 providers.
DR   DNASU; 4664; -.
DR   Ensembl; ENST00000337386.10; ENSP00000336894.5; ENSG00000138386.17. [Q13506-1]
DR   Ensembl; ENST00000409581.5; ENSP00000387089.1; ENSG00000138386.17. [Q13506-1]
DR   GeneID; 4664; -.
DR   KEGG; hsa:4664; -.
DR   MANE-Select; ENST00000337386.10; ENSP00000336894.5; NM_005966.4; NP_005957.2.
DR   UCSC; uc002usb.4; human. [Q13506-1]
DR   AGR; HGNC:7626; -.
DR   CTD; 4664; -.
DR   DisGeNET; 4664; -.
DR   GeneCards; NAB1; -.
DR   HGNC; HGNC:7626; NAB1.
DR   HPA; ENSG00000138386; Low tissue specificity.
DR   MIM; 600800; gene.
DR   neXtProt; NX_Q13506; -.
DR   OpenTargets; ENSG00000138386; -.
DR   PharmGKB; PA31431; -.
DR   VEuPathDB; HostDB:ENSG00000138386; -.
DR   eggNOG; KOG3835; Eukaryota.
DR   GeneTree; ENSGT00390000006330; -.
DR   HOGENOM; CLU_561344_0_0_1; -.
DR   InParanoid; Q13506; -.
DR   OMA; SAGCYRQ; -.
DR   OrthoDB; 4181992at2759; -.
DR   PhylomeDB; Q13506; -.
DR   TreeFam; TF315501; -.
DR   PathwayCommons; Q13506; -.
DR   Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR   Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR   SignaLink; Q13506; -.
DR   BioGRID-ORCS; 4664; 13 hits in 1156 CRISPR screens.
DR   ChiTaRS; NAB1; human.
DR   EvolutionaryTrace; Q13506; -.
DR   GeneWiki; NAB1; -.
DR   GenomeRNAi; 4664; -.
DR   Pharos; Q13506; Tbio.
DR   PRO; PR:Q13506; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q13506; Protein.
DR   Bgee; ENSG00000138386; Expressed in ganglionic eminence and 209 other cell types or tissues.
DR   ExpressionAtlas; Q13506; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR   GO; GO:0042552; P:myelination; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; NAS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0045682; P:regulation of epidermis development; IEA:Ensembl.
DR   GO; GO:0014037; P:Schwann cell differentiation; IEA:Ensembl.
DR   Gene3D; 1.20.120.2010; NAB conserved domain 2; 1.
DR   InterPro; IPR006986; Nab1_C.
DR   InterPro; IPR006989; NAB_co-repressor_dom.
DR   InterPro; IPR039040; NAB_fam.
DR   InterPro; IPR006988; Nab_N.
DR   InterPro; IPR038398; NCD2_sf.
DR   PANTHER; PTHR12623; NGFI-A BINDING PROTEIN; 1.
DR   PANTHER; PTHR12623:SF9; NGFI-A-BINDING PROTEIN 1; 1.
DR   Pfam; PF04902; Nab1; 1.
DR   Pfam; PF04904; NCD1; 1.
DR   Pfam; PF04905; NCD2; 1.
DR   Genevisible; Q13506; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..486
FT                   /note="NGFI-A-binding protein 1"
FT                   /id="PRO_0000077038"
FT   REGION          4..82
FT                   /note="NCD1"
FT   REGION          162..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..310
FT                   /note="NCD2"
FT   REGION          307..338
FT                   /note="Necessary for nuclear localization"
FT                   /evidence="ECO:0000250"
FT   REGION          399..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..432
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61122"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61122"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61122"
FT   CROSSLNK        126
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        129
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        143
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        212
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        333
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000269|PubMed:21836637"
FT   CROSSLNK        333
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        355
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        369
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        373
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        454
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        465
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        477
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        480
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000269|PubMed:21836637"
FT   CROSSLNK        480
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         336..364
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_003384"
FT   CONFLICT        129
FT                   /note="K -> N (in Ref. 1; AAC50588)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        366
FT                   /note="Missing (in Ref. 1; AAC50588)"
FT                   /evidence="ECO:0000305"
FT   HELIX           193..209
FT                   /evidence="ECO:0007829|PDB:2YUF"
FT   HELIX           215..224
FT                   /evidence="ECO:0007829|PDB:2YUF"
FT   HELIX           227..232
FT                   /evidence="ECO:0007829|PDB:2YUF"
FT   HELIX           234..237
FT                   /evidence="ECO:0007829|PDB:2YUF"
FT   HELIX           243..252
FT                   /evidence="ECO:0007829|PDB:2YUF"
FT   STRAND          255..257
FT                   /evidence="ECO:0007829|PDB:2YUF"
FT   HELIX           272..286
FT                   /evidence="ECO:0007829|PDB:2YUF"
FT   HELIX           288..291
FT                   /evidence="ECO:0007829|PDB:2YUF"
FT   HELIX           294..310
FT                   /evidence="ECO:0007829|PDB:2YUF"
SQ   SEQUENCE   487 AA;  54401 MW;  385B16391D670059 CRC64;
     MAAALPRTLG ELQLYRILQK ANLLSYFDAF IQQGGDDVQQ LCEAGEEEFL EIMALVGMAS
     KPLHVRRLQK ALRDWVTNPG LFNQPLTSLP VSSIPIYKLP EGSPTWLGIS CSSYERSSNA
     REPHLKIPKC AATTCVQSLG QGKSDVVGSL ALQSVGESRL WQGHHATESE HSLSPADLGS
     PASPKESSEA LDAAAALSVA ECVERMAPTL PKSDLNEVKE LLKTNKKLAK MIGHIFEMND
     DDPHKEEEIR KYSAIYGRFD SKRKDGKHLT LHELTVNEAA AQLCVKDNAL LTRRDELFAL
     ARQISREVTY KYTYRTTKSK CGERDELSPK RIKVEDGFPD FQDSVQTLFQ QARAKSEELA
     ALSSQQPEKV MAKQMEFLCN QAGYERLQHA ERRLSAGLYR QSSEEHSPNG LTSDNSDGQG
     ERPLNLRMPN LQNRQPHHFV VDGELSRLYP SEAKSHSSES LGILKDYPHS AFTLEKKVIK
     TEPEDSR
//