CRLF2_HUMAN
ID CRLF2_HUMAN Reviewed; 371 AA.
AC Q9HC73; J3QKD1; Q5G7M1; Q9H5R3;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cytokine receptor-like factor 2;
DE AltName: Full=Cytokine receptor-like 2;
DE AltName: Full=IL-XR;
DE AltName: Full=Thymic stromal lymphopoietin protein receptor;
DE Short=TSLP receptor;
DE Flags: Precursor;
GN Name=CRLF2; Synonyms=CRL2, ILXR, TSLPR;
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 1).
RC TISSUE=Dendritic cell;
RX PubMed=11237741; DOI=10.1006/bbrc.2001.4432;
RA Zhang W., Wang J., Wang Q., Chen G., Zhang J., Chen T., Wan T., Zhang Y.,
RA Cao X.;
RT "Identification of a novel type I cytokine receptor CRL2 preferentially
RT expressed by human dendritic cells and activated monocytes.";
RL Biochem. Biophys. Res. Commun. 281:878-883(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=T-cell;
RX PubMed=11474172; DOI=10.1159/000056941;
RA Tonozuka Y., Fujio K., Sugiyama T., Nosaka T., Hirai M., Kitamura T.;
RT "Molecular cloning of a human novel type I cytokine receptor related to
RT delta1/TSLPR.";
RL Cytogenet. Cell Genet. 93:23-25(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A RECEPTOR FOR
RP TSLP.
RX PubMed=11418668; DOI=10.4049/jimmunol.167.1.336;
RA Reche P.A., Soumelis V., Gorman D.M., Clifford T., Liu M.-R., Travis M.,
RA Zurawski S.M., Johnston J., Liu Y.-J., Spits H., de Waal Malefyt R.,
RA Kastelein R.A., Bazan J.F.;
RT "Human thymic stromal lymphopoietin preferentially stimulates myeloid
RT cells.";
RL J. Immunol. 167:336-343(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Li T., Yu X., Cao J., Wang S., Li X., Cui Q., Chen J., Zhang S., Chang Z.,
RA Fu X., Liu L.;
RT "Human thymic stromal lymphopoietin receptor presents three splicing
RT variants in selected tumor cells and functionally cooperates with IL-2
RT receptor beta to activate mitogenic signals.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
CC -!- FUNCTION: Receptor for thymic stromal lymphopoietin (TSLP). Forms a
CC functional complex with TSLP and IL7R which is capable of stimulating
CC cell proliferation through activation of STAT3 and STAT5. Also
CC activates JAK2 (By similarity). Implicated in the development of the
CC hematopoietic system. {ECO:0000250, ECO:0000269|PubMed:11418668}.
CC -!- SUBUNIT: Heterodimer of CRLF2 and IL7R.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HC73-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HC73-2; Sequence=VSP_008786, VSP_008787;
CC Name=3;
CC IsoId=Q9HC73-3; Sequence=VSP_057463;
CC -!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, kidney and
CC adult and fetal liver. Primarily expressed in dendrites and monocytes.
CC Weakly expressed in T-cells.
CC -!- INDUCTION: Up-regulated in activated peripheral monocytes and THP-1
CC cells.
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 -!- DOMAIN: The box 1 motif is important for association with JAKs.
CC -!- MISCELLANEOUS: The gene coding for this protein is located in the
CC pseudoautosomal region 1 (PAR1) of X and Y chromosomes.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
CC subfamily. {ECO:0000305}.
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DR EMBL; AF142570; AAG27923.1; -; mRNA.
DR EMBL; AB052639; BAB60717.1; -; mRNA.
DR EMBL; AF338733; AAK60618.1; -; mRNA.
DR EMBL; AY775789; AAW66851.1; -; mRNA.
DR EMBL; AK026800; BAB15557.1; -; mRNA.
DR EMBL; AC188046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX908382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS75944.1; -. [Q9HC73-3]
DR CCDS; CCDS75945.1; -. [Q9HC73-1]
DR RefSeq; NP_001012288.2; NM_001012288.2. [Q9HC73-3]
DR RefSeq; NP_071431.2; NM_022148.3. [Q9HC73-1]
DR PDB; 5J11; X-ray; 2.56 A; C=1-221.
DR PDB; 5J12; X-ray; 3.55 A; C=1-221.
DR PDBsum; 5J11; -.
DR PDBsum; 5J12; -.
DR AlphaFoldDB; Q9HC73; -.
DR SASBDB; Q9HC73; -.
DR SMR; Q9HC73; -.
DR BioGRID; 122066; 71.
DR STRING; 9606.ENSP00000383641; -.
DR GlyGen; Q9HC73; 4 sites.
DR iPTMnet; Q9HC73; -.
DR PhosphoSitePlus; Q9HC73; -.
DR BioMuta; CRLF2; -.
DR DMDM; 38257768; -.
DR MassIVE; Q9HC73; -.
DR PaxDb; Q9HC73; -.
DR PeptideAtlas; Q9HC73; -.
DR PRIDE; Q9HC73; -.
DR Antibodypedia; 23333; 502 antibodies from 34 providers.
DR DNASU; 64109; -.
DR Ensembl; ENST00000381566.6; ENSP00000370978.2; ENSG00000205755.12. [Q9HC73-1]
DR Ensembl; ENST00000381567.8; ENSP00000370979.4; ENSG00000205755.12. [Q9HC73-3]
DR Ensembl; ENST00000400841.8; ENSP00000383641.3; ENSG00000205755.12. [Q9HC73-1]
DR GeneID; 64109; -.
DR KEGG; hsa:64109; -.
DR MANE-Select; ENST00000400841.8; ENSP00000383641.3; NM_022148.4; NP_071431.2.
DR UCSC; uc004cpl.4; human.
DR UCSC; uc022brs.3; human. [Q9HC73-1]
DR CTD; 64109; -.
DR DisGeNET; 64109; -.
DR GeneCards; CRLF2; -.
DR HGNC; HGNC:14281; CRLF2.
DR HPA; ENSG00000205755; Tissue enhanced (bone marrow, gallbladder, lymphoid tissue).
DR MalaCards; CRLF2; -.
DR MIM; 300357; gene.
DR MIM; 400023; gene.
DR neXtProt; NX_Q9HC73; -.
DR OpenTargets; ENSG00000205755; -.
DR PharmGKB; PA26883; -.
DR VEuPathDB; HostDB:ENSG00000205755; -.
DR eggNOG; ENOG502RYG2; Eukaryota.
DR GeneTree; ENSGT00510000049974; -.
DR HOGENOM; CLU_060544_0_0_1; -.
DR InParanoid; Q9HC73; -.
DR OMA; LYEIQYK; -.
DR PhylomeDB; Q9HC73; -.
DR TreeFam; TF342693; -.
DR PathwayCommons; Q9HC73; -.
DR Reactome; R-HSA-1266695; Interleukin-7 signaling.
DR SignaLink; Q9HC73; -.
DR SIGNOR; Q9HC73; -.
DR BioGRID-ORCS; 64109; 2 hits in 161 CRISPR screens.
DR ChiTaRS; CRLF2; human.
DR GenomeRNAi; 64109; -.
DR Pharos; Q9HC73; Tbio.
DR PRO; PR:Q9HC73; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9HC73; protein.
DR Bgee; ENSG00000205755; Expressed in vermiform appendix and 47 other tissues.
DR ExpressionAtlas; Q9HC73; baseline and differential.
DR Genevisible; Q9HC73; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005127; F:ciliary neurotrophic factor receptor binding; IBA:GO_Central.
DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IDA:UniProtKB.
DR GO; GO:0004923; F:leukemia inhibitory factor receptor activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0038165; P:oncostatin-M-mediated signaling pathway; IEA:GOC.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0032754; P:positive regulation of interleukin-5 production; IMP:UniProtKB.
DR GO; GO:0033005; P:positive regulation of mast cell activation; IMP:UniProtKB.
DR GO; GO:1904894; P:positive regulation of receptor signaling pathway via STAT; IDA:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..371
FT /note="Cytokine receptor-like factor 2"
FT /id="PRO_0000011041"
FT TOPO_DOM 23..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 118..211
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 322..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 200..204
FT /note="WSXWS motif"
FT MOTIF 261..269
FT /note="Box 1 motif"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 71..84
FT /evidence="ECO:0000250|UniProtKB:Q8CII9"
FT DISULFID 180..218
FT /evidence="ECO:0000250|UniProtKB:Q8CII9"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_057463"
FT VAR_SEQ 162..233
FT /note="SKQENTCNVTIEGLDAEKCYSFWVRVKAMEDVYGPDTYPSDWSEVTCWQRGE
FT IRDACAETPTPPKPKLSKFI -> TQSRSVTQAGVQWCDLCLLQPSPPRFKRFSCLSLP
FT SSWDYRHPPPRLANFCIISRDGVSPCWPGWSRTCDLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008786"
FT VAR_SEQ 234..371
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008787"
FT CONFLICT 27
FT /note="Missing (in Ref. 5; BAB15557)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="K -> R (in Ref. 4; AAW66851)"
FT CONFLICT 305
FT /note="E -> G (in Ref. 4; AAW66851)"
FT CONFLICT 358
FT /note="G -> D (in Ref. 4; AAW66851)"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:5J11"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:5J11"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:5J11"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 161..174
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:5J11"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:5J11"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:5J11"
SQ SEQUENCE 371 AA; 42013 MW; DEA53814758B69E4 CRC64;
MGRLVLLWGA AVFLLGGWMA LGQGGAAEGV QIQIIYFNLE TVQVTWNASK YSRTNLTFHY
RFNGDEAYDQ CTNYLLQEGH TSGCLLDAEQ RDDILYFSIR NGTHPVFTAS RWMVYYLKPS
SPKHVRFSWH QDAVTVTCSD LSYGDLLYEV QYRSPFDTEW QSKQENTCNV TIEGLDAEKC
YSFWVRVKAM EDVYGPDTYP SDWSEVTCWQ RGEIRDACAE TPTPPKPKLS KFILISSLAI
LLMVSLLLLS LWKLWRVKKF LIPSVPDPKS IFPGLFEIHQ GNFQEWITDT QNVAHLHKMA
GAEQESGPEE PLVVQLAKTE AESPRMLDPQ TEEKEASGGS LQLPHQPLQG GDVVTIGGFT
FVMNDRSYVA L
