SP1_RAT
ID SP1_RAT Reviewed; 786 AA.
AC Q01714; Q8K4R0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Transcription factor Sp1;
GN Name=Sp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=1356762; DOI=10.1002/j.1460-2075.1992.tb05451.x;
RA Imataka H., Sogawa K., Yasumoto K., Kikuchi Y., Sasano K., Kobayashi A.,
RA Hayami M., Fujii-Kuriyama Y.;
RT "Two regulatory proteins that bind to the basic transcription element
RT (BTE), a GC box sequence in the promoter region of the rat P-4501A1 gene.";
RL EMBO J. 11:3663-3671(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-559, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=12379234; DOI=10.1016/s0006-291x(02)02419-1;
RA Takahara T., Kasahara D., Mori D., Yanagisawa S., Akanuma H.;
RT "The trans-spliced variants of Sp1 mRNA in rat.";
RL Biochem. Biophys. Res. Commun. 298:156-162(2002).
RN [3]
RP FUNCTION, AND INTERACTION WITH SMARCA4/BRG1.
RX PubMed=19081374; DOI=10.1016/j.neuron.2008.09.040;
RA Qiu Z., Ghosh A.;
RT "A calcium-dependent switch in a CREST-BRG1 complex regulates activity-
RT dependent gene expression.";
RL Neuron 60:775-787(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-7, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcription factor that can activate or repress
CC transcription in response to physiological and pathological stimuli.
CC Binds with high affinity to GC-rich motifs and regulates the expression
CC of a large number of genes involved in a variety of processes such as
CC cell growth, apoptosis, differentiation and immune responses. Highly
CC regulated by post-translational modifications (phosphorylations,
CC sumoylation, proteolytic cleavage, glycosylation and acetylation).
CC Binds also the PDGFR-alpha G-box promoter. May have a role in
CC modulating the cellular response to DNA damage. Implicated in chromatin
CC remodeling. Plays an essential role in the regulation of FE65 gene
CC expression. Positively regulates the transcription of the core clock
CC component ARNTL/BMAL1 (By similarity). Plays a role in the recruitment
CC of SMARCA4/BRG1 on the c-FOS promoter (PubMed:19081374). Plays a role
CC in protecting cells against oxidative stress following brain injury by
CC regulating the expression of RNF112 (By similarity).
CC {ECO:0000250|UniProtKB:O89090, ECO:0000250|UniProtKB:P08047,
CC ECO:0000269|PubMed:19081374}.
CC -!- SUBUNIT: Interacts with ATF7IP, ATF7IP2, BAHD1, POGZ, HCFC1, AATF and
CC PHC2. Interacts with SV40 VP2/3 proteins. Interacts with SV40 major
CC capsid protein VP1; this interaction leads to a cooperativity between
CC the 2 proteins in DNA binding. Interacts with HLTF; the interaction may
CC be required for basal transcriptional activity of HLTF. Interacts
CC (deacetylated form) with EP300; the interaction enhances gene
CC expression. Interacts with HDAC1 and JUN. Interacts with ELF1; the
CC interaction is inhibited by glycosylation of SP1. Interaction with
CC NFYA; the interaction is inhibited by glycosylation of SP1 (By
CC similarity). Interacts with SMARCA4/BRG1 (PubMed:19081374). Interacts
CC with ATF7IP and TBP. Interacts with MEIS2 and PBX1. Interacts with
CC EGR1. Interacts with RNF112 in an oxidative stress-regulated manner (By
CC similarity). Interacts with ZBTB7A; ZBTB7A prevents the binding to GC-
CC rich motifs in promoters and represses the transcriptional activity of
CC SP1 (By similarity). Interacts with DDX3X; this interaction potentiates
CC SP1-induced CDKN1A/WAF1/CIP1 transcription (By similarity).
CC {ECO:0000250|UniProtKB:O89090, ECO:0000250|UniProtKB:P08047,
CC ECO:0000269|PubMed:19081374}.
CC -!- INTERACTION:
CC Q01714; P18576: Nfya; NbExp=2; IntAct=EBI-862787, EBI-862695;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O89090}. Cytoplasm
CC {ECO:0000250}. Note=Nuclear location is governed by
CC glycosylated/phosphorylated states. Insulin promotes nuclear location,
CC while glucagon favors cytoplasmic location (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including lung,
CC kidney, spleen and thymus. {ECO:0000269|PubMed:12379234}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:P08047}.
CC -!- PTM: Phosphorylated on multiple serine and threonine residues.
CC Phosphorylation is coupled to ubiquitination, sumoylation and
CC proteolytic processing. Phosphorylation on Ser-60 enhances proteolytic
CC cleavage. Phosphorylation on Ser-7 enhances ubiquitination and protein
CC degradation. Hyperphosphorylation on Ser-102 in response to DNA damage
CC has no effect on transcriptional activity. MAPK1/MAPK3-mediated
CC phosphorylation on Thr-454 and Thr-740 enhances VEGF transcription but,
CC represses FGF2-triggered PDGFR-alpha transcription. Also implicated in
CC the repression of RECK by ERBB2. Hyperphosphorylated on Thr-279 and
CC Thr-740 during mitosis by MAPK8 shielding SP1 from degradation by the
CC ubiquitin-dependent pathway. Phosphorylated in the zinc-finger domain
CC by calmodulin-activated PKCzeta. Phosphorylation on Ser-642 by PKCzeta
CC is critical for TSA-activated LHR gene expression through release of
CC its repressor, p107. Phosphorylation on Thr-669, Ser-671 and Thr-682 is
CC stimulated by angiotensin II via the AT1 receptor inducing increased
CC binding to the PDGF-D promoter. This phosphorylation is increased in
CC injured artey wall. Ser-60 and Thr-682 can both be dephosphorylated by
CC PP2A during cell-cycle interphase. Dephosphorylation on Ser-60 leads to
CC increased chromatin association during interphase and increases the
CC transcriptional activity. On insulin stimulation, sequentially
CC glycosylated and phosphorylated on several C-terminal serine and
CC threonine residues (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylated. Acetylation/deacetylation events affect
CC transcriptional activity. Deacetylation leads to an increase in the
CC expression the 12(s)-lipooxygenase gene though recruitment of p300 to
CC the promoter (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Ubiquitination occurs on the C-terminal
CC proteolytically-cleaved peptide and is triggered by phosphorylation (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Sumoylated with SUMO1. Sumoylation modulates proteolytic cleavage
CC of the N-terminal repressor domain. Sumoylation levels are attenuated
CC during tumorigenesis. Phosphorylation mediates SP1 desumoylation (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Proteolytic cleavage in the N-terminal repressor domain is
CC prevented by sumoylation. The C-terminal cleaved product is susceptible
CC to degradation (By similarity). {ECO:0000250}.
CC -!- PTM: O-glycosylated; Contains 8 N-acetylglucosamine side chains. Levels
CC are controlled by insulin and the SP1 phosphorylation states. Insulin-
CC mediated O-glycosylation locates SP1 to the nucleus, where it is
CC sequentially deglycosylated and phosphorylated. O-glycosylation affects
CC transcriptional activity through disrupting the interaction with a
CC number of transcription factors including ELF1 and NFYA. Inhibited by
CC peroxisomome proliferator receptor gamma (PPARgamma) (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; D12768; BAA02235.1; -; mRNA.
DR EMBL; AB077988; BAC05486.1; -; Genomic_DNA.
DR PIR; JS0747; JS0747.
DR RefSeq; NP_036787.2; NM_012655.2.
DR AlphaFoldDB; Q01714; -.
DR SMR; Q01714; -.
DR BioGRID; 246914; 7.
DR IntAct; Q01714; 2.
DR MINT; Q01714; -.
DR STRING; 10116.ENSRNOP00000019403; -.
DR GlyGen; Q01714; 6 sites.
DR iPTMnet; Q01714; -.
DR PhosphoSitePlus; Q01714; -.
DR PaxDb; Q01714; -.
DR PRIDE; Q01714; -.
DR Ensembl; ENSRNOT00000019403; ENSRNOP00000019403; ENSRNOG00000014084.
DR GeneID; 24790; -.
DR KEGG; rno:24790; -.
DR UCSC; RGD:3738; rat.
DR CTD; 6667; -.
DR RGD; 3738; Sp1.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157804; -.
DR HOGENOM; CLU_019688_2_0_1; -.
DR InParanoid; Q01714; -.
DR OMA; DLHQMNG; -.
DR OrthoDB; 1085860at2759; -.
DR PhylomeDB; Q01714; -.
DR TreeFam; TF350150; -.
DR Reactome; R-RNO-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-RNO-6807505; RNA polymerase II transcribes snRNA genes.
DR PRO; PR:Q01714; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000014084; Expressed in spleen and 19 other tissues.
DR Genevisible; Q01714; RN.
DR GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000791; C:euchromatin; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IDA:RGD.
DR GO; GO:0017053; C:transcription repressor complex; ISO:RGD.
DR GO; GO:0043425; F:bHLH transcription factor binding; ISO:RGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:0071837; F:HMG box domain binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:ARUK-UCL.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0060216; P:definitive hemopoiesis; ISO:RGD.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; ISO:RGD.
DR GO; GO:0001892; P:embryonic placenta development; ISO:RGD.
DR GO; GO:0060136; P:embryonic process involved in female pregnancy; ISO:RGD.
DR GO; GO:0048706; P:embryonic skeletal system development; ISO:RGD.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0030324; P:lung development; ISO:RGD.
DR GO; GO:0030219; P:megakaryocyte differentiation; ISO:RGD.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:RGD.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:1904828; P:positive regulation of hydrogen sulfide biosynthetic process; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0033194; P:response to hydroperoxide; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0001829; P:trophectodermal cell differentiation; ISO:RGD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Biological rhythms; Cytoplasm; DNA-binding;
KW Glycoprotein; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT CHAIN 2..786
FT /note="Transcription factor Sp1"
FT /id="PRO_0000047139"
FT ZN_FING 627..656
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 657..686
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 687..714
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..83
FT /note="Repressor domain"
FT /evidence="ECO:0000250"
FT REGION 110..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..252
FT /note="Transactivation domain A (Gln-rich)"
FT /evidence="ECO:0000250"
FT REGION 262..496
FT /note="Transactivation domain B (Gln-rich)"
FT /evidence="ECO:0000250"
FT REGION 281..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..611
FT /note="Transactivation domain C (highly charged)"
FT /evidence="ECO:0000250"
FT REGION 562..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..786
FT /note="VZV IE62-binding"
FT /evidence="ECO:0000250"
FT REGION 709..786
FT /note="Domain D"
FT /evidence="ECO:0000250"
FT MOTIF 463..471
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT COMPBIAS 29..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 64..65
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 102
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 279
FT /note="Phosphothreonine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 454
FT /note="Phosphothreonine; by MAPK1 and MAPK3"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 613
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 641
FT /note="Phosphothreonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 642
FT /note="Phosphoserine; by PKC/PRKCZ; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 652
FT /note="Phosphothreonine; by PKC/PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 669
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 671
FT /note="Phosphoserine; by PKC/PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 682
FT /note="Phosphothreonine; by PKC/PRKCZ"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 699
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 703
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 704
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT MOD_RES 740
FT /note="Phosphothreonine; by MAPK1, MAPK3 and MAPK8"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT CARBOHYD 492
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 613
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 641
FT /note="O-linked (GlcNAc) threonine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 642
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 699
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 703
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P08047"
FT CONFLICT 78
FT /note="N -> NEN (in Ref. 1; BAA02235)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 786 AA; 80772 MW; 3DE2AD93F95E7C0B CRC64;
MSDQDHSMDE VTAVKIEKGV GGNNGGSGNG GGAAFSQTRS SSTGSSSSSG GGGGQESQPS
PLALLAATCS RIESPNENSN NSQGPSQSGG TGELDLTATQ LSQGANGWQI ISSSSGATPT
SKEQSGNSTN GSNGSESSKN RTVSGGQYVV AATPNLQNQQ VLTGLPGVMP NIQYQVIPQF
QTVDGQQLQF AATGAQVQQD GSGQIQIIPG ANQQIITNRG SGGNIIAAMP NLLQQAVPLQ
GLANNVLSGQ TQYVTNVPVA LNGNITLLPV NSVSAATLTP SSQAGTISSS GSQESGSQPV
TSGTAISSAS LVSSQASSSS FFTNANSYST TTTTSNMGIM NFTSSGSSGT SSQGQTSQRV
GGLQGSDSLN IQQNQTSGGS LQGSQQKEGE QSQQTQQQQI LIQPQLVQGG QALQALQAAP
LSGQTFTTQA ISQETLQNLQ LQAVQNSGPI IIRTPTVGPN GQVSWQTLQL QNLQVQNPQA
QTITLAPMQG VSLGQTSSSN TTLTPIASAA SIPAGTVTVN AAQLSSMPGL QTINLSALGT
SGIQVHQLPG LPLAIANTPG DHGAQLGLHG PGGDGIHDET AGGEEGENSP DPQPQAGRRT
RREACTCPYC KDSEGRGSGD PGKKKQHICH IQGCGKVYGK TSHLRAHLRW HTGERPFMCN
WSYCGKRFTR SDELQRHKRT HTGEKKFACP ECPKRFMRSD HLSKHIKTHQ NKKGGPGVAL
SVGTLPLDSG AGSEGSGTAT PSALITTNMV AMEAICPEGI ARLANSGINV MQVTELQSIN
ISGNGF
