CRLF1_HUMAN
ID CRLF1_HUMAN Reviewed; 422 AA.
AC O75462; Q9UHH5;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Cytokine receptor-like factor 1;
DE AltName: Full=Cytokine-like factor 1;
DE Short=CLF-1;
DE AltName: Full=ZcytoR5;
DE Flags: Precursor;
GN Name=CRLF1; ORFNames=UNQ288/PRO327;
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], SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Fetal lung;
RX PubMed=9686600;
RA Elson G.C.A., Graber P., Losberger C., Herren S., Gretener D., Menoud L.N.,
RA Wells T.N.C., Kosco-Vilbois M.H., Gauchat J.-F.;
RT "Cytokine-like factor-1, a novel soluble protein, shares homology with
RT members of the cytokine type I receptor family.";
RL J. Immunol. 161:1371-1379(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Magrangeas F., Jacques Y., Minvielle S.;
RT "Cloning and expression of a novel soluble protein containing hematopoietic
RT cytokine receptor domains.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lok S., Presnell S.R., Jelmberg A.C., Gilbert T., Whitmore T.E.,
RA Foster D.C., Adams R.L., Lehner J.M., O'Hara P.J.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 PROTEIN SEQUENCE OF 38-52.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP INTERACTION WITH CLCF1 AND CNTFR.
RX PubMed=10966616; DOI=10.1038/78765;
RA Elson G.C.A., Lelievre E., Guillet C., Chevalier S., Plun-Favreau H.,
RA Froger J., Suard I., de Coignac A.B., Delneste Y., Bonnefoy J.-Y.,
RA Gauchat J.-F., Gascan H.;
RT "CLF associates with CLC to form a functional heteromeric ligand for the
RT CNTF receptor complex.";
RL Nat. Neurosci. 3:867-872(2000).
RN [8]
RP INTERACTION WITH CLCF1; CNTFR AND SORL1.
RX PubMed=26858303; DOI=10.1128/mcb.00917-15;
RA Larsen J.V., Kristensen A.M., Pallesen L.T., Bauer J., Vaegter C.B.,
RA Nielsen M.S., Madsen P., Petersen C.M.;
RT "Cytokine-like factor 1, an essential facilitator of cardiotrophin-like
RT cytokine:ciliary neurotrophic factor receptor alpha signaling and sorLA-
RT mediated turnover.";
RL Mol. Cell. Biol. 36:1272-1286(2016).
RN [9]
RP VARIANTS CISS1 HIS-81 AND ARG-374.
RX PubMed=12509788; DOI=10.1086/346120;
RA Knappskog P.M., Majewski J., Livneh A., Nilsen P.T.E., Bringsli J.S.,
RA Ott J., Boman H.;
RT "Cold-induced sweating syndrome is caused by mutations in the CRLF1 gene.";
RL Am. J. Hum. Genet. 72:375-383(2003).
RN [10]
RP VARIANT CISS1 CYS-284.
RX PubMed=16952376; DOI=10.1016/j.jns.2006.07.001;
RA Hahn A.F., Jones D.L., Knappskog P.M., Boman H., McLeod J.G.;
RT "Cold-induced sweating syndrome: a report of two cases and demonstration of
RT genetic heterogeneity.";
RL J. Neurol. Sci. 250:62-70(2006).
RN [11]
RP VARIANT CISS1 GLY-76.
RX PubMed=17436251; DOI=10.1086/513608;
RA Dagoneau N., Bellais S., Blanchet P., Sarda P., Al-Gazali L.I.,
RA Di Rocco M., Huber C., Djouadi F., Le Goff C., Munnich A.,
RA Cormier-Daire V.;
RT "Mutations in cytokine receptor-like factor 1 (CRLF1) account for both
RT Crisponi and cold-induced sweating syndromes.";
RL Am. J. Hum. Genet. 80:966-970(2007).
RN [12]
RP VARIANT CISS1 GLY-76.
RX PubMed=17436252; DOI=10.1086/516843;
RA Crisponi L., Crisponi G., Meloni A., Toliat M.R., Nurnberg G., Usala G.,
RA Uda M., Masala M., Hohne W., Becker C., Marongiu M., Chiappe F., Kleta R.,
RA Rauch A., Wollnik B., Strasser F., Reese T., Jakobs C., Kurlemann G.,
RA Cao A., Nurnberg P., Rutsch F.;
RT "Crisponi syndrome is caused by mutations in the CRLF1 gene and is allelic
RT to cold-induced sweating syndrome type 1.";
RL Am. J. Hum. Genet. 80:971-981(2007).
RN [13]
RP VARIANTS CISS1 ASP-75; ILE-113 AND PRO-114.
RX PubMed=21326283; DOI=10.1038/ejhg.2010.253;
RA Herholz J., Meloni A., Marongiu M., Chiappe F., Deiana M., Herrero C.R.,
RA Zampino G., Hamamy H., Zalloum Y., Waaler P.E., Crisponi G., Crisponi L.,
RA Rutsch F.;
RT "Differential secretion of the mutated protein is a major component
RT affecting phenotypic severity in CRLF1-associated disorders.";
RL Eur. J. Hum. Genet. 19:525-533(2011).
RN [14]
RP VARIANT CISS1 LEU-138.
RX PubMed=23026229; DOI=10.1016/j.braindev.2012.08.011;
RA Tuysuz B., Kasapcopur O., Yalcinkaya C., Isik Hasiloglu Z., Knappskog P.M.,
RA Boman H.;
RT "Multiple small hyperintense lesions in the subcortical white matter on
RT cranial MR images in two Turkish brothers with cold-induced sweating
RT syndrome caused by a novel missense mutation in the CRLF1 gene.";
RL Brain Dev. 35:596-601(2013).
RN [15]
RP VARIANTS CISS1 PRO-74; PRO-145; CYS-216; SER-268; PRO-312 AND CYS-340.
RX PubMed=24488861; DOI=10.1002/humu.22522;
RA Piras R., Chiappe F., Torraca I.L., Buers I., Usala G., Angius A.,
RA Akin M.A., Basel-Vanagaite L., Benedicenti F., Chiodin E., El Assy O.,
RA Feingold-Zadok M., Guibert J., Kamien B., Kasapkara C.S., Kilic E.,
RA Boduroglu K., Kurtoglu S., Manzur A.Y., Onal E.E., Paderi E., Roche C.H.,
RA Tumer L., Unal S., Utine G.E., Zanda G., Zankl A., Zampino G., Crisponi G.,
RA Crisponi L., Rutsch F.;
RT "Expanding the mutational spectrum of CRLF1 in Crisponi/CISS1 syndrome.";
RL Hum. Mutat. 35:424-433(2014).
CC -!- FUNCTION: In complex with CLCF1, forms a heterodimeric neurotropic
CC cytokine that plays a crucial role during neuronal development
CC (Probable). May also play a regulatory role in the immune system.
CC {ECO:0000305|PubMed:26858303}.
CC -!- SUBUNIT: Forms covalent di- and tetramers. Forms a heteromeric complex
CC with cardiotrophin-like cytokine CLCF1/CLC; the CRLF1-CLCF1 complex is
CC a ligand for the ciliary neurotrophic factor receptor/CNTFR
CC (PubMed:9686600, PubMed:26858303). The CRLF1-CLCF1 heterodimer binds
CC SORL1 (via N-terminal ectodomain); within this complex, the interaction
CC is mediated predominantly by the CRLF1 moiety (PubMed:26858303). The
CC tripartite signaling complex formed by CRLF1, CLCF1 and CNTFR also
CC binds SORL1 (PubMed:26858303). {ECO:0000269|PubMed:26858303,
CC ECO:0000269|PubMed:9686600}.
CC -!- INTERACTION:
CC O75462; Q8NEV9: IL27; NbExp=2; IntAct=EBI-15587902, EBI-15887997;
CC O75462; Q92673: SORL1; NbExp=3; IntAct=EBI-15587902, EBI-1171329;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9686600}.
CC -!- TISSUE SPECIFICITY: Highest levels of expression observed in spleen,
CC thymus, lymph node, appendix, bone marrow, stomach, placenta, heart,
CC thyroid and ovary. Strongly expressed also in fetal lung.
CC {ECO:0000269|PubMed:9686600}.
CC -!- INDUCTION: Up-regulated in fibroblast primary cell cultures under
CC stimulation by IFNG/IFN-gamma, TNF and IL6/interleukin-6.
CC {ECO:0000269|PubMed:9686600}.
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding.
CC -!- DISEASE: Crisponi/Cold-induced sweating syndrome 1 (CISS1)
CC [MIM:272430]: An autosomal recessive disorder characterized by profuse
CC sweating induced by cool surroundings (temperatures of 7 to 18 degrees
CC Celsius). Patients manifest, in the neonatal period, orofacial weakness
CC with impaired sucking and swallowing, resulting in poor feeding.
CC Affected infants show a tendency to startle, with contractions of the
CC facial muscles in response to tactile stimuli or during crying,
CC trismus, abundant salivation, and opisthotonus. These features are
CC referred to as Crisponi syndrome and can result in early death in
CC infancy. Patients who survive into childhood have hyperhidrosis, mainly
CC of the upper body, in response to cold temperatures, and sweat very
CC little with heat. Additional abnormalities include a high-arched
CC palate, nasal voice, depressed nasal bridge, inability to fully extend
CC the elbows and kyphoscoliosis. {ECO:0000269|PubMed:12509788,
CC ECO:0000269|PubMed:16952376, ECO:0000269|PubMed:17436251,
CC ECO:0000269|PubMed:17436252, ECO:0000269|PubMed:21326283,
CC ECO:0000269|PubMed:23026229, ECO:0000269|PubMed:24488861}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
CC subfamily. {ECO:0000305}.
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DR EMBL; AF059293; AAC28335.1; -; mRNA.
DR EMBL; AF073515; AAD39681.1; -; mRNA.
DR EMBL; AF178684; AAD54385.1; -; mRNA.
DR EMBL; AY358291; AAQ88658.1; -; mRNA.
DR EMBL; BC044634; AAH44634.1; -; mRNA.
DR CCDS; CCDS32962.1; -.
DR RefSeq; NP_004741.1; NM_004750.4.
DR AlphaFoldDB; O75462; -.
DR SMR; O75462; -.
DR BioGRID; 114670; 124.
DR DIP; DIP-61205N; -.
DR IntAct; O75462; 7.
DR STRING; 9606.ENSP00000376188; -.
DR GlyConnect; 1167; 3 N-Linked glycans (1 site).
DR GlyGen; O75462; 6 sites, 3 N-linked glycans (1 site).
DR iPTMnet; O75462; -.
DR PhosphoSitePlus; O75462; -.
DR BioMuta; CRLF1; -.
DR EPD; O75462; -.
DR jPOST; O75462; -.
DR MassIVE; O75462; -.
DR MaxQB; O75462; -.
DR PaxDb; O75462; -.
DR PeptideAtlas; O75462; -.
DR PRIDE; O75462; -.
DR ProteomicsDB; 50025; -.
DR Antibodypedia; 28115; 245 antibodies from 27 providers.
DR DNASU; 9244; -.
DR Ensembl; ENST00000392386.8; ENSP00000376188.2; ENSG00000006016.12.
DR GeneID; 9244; -.
DR KEGG; hsa:9244; -.
DR MANE-Select; ENST00000392386.8; ENSP00000376188.2; NM_004750.5; NP_004741.1.
DR UCSC; uc010ebt.3; human.
DR CTD; 9244; -.
DR DisGeNET; 9244; -.
DR GeneCards; CRLF1; -.
DR GeneReviews; CRLF1; -.
DR HGNC; HGNC:2364; CRLF1.
DR HPA; ENSG00000006016; Tissue enhanced (heart).
DR MalaCards; CRLF1; -.
DR MIM; 272430; phenotype.
DR MIM; 604237; gene.
DR neXtProt; NX_O75462; -.
DR OpenTargets; ENSG00000006016; -.
DR Orphanet; 157820; Cold-induced sweating syndrome.
DR Orphanet; 1545; Crisponi syndrome.
DR Orphanet; 930; Idiopathic achalasia.
DR PharmGKB; PA26882; -.
DR VEuPathDB; HostDB:ENSG00000006016; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000156569; -.
DR HOGENOM; CLU_017892_0_0_1; -.
DR InParanoid; O75462; -.
DR OMA; HKTRNQA; -.
DR OrthoDB; 144839at2759; -.
DR PhylomeDB; O75462; -.
DR TreeFam; TF106501; -.
DR BRENDA; 1.1.1.105; 2681.
DR PathwayCommons; O75462; -.
DR Reactome; R-HSA-6788467; IL-6-type cytokine receptor ligand interactions.
DR Reactome; R-HSA-9020956; Interleukin-27 signaling.
DR SignaLink; O75462; -.
DR SIGNOR; O75462; -.
DR BioGRID-ORCS; 9244; 10 hits in 1069 CRISPR screens.
DR GeneWiki; CRLF1; -.
DR GenomeRNAi; 9244; -.
DR Pharos; O75462; Tbio.
DR PRO; PR:O75462; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75462; protein.
DR Bgee; ENSG00000006016; Expressed in right coronary artery and 148 other tissues.
DR ExpressionAtlas; O75462; baseline and differential.
DR Genevisible; O75462; HS.
DR GO; GO:0097058; C:CRLF-CLCF1 complex; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0019955; F:cytokine binding; IPI:HGNC-UCL.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
DR GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR015152; Growth/epo_recpt_lig-bind.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF09067; EpoR_lig-bind; 1.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 38..422
FT /note="Cytokine receptor-like factor 1"
FT /id="PRO_0000011039"
FT DOMAIN 38..131
FT /note="Ig-like C2-type"
FT DOMAIN 137..232
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 237..341
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 332..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 327..331
FT /note="WSXWS motif"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM58"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 143..153
FT /evidence="ECO:0000250"
FT DISULFID 184..195
FT /evidence="ECO:0000250"
FT VARIANT 74
FT /note="L -> P (in CISS1; dbSNP:rs1295488778)"
FT /evidence="ECO:0000269|PubMed:24488861"
FT /id="VAR_070817"
FT VARIANT 75
FT /note="Y -> D (in CISS1)"
FT /evidence="ECO:0000269|PubMed:21326283"
FT /id="VAR_070818"
FT VARIANT 76
FT /note="W -> G (in CISS1; dbSNP:rs137853143)"
FT /evidence="ECO:0000269|PubMed:17436251,
FT ECO:0000269|PubMed:17436252"
FT /id="VAR_033113"
FT VARIANT 81
FT /note="R -> H (in CISS1; dbSNP:rs104894670)"
FT /evidence="ECO:0000269|PubMed:12509788"
FT /id="VAR_017865"
FT VARIANT 113
FT /note="N -> I (in CISS1; together with P-114)"
FT /evidence="ECO:0000269|PubMed:21326283"
FT /id="VAR_070819"
FT VARIANT 114
FT /note="L -> P (in CISS1; together with I-113;
FT dbSNP:rs774359694)"
FT /evidence="ECO:0000269|PubMed:21326283"
FT /id="VAR_070820"
FT VARIANT 138
FT /note="P -> L (in CISS1; dbSNP:rs137853930)"
FT /evidence="ECO:0000269|PubMed:23026229"
FT /id="VAR_070821"
FT VARIANT 145
FT /note="S -> P (in CISS1)"
FT /evidence="ECO:0000269|PubMed:24488861"
FT /id="VAR_070822"
FT VARIANT 176
FT /note="R -> K (in dbSNP:rs11672248)"
FT /id="VAR_028355"
FT VARIANT 216
FT /note="R -> C (in CISS1; dbSNP:rs556029569)"
FT /evidence="ECO:0000269|PubMed:24488861"
FT /id="VAR_070823"
FT VARIANT 268
FT /note="F -> S (in CISS1; dbSNP:rs761982168)"
FT /evidence="ECO:0000269|PubMed:24488861"
FT /id="VAR_070824"
FT VARIANT 284
FT /note="W -> C (in CISS1; dbSNP:rs137853927)"
FT /evidence="ECO:0000269|PubMed:16952376"
FT /id="VAR_070825"
FT VARIANT 312
FT /note="R -> P (in CISS1; dbSNP:rs137853933)"
FT /evidence="ECO:0000269|PubMed:24488861"
FT /id="VAR_070826"
FT VARIANT 340
FT /note="R -> C (in CISS1; dbSNP:rs771459625)"
FT /evidence="ECO:0000269|PubMed:24488861"
FT /id="VAR_070827"
FT VARIANT 374
FT /note="L -> R (in CISS1; dbSNP:rs104894668)"
FT /evidence="ECO:0000269|PubMed:12509788"
FT /id="VAR_017866"
FT CONFLICT 240
FT /note="D -> E (in Ref. 3; AAD54385)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 46302 MW; AD9DEFCB01B84228 CRC64;
MPAGRRGPAA QSARRPPPLL PLLLLLCVLG APRAGSGAHT AVISPQDPTL LIGSSLLATC
SVHGDPPGAT AEGLYWTLNG RRLPPELSRV LNASTLALAL ANLNGSRQRS GDNLVCHARD
GSILAGSCLY VGLPPEKPVN ISCWSKNMKD LTCRWTPGAH GETFLHTNYS LKYKLRWYGQ
DNTCEEYHTV GPHSCHIPKD LALFTPYEIW VEATNRLGSA RSDVLTLDIL DVVTTDPPPD
VHVSRVGGLE DQLSVRWVSP PALKDFLFQA KYQIRYRVED SVDWKVVDDV SNQTSCRLAG
LKPGTVYFVQ VRCNPFGIYG SKKAGIWSEW SHPTAASTPR SERPGPGGGA CEPRGGEPSS
GPVRRELKQF LGWLKKHAYC SNLSFRLYDQ WRAWMQKSHK TRNQDEGILP SGRRGTARGP
AR
