ID   GNL1_HUMAN              Reviewed;         607 AA.
AC   P36915; B0S838; Q96CT5;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Guanine nucleotide-binding protein-like 1;
DE   AltName: Full=GTP-binding protein HSR1;
GN   Name=GNL1; Synonyms=HSR1;
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 2).
RC   TISSUE=T-cell;
RX   PubMed=8180467; DOI=10.1007/bf00292335;
RA   Vernet C., Ribouchon M.-T., Chimini G., Pontarotti P.;
RT   "Structure and evolution of a member of a new subfamily of GTP-binding
RT   proteins mapping to the human MHC class I region.";
RL   Mamm. Genome 5:100-105(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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 1).
RC   TISSUE=Muscle, and Skin;
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   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-33; SER-34; THR-48;
RP   THR-50; SER-51; SER-324; SER-561; SER-562 AND SER-563, AND IDENTIFICATION
RP   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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; THR-50 AND SER-51, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
RP   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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND IDENTIFICATION BY
RP   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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; THR-50; SER-51 AND
RP   SER-68, 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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48; THR-50 AND SER-51, AND
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).
CC   -!- FUNCTION: Possible regulatory or functional link with the
CC       histocompatibility cluster.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P36915-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P36915-2; Sequence=VSP_026992, VSP_026993;
CC   -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC       characterized by a circular permutation of the GTPase motifs described
CC       by a G4-G1-G3 pattern.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR   EMBL; L25665; AAA66492.1; -; mRNA.
DR   EMBL; BT006648; AAP35294.1; -; mRNA.
DR   EMBL; AL662800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX000357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX248518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX927220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR388372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR936927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03294.1; -; Genomic_DNA.
DR   EMBL; BC013959; AAH13959.1; -; mRNA.
DR   EMBL; BC018366; AAH18366.1; -; mRNA.
DR   CCDS; CCDS4680.1; -. [P36915-1]
DR   PIR; I57013; I57013.
DR   RefSeq; NP_005266.2; NM_005275.3. [P36915-1]
DR   RefSeq; XP_005249072.1; XM_005249015.3.
DR   AlphaFoldDB; P36915; -.
DR   BioGRID; 109056; 129.
DR   IntAct; P36915; 16.
DR   STRING; 9606.ENSP00000365806; -.
DR   GlyGen; P36915; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P36915; -.
DR   PhosphoSitePlus; P36915; -.
DR   BioMuta; GNL1; -.
DR   DMDM; 158939140; -.
DR   EPD; P36915; -.
DR   jPOST; P36915; -.
DR   MassIVE; P36915; -.
DR   MaxQB; P36915; -.
DR   PaxDb; 9606-ENSP00000365806; -.
DR   PeptideAtlas; P36915; -.
DR   ProteomicsDB; 55237; -. [P36915-1]
DR   ProteomicsDB; 55238; -. [P36915-2]
DR   Pumba; P36915; -.
DR   Antibodypedia; 26307; 280 antibodies from 30 providers.
DR   DNASU; 2794; -.
DR   Ensembl; ENST00000376621.8; ENSP00000365806.3; ENSG00000204590.13. [P36915-1]
DR   Ensembl; ENST00000383596.6; ENSP00000373090.2; ENSG00000206492.11. [P36915-1]
DR   Ensembl; ENST00000417834.5; ENSP00000403576.1; ENSG00000226882.9. [P36915-1]
DR   Ensembl; ENST00000428189.5; ENSP00000409074.1; ENSG00000229470.9. [P36915-1]
DR   Ensembl; ENST00000437917.5; ENSP00000411162.1; ENSG00000228581.9. [P36915-1]
DR   Ensembl; ENST00000441604.5; ENSP00000394290.1; ENSG00000235986.9. [P36915-1]
DR   Ensembl; ENST00000454829.5; ENSP00000409367.1; ENSG00000232143.9. [P36915-1]
DR   GeneID; 2794; -.
DR   KEGG; hsa:2794; -.
DR   MANE-Select; ENST00000376621.8; ENSP00000365806.3; NM_005275.5; NP_005266.2.
DR   UCSC; uc003nqh.4; human. [P36915-1]
DR   AGR; HGNC:4413; -.
DR   CTD; 2794; -.
DR   DisGeNET; 2794; -.
DR   GeneCards; GNL1; -.
DR   HGNC; HGNC:4413; GNL1.
DR   HPA; ENSG00000204590; Low tissue specificity.
DR   MIM; 143024; gene.
DR   neXtProt; NX_P36915; -.
DR   OpenTargets; ENSG00000204590; -.
DR   PharmGKB; PA28792; -.
DR   VEuPathDB; HostDB:ENSG00000204590; -.
DR   eggNOG; KOG1424; Eukaryota.
DR   GeneTree; ENSGT00940000158047; -.
DR   HOGENOM; CLU_013649_1_1_1; -.
DR   InParanoid; P36915; -.
DR   OMA; CDFPVRP; -.
DR   OrthoDB; 130417at2759; -.
DR   PhylomeDB; P36915; -.
DR   TreeFam; TF324569; -.
DR   PathwayCommons; P36915; -.
DR   SignaLink; P36915; -.
DR   BioGRID-ORCS; 2794; 38 hits in 1149 CRISPR screens.
DR   ChiTaRS; GNL1; human.
DR   GenomeRNAi; 2794; -.
DR   Pharos; P36915; Tbio.
DR   PRO; PR:P36915; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P36915; Protein.
DR   Bgee; ENSG00000204590; Expressed in right testis and 99 other cell types or tissues.
DR   ExpressionAtlas; P36915; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR   GO; GO:0006974; P:DNA damage response; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR   GO; GO:0002456; P:T cell mediated immunity; NAS:UniProtKB.
DR   CDD; cd01857; HSR1_MMR1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR043358; GNL1-like.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR45709:SF7; GUANINE NUCLEOTIDE-BINDING PROTEIN-LIKE 1; 1.
DR   PANTHER; PTHR45709; LARGE SUBUNIT GTPASE 1 HOMOLOG-RELATED; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51721; G_CP; 1.
DR   Genevisible; P36915; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..607
FT                   /note="Guanine nucleotide-binding protein-like 1"
FT                   /id="PRO_0000122441"
FT   DOMAIN          178..418
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          547..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..583
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         225..228
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         367..374
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         411..415
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         33
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         48
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         50
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         324
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         561
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         562
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         563
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VAR_SEQ         1..177
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8180467"
FT                   /id="VSP_026992"
FT   VAR_SEQ         178..183
FT                   /note="WRQLWR -> MEAAVA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8180467"
FT                   /id="VSP_026993"
FT   CONFLICT        232..233
FT                   /note="PA -> RR (in Ref. 1; AAA66492)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        315
FT                   /note="Missing (in Ref. 1; AAA66492)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        339
FT                   /note="E -> EQ (in Ref. 1; AAA66492)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        514
FT                   /note="L -> V (in Ref. 1; AAA66492)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   607 AA;  68661 MW;  F8EBB4EDBB73D929 CRC64;
     MPRKKPFSVK QKKKQLQDKR ERKRGLQDGL RSSSNSRSGS RERREEQTDT SDGESVTHHI
     RRLNQQPSQG LGPRGYDPNR YRLHFERDSR EEVERRKRAA REQVLQPVSA ELLELDIREV
     YQPGSVLDFP RRPPWSYEMS KEQLMSQEER SFQDYLGKIH GAYSSEKLSY FEHNLETWRQ
     LWRVLEMSDI VLLITDIRHP VVNFPPALYE YVTGELGLAL VLVLNKVDLA PPALVVAWKH
     YFHQHYPQLH VVLFTSFPRD PRTPQDPSSV LKKSRRRGRG WTRALGPEQL LRACEAITVG
     KVDLSSWREK IARDVAGATW GNGSGEEEEE EDGPAVLVEQ QTDSAMEPTG PTQERYKDGV
     VTIGCVGFPN VGKSSLINGL VGRKVVSVSR TPGHTRYFQT YFLTPSVKLC DCPGLIFPSL
     LPRQLQVLAG IYPIAQIQEP YTAVGYLASR IPVQALLHLR HPEAEDPSAE HPWCAWDICE
     AWAEKRGYKT AKAARNDVYR AANSLLRLAV DGRLSLCFHP PGYSEQKGTW ESHPETTELV
     VLQGRVGPAG DEEEEEEEEL SSSCEEEGEE DRDADEEGEG DEETPTSAPG SSLAGRNPYA
     LLGEDEC
//