ID   CNTFR_HUMAN             Reviewed;         372 AA.
AC   P26992; Q5U050;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   24-JAN-2024, entry version 204.
DE   RecName: Full=Ciliary neurotrophic factor receptor subunit alpha;
DE            Short=CNTF receptor subunit alpha;
DE            Short=CNTFR-alpha;
DE   Flags: Precursor;
GN   Name=CNTFR;
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].
RX   PubMed=1648265; DOI=10.1126/science.1648265;
RA   Davis S., Aldrich T.H., Valenzuela D.M., Wong V., Furth M.E., Squinto S.P.,
RA   Yancopoulos G.D.;
RT   "The receptor for ciliary neurotrophic factor.";
RL   Science 253:59-63(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7774913; DOI=10.1016/0888-7543(95)80121-2;
RA   Valenzuela D.M., Rojas E., le Beau M.M., Espinosa R., Brannan C.I.,
RA   McClain J., Masiakowski P., Ip N.Y., Copeland N.G., Jenkins N.A.,
RA   Yancopoulos G.D.;
RT   "Genomic organization and chromosomal localization of the human and mouse
RT   genes encoding the alpha receptor component for ciliary neurotrophic
RT   factor.";
RL   Genomics 25:157-163(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [7]
RP   FUNCTION, AND IDENTIFICATION IN HUMANIN RECEPTOR COMPLEX.
RX   PubMed=19386761; DOI=10.1091/mbc.e09-02-0168;
RA   Hashimoto Y., Kurita M., Aiso S., Nishimoto I., Matsuoka M.;
RT   "Humanin inhibits neuronal cell death by interacting with a cytokine
RT   receptor complex or complexes involving CNTF receptor alpha/WSX-1/gp130.";
RL   Mol. Biol. Cell 20:2864-2873(2009).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH CLCF1; CRLF1 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   STRUCTURE BY NMR OF 202-305.
RX   PubMed=12707266; DOI=10.1074/jbc.m301976200;
RA   Man D., He W., Sze K.H., Gong K., Smith D.K., Zhu G., Ip N.Y.;
RT   "Solution structure of the C-terminal domain of the ciliary neurotrophic
RT   factor (CNTF) receptor and ligand free associations among components of the
RT   CNTF receptor complex.";
RL   J. Biol. Chem. 278:23285-23294(2003).
CC   -!- FUNCTION: Binds to CNTF. The alpha subunit provides the receptor
CC       specificity. Receptor for heterodimeric neurotropic cytokine composed
CC       of CLCF1/CLC and CRLF1/CLF-1 (PubMed:26858303). Acts as a receptor for
CC       the neuroprotective peptide humanin as part of a complex with
CC       IL6ST/GP130 and IL27RA/WSX1 (PubMed:19386761).
CC       {ECO:0000269|PubMed:19386761, ECO:0000269|PubMed:26858303}.
CC   -!- SUBUNIT: Forms a heterotrimer with LIFR and IL6ST. Interacts with
CC       heterodimeric neurotropic cytokine composed of CLCF1/CLC and CRLF1/CLF-
CC       1 (PubMed:26858303). Either alone or in complex with the heterodimer
CC       CLCF1-CRLF1 interacts with SORL1; this interaction may promote
CC       internalization and lysosomal degradation (PubMed:26858303). Component
CC       of a receptor complex composed of IL6ST/GP130, IL27RA/WSX1 and CNTFR
CC       which interacts with the neuroprotective peptide humanin
CC       (PubMed:19386761). {ECO:0000269|PubMed:19386761,
CC       ECO:0000269|PubMed:26858303}.
CC   -!- INTERACTION:
CC       P26992; PRO_0000015616 [Q9UBD9]: CLCF1; NbExp=3; IntAct=EBI-743758, EBI-25298664;
CC       P26992; P26441: CNTF; NbExp=13; IntAct=EBI-743758, EBI-1050897;
CC       P26992; Q92673: SORL1; NbExp=7; IntAct=EBI-743758, EBI-1171329;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- TISSUE SPECIFICITY: Nervous system and skeletal muscle.
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   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; M73238; AAA35707.1; -; mRNA.
DR   EMBL; L38025; AAA91337.1; -; Genomic_DNA.
DR   EMBL; L38022; AAA91337.1; JOINED; Genomic_DNA.
DR   EMBL; L38023; AAA91337.1; JOINED; Genomic_DNA.
DR   EMBL; L38024; AAA91337.1; JOINED; Genomic_DNA.
DR   EMBL; BT019824; AAV38627.1; -; mRNA.
DR   EMBL; AL160270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58445.1; -; Genomic_DNA.
DR   EMBL; CH471071; EAW58446.1; -; Genomic_DNA.
DR   EMBL; CH471071; EAW58447.1; -; Genomic_DNA.
DR   EMBL; CH471071; EAW58448.1; -; Genomic_DNA.
DR   EMBL; BC001492; AAH01492.1; -; mRNA.
DR   CCDS; CCDS6558.1; -.
DR   PIR; A40854; UHHUCN.
DR   RefSeq; NP_001193940.1; NM_001207011.1.
DR   RefSeq; NP_001833.1; NM_001842.4.
DR   RefSeq; NP_671693.1; NM_147164.2.
DR   RefSeq; XP_016869752.1; XM_017014263.1.
DR   RefSeq; XP_016869753.1; XM_017014264.1.
DR   RefSeq; XP_016869754.1; XM_017014265.1.
DR   PDB; 1UC6; NMR; -; A=202-305.
DR   PDB; 8D74; EM; 3.03 A; C=23-342.
DR   PDB; 8D7E; EM; 2.93 A; C=23-342.
DR   PDB; 8D7H; EM; 3.40 A; C/G=23-342.
DR   PDB; 8D7R; EM; 3.90 A; C=23-346.
DR   PDBsum; 1UC6; -.
DR   PDBsum; 8D74; -.
DR   PDBsum; 8D7E; -.
DR   PDBsum; 8D7H; -.
DR   PDBsum; 8D7R; -.
DR   AlphaFoldDB; P26992; -.
DR   BMRB; P26992; -.
DR   EMDB; EMD-27227; -.
DR   EMDB; EMD-27228; -.
DR   EMDB; EMD-27229; -.
DR   EMDB; EMD-27230; -.
DR   EMDB; EMD-27231; -.
DR   SMR; P26992; -.
DR   BioGRID; 107671; 18.
DR   CORUM; P26992; -.
DR   DIP; DIP-5777N; -.
DR   IntAct; P26992; 15.
DR   MINT; P26992; -.
DR   STRING; 9606.ENSP00000368265; -.
DR   TCDB; 8.A.152.2.1; the interleukin receptor (ilr) family.
DR   GlyCosmos; P26992; 4 sites, No reported glycans.
DR   GlyGen; P26992; 4 sites.
DR   PhosphoSitePlus; P26992; -.
DR   BioMuta; CNTFR; -.
DR   DMDM; 1352099; -.
DR   EPD; P26992; -.
DR   jPOST; P26992; -.
DR   MassIVE; P26992; -.
DR   PaxDb; 9606-ENSP00000368265; -.
DR   PeptideAtlas; P26992; -.
DR   ProteomicsDB; 54371; -.
DR   Antibodypedia; 25488; 365 antibodies from 39 providers.
DR   DNASU; 1271; -.
DR   Ensembl; ENST00000351266.8; ENSP00000242338.4; ENSG00000122756.15.
DR   Ensembl; ENST00000378980.8; ENSP00000368265.3; ENSG00000122756.15.
DR   Ensembl; ENST00000610543.4; ENSP00000480451.1; ENSG00000122756.15.
DR   GeneID; 1271; -.
DR   KEGG; hsa:1271; -.
DR   MANE-Select; ENST00000378980.8; ENSP00000368265.3; NM_147164.3; NP_671693.1.
DR   UCSC; uc003zup.2; human.
DR   AGR; HGNC:2170; -.
DR   CTD; 1271; -.
DR   DisGeNET; 1271; -.
DR   GeneCards; CNTFR; -.
DR   HGNC; HGNC:2170; CNTFR.
DR   HPA; ENSG00000122756; Tissue enhanced (brain, skeletal muscle).
DR   MIM; 118946; gene.
DR   neXtProt; NX_P26992; -.
DR   OpenTargets; ENSG00000122756; -.
DR   PharmGKB; PA26684; -.
DR   VEuPathDB; HostDB:ENSG00000122756; -.
DR   eggNOG; ENOG502QUDK; Eukaryota.
DR   GeneTree; ENSGT00940000158864; -.
DR   InParanoid; P26992; -.
DR   OMA; KICDTGE; -.
DR   OrthoDB; 5346848at2759; -.
DR   PhylomeDB; P26992; -.
DR   TreeFam; TF331210; -.
DR   PathwayCommons; P26992; -.
DR   Reactome; R-HSA-6788467; IL-6-type cytokine receptor ligand interactions.
DR   SignaLink; P26992; -.
DR   SIGNOR; P26992; -.
DR   BioGRID-ORCS; 1271; 8 hits in 1141 CRISPR screens.
DR   ChiTaRS; CNTFR; human.
DR   EvolutionaryTrace; P26992; -.
DR   GenomeRNAi; 1271; -.
DR   Pharos; P26992; Tbio.
DR   PRO; PR:P26992; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; P26992; Protein.
DR   Bgee; ENSG00000122756; Expressed in ventricular zone and 99 other cell types or tissues.
DR   ExpressionAtlas; P26992; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:CACAO.
DR   GO; GO:0070110; C:ciliary neurotrophic factor receptor complex; IDA:BHF-UCL.
DR   GO; GO:0097059; C:CNTFR-CLCF1 complex; IDA:BHF-UCL.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0019898; C:extrinsic component of membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0004897; F:ciliary neurotrophic factor receptor activity; TAS:ProtInc.
DR   GO; GO:0019955; F:cytokine binding; IPI:HGNC-UCL.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR   GO; GO:0003360; P:brainstem development; IEA:Ensembl.
DR   GO; GO:0070120; P:ciliary neurotrophic factor-mediated signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
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; IMP:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0007548; P:sex differentiation; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR   GO; GO:0060538; P:skeletal muscle organ development; IEA:Ensembl.
DR   GO; GO:0001967; P:suckling behavior; IEA:Ensembl.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR003530; Hematopoietin_rcpt_L_F3_CS.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   PANTHER; PTHR23036:SF21; CILIARY NEUROTROPHIC FACTOR RECEPTOR SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR23036; CYTOKINE RECEPTOR; 1.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS01354; HEMATOPO_REC_L_F3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   Genevisible; P26992; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Receptor; Reference proteome;
KW   Repeat; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..342
FT                   /note="Ciliary neurotrophic factor receptor subunit alpha"
FT                   /id="PRO_0000010991"
FT   PROPEP          343..372
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010992"
FT   DOMAIN          27..104
FT                   /note="Ig-like C2-type"
FT   DOMAIN          108..205
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          206..306
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          301..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           290..294
FT                   /note="WSXWS motif"
FT   COMPBIAS        312..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           342
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        60
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        46..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          51..53
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          55..59
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          73..76
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:8D7H"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          97..106
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          113..119
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          121..123
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          126..130
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          140..147
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          159..162
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          177..184
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          189..196
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   TURN            198..200
FT                   /evidence="ECO:0007829|PDB:8D7H"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          223..225
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          243..251
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          255..258
FT                   /evidence="ECO:0007829|PDB:8D74"
FT   STRAND          261..266
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          272..274
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          276..280
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          283..288
FT                   /evidence="ECO:0007829|PDB:8D7E"
FT   STRAND          295..299
FT                   /evidence="ECO:0007829|PDB:1UC6"
SQ   SEQUENCE   372 AA;  40633 MW;  B2F3F73DE8F8750E CRC64;
     MAAPVPWACC AVLAAAAAVV YAQRHSPQEA PHVQYERLGS DVTLPCGTAN WDAAVTWRVN
     GTDLAPDLLN GSQLVLHGLE LGHSGLYACF HRDSWHLRHQ VLLHVGLPPR EPVLSCRSNT
     YPKGFYCSWH LPTPTYIPNT FNVTVLHGSK IMVCEKDPAL KNRCHIRYMH LFSTIKYKVS
     ISVSNALGHN ATAITFDEFT IVKPDPPENV VARPVPSNPR RLEVTWQTPS TWPDPESFPL
     KFFLRYRPLI LDQWQHVELS DGTAHTITDA YAGKEYIIQV AAKDNEIGTW SDWSVAAHAT
     PWTEEPRHLT TEAQAAETTT STTSSLAPPP TTKICDPGEL GSGGGPSAPF LVSVPITLAL
     AAAAATASSL LI
//