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   02-SEP-2026, entry version 165.
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, 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="https://atlasgeneticsoncology.org/gene/49730/OLFM4";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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_006418.5.
DR   AlphaFoldDB; Q6UX06; -.
DR   SMR; Q6UX06; -.
DR   BioGRID; 115813; 79.
DR   DIP; DIP-59533N; -.
DR   FunCoup; Q6UX06; 10.
DR   IntAct; Q6UX06; 92.
DR   MINT; Q6UX06; -.
DR   STRING; 9606.ENSP00000219022; -.
DR   GlyConnect; Q6UX06; 12 N-Linked glycans (6 sites).
DR   GlyCosmos; Q6UX06; 6 sites, 11 glycans.
DR   GlyGen; Q6UX06; 8 sites, 56 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; 9606-ENSP00000219022; -.
DR   PeptideAtlas; Q6UX06; -.
DR   PRIDE; Q6UX06; -.
DR   ProteomicsDB; 67547; -.
DR   Pumba; Q6UX06; -.
DR   Antibodypedia; 24251; 256 antibodies from 35 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   AGR; HGNC:17190; -.
DR   ClinPGx; PA134984745; -.
DR   CTD; 10562; -.
DR   DisGeNET; 10562; -.
DR   GeneCards; OLFM4; -.
DR   HGNC; HGNC:17190; OLFM4.
DR   HPA; ENSG00000102837; Tissue enhanced (intestine, pancreas).
DR   MalaCards; OLFM4; -.
DR   MIM; 614061; gene.
DR   OpenTargets; ENSG00000102837; -.
DR   VEuPathDB; HostDB:ENSG00000102837; -.
DR   eggNOG; KOG3545; Eukaryota.
DR   GeneTree; ENSGT00940000155454; -.
DR   HOGENOM; CLU_035236_5_0_1; -.
DR   InParanoid; Q6UX06; -.
DR   OMA; LRITYGQ; -.
DR   OrthoDB; 8626508at2759; -.
DR   PAN-GO; Q6UX06; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q6UX06; -.
DR   PathwayCommons; Q6UX06; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; Q6UX06; -.
DR   Agora; ENSG00000102837; -.
DR   BioGRID-ORCS; 10562; 14 hits in 1146 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 123 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
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: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; IPR050605; Olfactomedin-like_domain.
DR   InterPro; IPR011041; Quinoprot_gluc/sorb_DH_b-prop.
DR   PANTHER; PTHR23192:SF7; OLFACTOMEDIN-4; 1.
DR   PANTHER; PTHR23192; OLFACTOMEDIN-RELATED; 1.
DR   Pfam; PF02191; OLF; 1.
DR   SMART; SM00284; OLF; 1.
DR   SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR   PROSITE; PS51132; OLF; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Coiled coil; Disulfide bond; Glycoprotein; Mitochondrion;
KW   Proteomics identification; 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
//