FCRL2_HUMAN
ID FCRL2_HUMAN Reviewed; 508 AA.
AC Q96LA5; A0N0M5; A1L307; A6NMS0; Q6NTA1; Q9BZI4; Q9BZI5; Q9BZI6;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Fc receptor-like protein 2;
DE Short=FcR-like protein 2;
DE Short=FcRL2;
DE AltName: Full=Fc receptor homolog 2;
DE Short=FcRH2;
DE AltName: Full=IFGP family protein 4;
DE AltName: Full=Immunoglobulin receptor translocation-associated protein 4;
DE AltName: Full=SH2 domain-containing phosphatase anchor protein 1;
DE AltName: CD_antigen=CD307b;
DE Flags: Precursor;
GN Name=FCRL2; Synonyms=FCRH2, IFGP4, IRTA4, SPAP1; ORFNames=UNQ9236/PRO31998;
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), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Lymph node;
RX PubMed=11493702; DOI=10.1073/pnas.171308498;
RA Davis R.S., Wang Y.-H., Kubagawa H., Cooper M.D.;
RT "Identification of a family of Fc receptor homologs with preferential B
RT cell expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9772-9777(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), INTERACTION WITH PTPN6,
RP TISSUE SPECIFICITY, PHOSPHORYLATION, AND GLYCOSYLATION.
RX PubMed=11162587; DOI=10.1006/bbrc.2000.4213;
RA Xu M.-J., Zhao R., Zhao Z.J.;
RT "Molecular cloning and characterization of SPAP1, an inhibitory receptor.";
RL Biochem. Biophys. Res. Commun. 280:768-775(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11929751; DOI=10.1182/blood.v99.8.2662;
RA Miller I., Hatzivassiliou G., Cattoretti G., Mendelsohn C.,
RA Dalla-Favera R.;
RT "IRTAs: a new family of immunoglobulin-like receptors differentially
RT expressed in B cells.";
RL Blood 99:2662-2669(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Tonsil;
RX PubMed=12037601; DOI=10.1007/s00251-002-0436-x;
RA Guselnikov S.V., Ershova S.A., Mechetina L.V., Najakshin A.M.,
RA Volkova O.Y., Alabyev B.Y., Taranin A.V.;
RT "A family of highly diverse human and mouse genes structurally links
RT leukocyte FcR, gp42 and PECAM-1.";
RL Immunogenetics 54:87-95(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA Nickerson D.A.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
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 [10]
RP PROTEIN SEQUENCE OF 20-34.
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 [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16849395; DOI=10.1093/intimm/dxl069;
RA Polson A.G., Zheng B., Elkins K., Chang W., Du C., Dowd P., Yen L., Tan C.,
RA Hongo J.-A., Koeppen H., Ebens A.;
RT "Expression pattern of the human FcRH/IRTA receptors in normal tissue and
RT in B-chronic lymphocytic leukemia.";
RL Int. Immunol. 18:1363-1373(2006).
CC -!- FUNCTION: May have an regulatory role in normal and neoplastic B cell
CC development. {ECO:0000269|PubMed:11493702}.
CC -!- SUBUNIT: The tyrosine-phosphorylated isoform 2 interacts with PTPN6.
CC {ECO:0000269|PubMed:11162587}.
CC -!- INTERACTION:
CC Q96LA5; O43639: NCK2; NbExp=3; IntAct=EBI-10185081, EBI-713635;
CC Q96LA5-2; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-17263163, EBI-10266796;
CC Q96LA5-2; P21145: MAL; NbExp=3; IntAct=EBI-17263163, EBI-3932027;
CC Q96LA5-2; P60201-2: PLP1; NbExp=3; IntAct=EBI-17263163, EBI-12188331;
CC Q96LA5-2; Q8N966: ZDHHC22; NbExp=3; IntAct=EBI-17263163, EBI-10268111;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16849395};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:16849395}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96LA5-1; Sequence=Displayed;
CC Name=2; Synonyms=SPAP1A;
CC IsoId=Q96LA5-2; Sequence=VSP_014111, VSP_014112;
CC Name=3; Synonyms=SPAP1B;
CC IsoId=Q96LA5-3; Sequence=VSP_014111, VSP_014112, VSP_014116,
CC VSP_014117;
CC Name=4; Synonyms=SPAP1C;
CC IsoId=Q96LA5-4; Sequence=VSP_014111, VSP_014112, VSP_014114,
CC VSP_014115;
CC Name=5;
CC IsoId=Q96LA5-5; Sequence=VSP_014113, VSP_014118;
CC -!- TISSUE SPECIFICITY: Expressed in the secondary lymphoid organs, spleen
CC and lymph node. Expression is limited to the mature B-cell lines.
CC Highly expressed in CD19 and within the mantle zones of the tonsil
CC tissue. Isoform 2 is expressed in the spleen, peripheral blood and bone
CC marrow. Isoform 2 and isoform 4 are expressed in B-cell lines.
CC Preferentially expressed in memory B-cells (at protein level).
CC {ECO:0000269|PubMed:11162587, ECO:0000269|PubMed:11493702,
CC ECO:0000269|PubMed:11929751, ECO:0000269|PubMed:16849395}.
CC -!- DOMAIN: Contains 2 copies of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). The
CC phosphorylated ITIM motif bind the SH2 domain of PTPN6.
CC -!- PTM: Isoform 2 is N- and O-glycosylated, and phosphorylated.
CC {ECO:0000269|PubMed:11162587}.
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DR EMBL; AY043465; AAK91778.1; -; mRNA.
DR EMBL; AF319438; AAK01402.1; -; mRNA.
DR EMBL; AF319439; AAK01403.1; -; mRNA.
DR EMBL; AF319440; AAK01404.1; -; mRNA.
DR EMBL; AF459633; AAL60249.1; -; mRNA.
DR EMBL; AF390037; AAM12152.1; -; mRNA.
DR EMBL; EF064733; ABK41916.1; -; Genomic_DNA.
DR EMBL; AY358130; AAQ88497.1; -; mRNA.
DR EMBL; AL356276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52864.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52867.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52869.1; -; Genomic_DNA.
DR EMBL; BC069185; AAH69185.1; -; mRNA.
DR EMBL; BC129836; AAI29837.1; -; mRNA.
DR CCDS; CCDS1168.1; -. [Q96LA5-1]
DR PIR; JC7593; JC7593.
DR RefSeq; NP_001152960.1; NM_001159488.1.
DR RefSeq; NP_110391.2; NM_030764.3. [Q96LA5-1]
DR AlphaFoldDB; Q96LA5; -.
DR SMR; Q96LA5; -.
DR BioGRID; 122656; 11.
DR IntAct; Q96LA5; 6.
DR STRING; 9606.ENSP00000355157; -.
DR GlyGen; Q96LA5; 5 sites.
DR iPTMnet; Q96LA5; -.
DR PhosphoSitePlus; Q96LA5; -.
DR BioMuta; FCRL2; -.
DR DMDM; 68052374; -.
DR MassIVE; Q96LA5; -.
DR PaxDb; Q96LA5; -.
DR PeptideAtlas; Q96LA5; -.
DR PRIDE; Q96LA5; -.
DR ProteomicsDB; 77172; -. [Q96LA5-1]
DR ProteomicsDB; 77173; -. [Q96LA5-2]
DR ProteomicsDB; 77174; -. [Q96LA5-3]
DR ProteomicsDB; 77175; -. [Q96LA5-4]
DR ProteomicsDB; 77176; -. [Q96LA5-5]
DR TopDownProteomics; Q96LA5-1; -. [Q96LA5-1]
DR Antibodypedia; 34233; 126 antibodies from 21 providers.
DR DNASU; 79368; -.
DR Ensembl; ENST00000361516.8; ENSP00000355157.3; ENSG00000132704.16. [Q96LA5-1]
DR Ensembl; ENST00000368181.4; ENSP00000357163.4; ENSG00000132704.16. [Q96LA5-5]
DR Ensembl; ENST00000469986.1; ENSP00000417393.1; ENSG00000132704.16. [Q96LA5-3]
DR GeneID; 79368; -.
DR KEGG; hsa:79368; -.
DR MANE-Select; ENST00000361516.8; ENSP00000355157.3; NM_030764.4; NP_110391.2.
DR UCSC; uc001fre.3; human. [Q96LA5-1]
DR CTD; 79368; -.
DR DisGeNET; 79368; -.
DR GeneCards; FCRL2; -.
DR HGNC; HGNC:14875; FCRL2.
DR HPA; ENSG00000132704; Group enriched (intestine, lymphoid tissue).
DR MIM; 606509; gene.
DR neXtProt; NX_Q96LA5; -.
DR OpenTargets; ENSG00000132704; -.
DR PharmGKB; PA37913; -.
DR VEuPathDB; HostDB:ENSG00000132704; -.
DR eggNOG; ENOG502S65W; Eukaryota.
DR GeneTree; ENSGT01050000244808; -.
DR HOGENOM; CLU_023383_6_2_1; -.
DR InParanoid; Q96LA5; -.
DR OMA; ICPLACG; -.
DR OrthoDB; 53940at2759; -.
DR PhylomeDB; Q96LA5; -.
DR TreeFam; TF351107; -.
DR PathwayCommons; Q96LA5; -.
DR SignaLink; Q96LA5; -.
DR BioGRID-ORCS; 79368; 6 hits in 1072 CRISPR screens.
DR GeneWiki; FCRL2; -.
DR GenomeRNAi; 79368; -.
DR Pharos; Q96LA5; Tbio.
DR PRO; PR:Q96LA5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q96LA5; protein.
DR Bgee; ENSG00000132704; Expressed in buccal mucosa cell and 87 other tissues.
DR Genevisible; Q96LA5; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; NAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 4.
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 Pfam; PF13895; Ig_2; 3.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 20..508
FT /note="Fc receptor-like protein 2"
FT /id="PRO_0000014761"
FT TOPO_DOM 20..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..98
FT /note="Ig-like C2-type 1"
FT DOMAIN 109..187
FT /note="Ig-like C2-type 2"
FT DOMAIN 201..290
FT /note="Ig-like C2-type 3"
FT DOMAIN 300..387
FT /note="Ig-like C2-type 4"
FT REGION 429..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 446..451
FT /note="ITIM motif 1"
FT MOTIF 460..465
FT /note="ITIM motif 2"
FT MOTIF 472..477
FT /note="ITIM motif 3"
FT MOTIF 500..505
FT /note="ITIM motif 4"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 128..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 226..275
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 321..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..253
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11162587,
FT ECO:0000303|PubMed:12037601, ECO:0000303|PubMed:15489334"
FT /id="VSP_014111"
FT VAR_SEQ 104..387
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014113"
FT VAR_SEQ 254..295
FT /note="RSLSAELEIPAVKESDAGKYYCRADNGHVPIQSKVVNIPVRI -> MWEWKI
FT CNSHGARPFAEPAGWEFVNLLRHHKSFLIAPLCLSV (in isoform 2, isoform
FT 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11162587,
FT ECO:0000303|PubMed:12037601, ECO:0000303|PubMed:15489334"
FT /id="VSP_014112"
FT VAR_SEQ 389..397
FT /note="PDGYRRDLM -> GWVLPGYRV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11162587"
FT /id="VSP_014114"
FT VAR_SEQ 398..508
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11162587"
FT /id="VSP_014115"
FT VAR_SEQ 428..445
FT /note="ESSATNEPRGASRPNPQE -> CIYHLDSPYFAMTFPLLI (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:11162587"
FT /id="VSP_014116"
FT VAR_SEQ 446..508
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11162587"
FT /id="VSP_014117"
FT VAR_SEQ 465..486
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014118"
FT VARIANT 202
FT /note="I -> N (in dbSNP:rs16839100)"
FT /id="VAR_049873"
SQ SEQUENCE 508 AA; 55542 MW; 9AB30E0411B41EDC CRC64;
MLLWSLLVIF DAVTEQADSL TLVAPSSVFE GDSIVLKCQG EQNWKIQKMA YHKDNKELSV
FKKFSDFLIQ SAVLSDSGNY FCSTKGQLFL WDKTSNIVKI KVQELFQRPV LTASSFQPIE
GGPVSLKCET RLSPQRLDVQ LQFCFFRENQ VLGSGWSSSP ELQISAVWSE DTGSYWCKAE
TVTHRIRKQS LQSQIHVQRI PISNVSLEIR APGGQVTEGQ KLILLCSVAG GTGNVTFSWY
REATGTSMGK KTQRSLSAEL EIPAVKESDA GKYYCRADNG HVPIQSKVVN IPVRIPVSRP
VLTLRSPGAQ AAVGDLLELH CEALRGSPPI LYQFYHEDVT LGNSSAPSGG GASFNLSLTA
EHSGNYSCEA NNGLGAQCSE AVPVSISGPD GYRRDLMTAG VLWGLFGVLG FTGVALLLYA
LFHKISGESS ATNEPRGASR PNPQEFTYSS PTPDMEELQP VYVNVGSVDV DVVYSQVWSM
QQPESSANIR TLLENKDSQV IYSSVKKS
