OLFM4_HUMAN
ID OLFM4_HUMAN Reviewed; 510 AA.
AC Q6UX06; O95362; Q5VWG0; Q86T22;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Olfactomedin-4;
DE Short=OLM4;
DE AltName: Full=Antiapoptotic protein GW112;
DE AltName: Full=G-CSF-stimulated clone 1 protein;
DE Short=hGC-1;
DE AltName: Full=hOLfD;
DE Flags: Precursor;
GN Name=OLFM4; Synonyms=GW112; ORFNames=UNQ362/PRO698;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and PNS;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-510, TISSUE SPECIFICITY, AND PTM.
RX PubMed=11867215; DOI=10.1016/s0378-1119(01)00763-6;
RA Zhang J., Liu W.-L., Tang D.C., Chen L., Wang M., Pack S.D., Zhuang Z.,
RA Rodgers G.P.;
RT "Identification and characterization of a novel member of olfactomedin-
RT related protein family, hGC-1, expressed during myeloid lineage
RT development.";
RL Gene 283:83-93(2002).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NDUFA13.
RX PubMed=15059901; DOI=10.1158/0008-5472.can-03-3443;
RA Zhang X., Huang Q., Yang Z., Li Y., Li C.-Y.;
RT "GW112, a novel antiapoptotic protein that promotes tumor growth.";
RL Cancer Res. 64:2474-2481(2004).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DOMAIN, SUBUNIT,
RP INTERACTION WITH CELL SURFACE LECTINS AND CADHERIN, AND MUTAGENESIS OF
RP CYS-83; CYS-85; CYS-226; CYS-246 AND CYS-437.
RX PubMed=16566923; DOI=10.1016/j.yexcr.2006.02.011;
RA Liu W., Chen L., Zhu J., Rodgers G.P.;
RT "The glycoprotein hGC-1 binds to cadherin and lectins.";
RL Exp. Cell Res. 312:1785-1797(2006).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17270022; DOI=10.1111/j.1349-7006.2007.00397.x;
RA Kobayashi D., Koshida S., Moriai R., Tsuji N., Watanabe N.;
RT "Olfactomedin 4 promotes S-phase transition in proliferation of pancreatic
RT cancer cells.";
RL Cancer Sci. 98:334-340(2007).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20724538; DOI=10.1182/blood-2009-10-246439;
RA Liu W., Lee H.W., Liu Y., Wang R., Rodgers G.P.;
RT "Olfactomedin 4 is a novel target gene of retinoic acids and 5-aza-2'-
RT deoxycytidine involved in human myeloid leukemia cell growth,
RT differentiation, and apoptosis.";
RL Blood 116:4938-4947(2010).
CC -!- FUNCTION: May promote proliferation of pancreatic cancer cells by
CC favoring the transition from the S to G2/M phase. In myeloid leukemic
CC cell lines, inhibits cell growth and induces cell differentiation and
CC apoptosis. May play a role in the inhibition of EIF4EBP1
CC phosphorylation/deactivation. Facilitates cell adhesion, most probably
CC through interaction with cell surface lectins and cadherin.
CC {ECO:0000269|PubMed:16566923, ECO:0000269|PubMed:17270022,
CC ECO:0000269|PubMed:20724538}.
CC -!- SUBUNIT: Homomultimer; disulfide-linked. Interacts with NDUFA13.
CC Interacts with cell surface lectins (locutions ricinus communis
CC agglutinin I, concanavalin-A and wheat germ agglutinin) and cadherin.
CC {ECO:0000269|PubMed:15059901, ECO:0000269|PubMed:16566923}.
CC -!- INTERACTION:
CC Q6UX06; P41181: AQP2; NbExp=3; IntAct=EBI-2804156, EBI-12701138;
CC Q6UX06; Q92482: AQP3; NbExp=3; IntAct=EBI-2804156, EBI-2808854;
CC Q6UX06; J3KQ12: BSCL2; NbExp=3; IntAct=EBI-2804156, EBI-11532900;
CC Q6UX06; O95471: CLDN7; NbExp=3; IntAct=EBI-2804156, EBI-740744;
CC Q6UX06; Q6ZS10: CLEC17A; NbExp=3; IntAct=EBI-2804156, EBI-11977093;
CC Q6UX06; Q9BXN2-6: CLEC7A; NbExp=3; IntAct=EBI-2804156, EBI-11989440;
CC Q6UX06; Q9BQT9: CLSTN3; NbExp=3; IntAct=EBI-2804156, EBI-11291074;
CC Q6UX06; Q9HBJ8: CLTRN; NbExp=3; IntAct=EBI-2804156, EBI-3924906;
CC Q6UX06; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-2804156, EBI-6942903;
CC Q6UX06; O14944: EREG; NbExp=3; IntAct=EBI-2804156, EBI-17272224;
CC Q6UX06; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-2804156, EBI-18304435;
CC Q6UX06; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-2804156, EBI-12142257;
CC Q6UX06; Q14626: IL11RA; NbExp=3; IntAct=EBI-2804156, EBI-13638581;
CC Q6UX06; Q9NQX7-3: ITM2C; NbExp=3; IntAct=EBI-2804156, EBI-12811565;
CC Q6UX06; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-2804156, EBI-749265;
CC Q6UX06; P43628: KIR2DL3; NbExp=3; IntAct=EBI-2804156, EBI-8632435;
CC Q6UX06; Q8N743: KIR3DL3; NbExp=3; IntAct=EBI-2804156, EBI-17272405;
CC Q6UX06; Q5T700: LDLRAD1; NbExp=7; IntAct=EBI-2804156, EBI-10173166;
CC Q6UX06; A8MZ59: LEUTX; NbExp=3; IntAct=EBI-2804156, EBI-17490413;
CC Q6UX06; Q6ZUX7: LHFPL2; NbExp=3; IntAct=EBI-2804156, EBI-17566767;
CC Q6UX06; Q9Y239: NOD1; NbExp=2; IntAct=EBI-2804156, EBI-1051262;
CC Q6UX06; Q9HC29: NOD2; NbExp=2; IntAct=EBI-2804156, EBI-7445625;
CC Q6UX06; P15151: PVR; NbExp=3; IntAct=EBI-2804156, EBI-3919694;
CC Q6UX06; Q6DKI7: PVRIG; NbExp=3; IntAct=EBI-2804156, EBI-17964309;
CC Q6UX06; Q9NXS2-3: QPCTL; NbExp=3; IntAct=EBI-2804156, EBI-13336719;
CC Q6UX06; P54219-3: SLC18A1; NbExp=3; IntAct=EBI-2804156, EBI-17595455;
CC Q6UX06; A1A5C7-2: SLC22A23; NbExp=3; IntAct=EBI-2804156, EBI-12081840;
CC Q6UX06; Q96L08: SUSD3; NbExp=3; IntAct=EBI-2804156, EBI-18194029;
CC Q6UX06; Q8N205: SYNE4; NbExp=3; IntAct=EBI-2804156, EBI-7131783;
CC Q6UX06; Q9UP52: TFR2; NbExp=3; IntAct=EBI-2804156, EBI-3934135;
CC Q6UX06; Q8N3G9: TMEM130; NbExp=3; IntAct=EBI-2804156, EBI-19763514;
CC Q6UX06; O14788: TNFSF11; NbExp=3; IntAct=EBI-2804156, EBI-7404021;
CC Q6UX06; O43557: TNFSF14; NbExp=3; IntAct=EBI-2804156, EBI-524131;
CC Q6UX06; Q8WUV1: TSPAN18; NbExp=3; IntAct=EBI-2804156, EBI-17670824;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Mitochondrion.
CC Note=Subcellular location is not clearly defined: has been shown to be
CC secreted (PubMed:16566923), but also in the mitochondrion
CC (PubMed:15059901 and PubMed:20724538), cytoplasm and plasma membrane
CC (PubMed:20724538) and in the nucleus (PubMed:15059901).
CC {ECO:0000269|PubMed:15059901, ECO:0000269|PubMed:16566923,
CC ECO:0000269|PubMed:20724538}.
CC -!- TISSUE SPECIFICITY: Expressed during myeloid lineage development. Much
CC higher expression in bone marrow neutrophils than in peripheral blood
CC neutrophils (at protein level). Strongly expressed in the prostate,
CC small intestine and colon and moderately expressed in the bone marrow
CC and stomach. Overexpressed in some pancreatic cancer tissues.
CC {ECO:0000269|PubMed:11867215, ECO:0000269|PubMed:16566923,
CC ECO:0000269|PubMed:17270022, ECO:0000269|PubMed:20724538}.
CC -!- DEVELOPMENTAL STAGE: Elevated expression during the early S phase of
CC the cell cycle, followed by a gradual decrease during late S phase.
CC {ECO:0000269|PubMed:17270022}.
CC -!- INDUCTION: By retinoic acid. This induction requires functional NFKB
CC pathway. {ECO:0000269|PubMed:20724538}.
CC -!- DOMAIN: The olfactomedin-like domain is involved in the interaction
CC with cadherin. {ECO:0000269|PubMed:16566923}.
CC -!- PTM: N-glycosylated.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72970.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC72970.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/OLFM4ID49730ch13q14.html";
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DR EMBL; AY358567; AAQ88930.1; -; mRNA.
DR EMBL; AL390736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471124; EAW52052.1; -; Genomic_DNA.
DR EMBL; BC047740; AAH47740.1; -; mRNA.
DR EMBL; BC117329; AAI17330.1; -; mRNA.
DR EMBL; AF097021; AAC72970.1; ALT_SEQ; mRNA.
DR CCDS; CCDS9440.1; -.
DR RefSeq; NP_006409.3; NM_006418.4.
DR AlphaFoldDB; Q6UX06; -.
DR SMR; Q6UX06; -.
DR BioGRID; 115813; 76.
DR DIP; DIP-59533N; -.
DR IntAct; Q6UX06; 51.
DR STRING; 9606.ENSP00000219022; -.
DR GlyConnect; 1585; 12 N-Linked glycans (6 sites).
DR GlyGen; Q6UX06; 6 sites, 10 N-linked glycans (6 sites).
DR iPTMnet; Q6UX06; -.
DR PhosphoSitePlus; Q6UX06; -.
DR BioMuta; OLFM4; -.
DR DMDM; 74749412; -.
DR CPTAC; CPTAC-1528; -.
DR CPTAC; CPTAC-1529; -.
DR jPOST; Q6UX06; -.
DR MassIVE; Q6UX06; -.
DR PaxDb; Q6UX06; -.
DR PeptideAtlas; Q6UX06; -.
DR PRIDE; Q6UX06; -.
DR ProteomicsDB; 67547; -.
DR Antibodypedia; 24251; 273 antibodies from 32 providers.
DR DNASU; 10562; -.
DR Ensembl; ENST00000219022.3; ENSP00000219022.2; ENSG00000102837.7.
DR GeneID; 10562; -.
DR KEGG; hsa:10562; -.
DR MANE-Select; ENST00000219022.3; ENSP00000219022.2; NM_006418.5; NP_006409.3.
DR UCSC; uc001vhl.4; human.
DR CTD; 10562; -.
DR DisGeNET; 10562; -.
DR GeneCards; OLFM4; -.
DR HGNC; HGNC:17190; OLFM4.
DR HPA; ENSG00000102837; Tissue enhanced (intestine, pancreas).
DR MIM; 614061; gene.
DR neXtProt; NX_Q6UX06; -.
DR OpenTargets; ENSG00000102837; -.
DR PharmGKB; PA134984745; -.
DR VEuPathDB; HostDB:ENSG00000102837; -.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000155454; -.
DR HOGENOM; CLU_035236_5_0_1; -.
DR InParanoid; Q6UX06; -.
DR OMA; VRIEIME; -.
DR OrthoDB; 623462at2759; -.
DR PhylomeDB; Q6UX06; -.
DR TreeFam; TF315964; -.
DR PathwayCommons; Q6UX06; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q6UX06; -.
DR BioGRID-ORCS; 10562; 13 hits in 1068 CRISPR screens.
DR ChiTaRS; OLFM4; human.
DR GenomeRNAi; 10562; -.
DR Pharos; Q6UX06; Tbio.
DR PRO; PR:Q6UX06; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q6UX06; protein.
DR Bgee; ENSG00000102837; Expressed in urethra and 122 other tissues.
DR ExpressionAtlas; Q6UX06; baseline and differential.
DR Genevisible; Q6UX06; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IMP:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0045296; F:cadherin binding; IMP:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR003112; Olfac-like_dom.
DR InterPro; IPR031221; Olfactomedin-4.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR PANTHER; PTHR23192:SF7; PTHR23192:SF7; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR SUPFAM; SSF50952; SSF50952; 1.
DR PROSITE; PS51132; OLF; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Coiled coil; Disulfide bond; Glycoprotein; Mitochondrion;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..510
FT /note="Olfactomedin-4"
FT /id="PRO_0000311398"
FT DOMAIN 245..507
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT COILED 155..234
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 246..437
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT VARIANT 36
FT /note="S -> P (in dbSNP:rs35790097)"
FT /id="VAR_037246"
FT MUTAGEN 83
FT /note="C->A: Abolishes secretion. No effect on multimer
FT formation."
FT /evidence="ECO:0000269|PubMed:16566923"
FT MUTAGEN 85
FT /note="C->A: Abolishes secretion. No effect on multimer
FT formation."
FT /evidence="ECO:0000269|PubMed:16566923"
FT MUTAGEN 226
FT /note="C->A: No effect on secretion. Affects multimer
FT formation."
FT /evidence="ECO:0000269|PubMed:16566923"
FT MUTAGEN 246
FT /note="C->A: Abolishes secretion. No effect on multimer
FT formation."
FT /evidence="ECO:0000269|PubMed:16566923"
FT MUTAGEN 437
FT /note="C->A: Abolishes secretion. No effect on multimer
FT formation."
FT /evidence="ECO:0000269|PubMed:16566923"
FT CONFLICT 129
FT /note="V -> L (in Ref. 5; AAC72970)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="R -> I (in Ref. 5; AAC72970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 510 AA; 57280 MW; ACF03365D2164900 CRC64;
MRPGLSFLLA LLFFLGQAAG DLGDVGPPIP SPGFSSFPGV DSSSSFSSSS RSGSSSSRSL
GSGGSVSQLF SNFTGSVDDR GTCQCSVSLP DTTFPVDRVE RLEFTAHVLS QKFEKELSKV
REYVQLISVY EKKLLNLTVR IDIMEKDTIS YTELDFELIK VEVKEMEKLV IQLKESFGGS
SEIVDQLEVE IRNMTLLVEK LETLDKNNVL AIRREIVALK TKLKECEASK DQNTPVVHPP
PTPGSCGHGG VVNISKPSVV QLNWRGFSYL YGAWGRDYSP QHPNKGLYWV APLNTDGRLL
EYYRLYNTLD DLLLYINARE LRITYGQGSG TAVYNNNMYV NMYNTGNIAR VNLTTNTIAV
TQTLPNAAYN NRFSYANVAW QDIDFAVDEN GLWVIYSTEA STGNMVISKL NDTTLQVLNT
WYTKQYKPSA SNAFMVCGVL YATRTMNTRT EEIFYYYDTN TGKEGKLDIV MHKMQEKVQS
INYNPFDQKL YVYNDGYLLN YDLSVLQKPQ
