Full text data of OLFM4
OLFM4
(GW112)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Olfactomedin-4; OLM4 (Antiapoptotic protein GW112; G-CSF-stimulated clone 1 protein; hGC-1; hOLfD; Flags: Precursor)
Olfactomedin-4; OLM4 (Antiapoptotic protein GW112; G-CSF-stimulated clone 1 protein; hGC-1; hOLfD; Flags: Precursor)
UniProt
Q6UX06
ID OLFM4_HUMAN Reviewed; 510 AA.
AC Q6UX06; O95362; Q5VWG0; Q86T22;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 12-APR-2005, sequence version 1.
DT 22-JAN-2014, entry version 86.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA 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.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA 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.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Zhuang Z., Rodgers G.P.;
RT "Identification and characterization of a novel member of
RT olfactomedin-related protein family, hGC-1, expressed during myeloid
RT lineage 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
RT pancreatic 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
CC leukemic cell lines, inhibits cell growth and induces cell
CC differentiation and apoptosis. May play a role in the inhibition
CC of EIF4EBP1 phosphorylation/deactivation. Facilitates cell
CC adhesion, most probably through interaction with cell surface
CC lectins and cadherin.
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
CC cadherin.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC Mitochondrion. Note=Subcellular location is not clearly defined:
CC has been shown to be secreted (PubMed:16566923), but also in the
CC mitochondrion (PubMed:15059901 and PubMed:20724538), cytoplasm and
CC plasma membrane (PubMed:20724538) and in the nucleus
CC (PubMed:15059901).
CC -!- TISSUE SPECIFICITY: Expressed during myeloid lineage development.
CC Much higher expression in bone marrow neutrophils than in
CC peripheral blood neutrophils (at protein level). Strongly
CC expressed in the prostate, small intestine and colon and
CC moderately expressed in the bone marrow and stomach. Overexpressed
CC in some pancreatic cancer tissues.
CC -!- DEVELOPMENTAL STAGE: Elevated expression during the early S phase
CC of the cell cycle, followed by a gradual decrease during late S
CC phase.
CC -!- INDUCTION: By retinoic acid. This induction requires functional
CC NFKB pathway.
CC -!- DOMAIN: The olfactomedin-like domain is involved in the
CC interaction with cadherin.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Contains 1 olfactomedin-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72970.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAC72970.1; Type=Frameshift; Positions=Several;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/OLFM4ID49730ch13q14.html";
CC -----------------------------------------------------------------------
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DR EMBL; AY358567; AAQ88930.1; -; mRNA.
DR EMBL; AL390736; CAH71311.2; -; 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 RefSeq; NP_006409.3; NM_006418.4.
DR UniGene; Hs.508113; -.
DR ProteinModelPortal; Q6UX06; -.
DR SMR; Q6UX06; 156-203.
DR DIP; DIP-59533N; -.
DR IntAct; Q6UX06; 1.
DR STRING; 9606.ENSP00000219022; -.
DR PhosphoSite; Q6UX06; -.
DR DMDM; 74749412; -.
DR PaxDb; Q6UX06; -.
DR PRIDE; Q6UX06; -.
DR DNASU; 10562; -.
DR Ensembl; ENST00000219022; ENSP00000219022; ENSG00000102837.
DR GeneID; 10562; -.
DR KEGG; hsa:10562; -.
DR UCSC; uc001vhl.3; human.
DR CTD; 10562; -.
DR GeneCards; GC13P053602; -.
DR HGNC; HGNC:17190; OLFM4.
DR MIM; 614061; gene.
DR neXtProt; NX_Q6UX06; -.
DR PharmGKB; PA134984745; -.
DR eggNOG; NOG297900; -.
DR HOGENOM; HOG000115264; -.
DR HOVERGEN; HBG106662; -.
DR InParanoid; Q6UX06; -.
DR OMA; GTCQCSV; -.
DR OrthoDB; EOG7QVM2N; -.
DR PhylomeDB; Q6UX06; -.
DR ChiTaRS; OLFM4; human.
DR GenomeRNAi; 10562; -.
DR NextBio; 40085; -.
DR PRO; PR:Q6UX06; -.
DR Bgee; Q6UX06; -.
DR CleanEx; HS_OLFM4; -.
DR Genevestigator; Q6UX06; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR InterPro; IPR003112; Olfac-like.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
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; Complete proteome; Disulfide bond;
KW Glycoprotein; Mitochondrion; Polymorphism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 20 Potential.
FT CHAIN 21 510 Olfactomedin-4.
FT /FTId=PRO_0000311398.
FT DOMAIN 245 507 Olfactomedin-like.
FT COILED 155 234 Potential.
FT COMPBIAS 31 71 Ser-rich.
FT CARBOHYD 72 72 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 136 136 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 253 253 N-linked (GlcNAc...) (Potential).
FT DISULFID 246 437 By similarity.
FT VARIANT 36 36 S -> P (in dbSNP:rs35790097).
FT /FTId=VAR_037246.
FT MUTAGEN 83 83 C->A: Abolishes secretion. No effect on
FT multimer formation.
FT MUTAGEN 85 85 C->A: Abolishes secretion. No effect on
FT multimer formation.
FT MUTAGEN 226 226 C->A: No effect on secretion. Affects
FT multimer formation.
FT MUTAGEN 246 246 C->A: Abolishes secretion. No effect on
FT multimer formation.
FT MUTAGEN 437 437 C->A: Abolishes secretion. No effect on
FT multimer formation.
FT CONFLICT 129 129 V -> L (in Ref. 5; AAC72970).
FT CONFLICT 304 304 R -> I (in Ref. 5; AAC72970).
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
//
ID OLFM4_HUMAN Reviewed; 510 AA.
AC Q6UX06; O95362; Q5VWG0; Q86T22;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 12-APR-2005, sequence version 1.
DT 22-JAN-2014, entry version 86.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics 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.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA 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.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA 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.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Zhuang Z., Rodgers G.P.;
RT "Identification and characterization of a novel member of
RT olfactomedin-related protein family, hGC-1, expressed during myeloid
RT lineage 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
RT pancreatic 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
CC leukemic cell lines, inhibits cell growth and induces cell
CC differentiation and apoptosis. May play a role in the inhibition
CC of EIF4EBP1 phosphorylation/deactivation. Facilitates cell
CC adhesion, most probably through interaction with cell surface
CC lectins and cadherin.
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
CC cadherin.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC Mitochondrion. Note=Subcellular location is not clearly defined:
CC has been shown to be secreted (PubMed:16566923), but also in the
CC mitochondrion (PubMed:15059901 and PubMed:20724538), cytoplasm and
CC plasma membrane (PubMed:20724538) and in the nucleus
CC (PubMed:15059901).
CC -!- TISSUE SPECIFICITY: Expressed during myeloid lineage development.
CC Much higher expression in bone marrow neutrophils than in
CC peripheral blood neutrophils (at protein level). Strongly
CC expressed in the prostate, small intestine and colon and
CC moderately expressed in the bone marrow and stomach. Overexpressed
CC in some pancreatic cancer tissues.
CC -!- DEVELOPMENTAL STAGE: Elevated expression during the early S phase
CC of the cell cycle, followed by a gradual decrease during late S
CC phase.
CC -!- INDUCTION: By retinoic acid. This induction requires functional
CC NFKB pathway.
CC -!- DOMAIN: The olfactomedin-like domain is involved in the
CC interaction with cadherin.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Contains 1 olfactomedin-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72970.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAC72970.1; Type=Frameshift; Positions=Several;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/OLFM4ID49730ch13q14.html";
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DR EMBL; AY358567; AAQ88930.1; -; mRNA.
DR EMBL; AL390736; CAH71311.2; -; 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 RefSeq; NP_006409.3; NM_006418.4.
DR UniGene; Hs.508113; -.
DR ProteinModelPortal; Q6UX06; -.
DR SMR; Q6UX06; 156-203.
DR DIP; DIP-59533N; -.
DR IntAct; Q6UX06; 1.
DR STRING; 9606.ENSP00000219022; -.
DR PhosphoSite; Q6UX06; -.
DR DMDM; 74749412; -.
DR PaxDb; Q6UX06; -.
DR PRIDE; Q6UX06; -.
DR DNASU; 10562; -.
DR Ensembl; ENST00000219022; ENSP00000219022; ENSG00000102837.
DR GeneID; 10562; -.
DR KEGG; hsa:10562; -.
DR UCSC; uc001vhl.3; human.
DR CTD; 10562; -.
DR GeneCards; GC13P053602; -.
DR HGNC; HGNC:17190; OLFM4.
DR MIM; 614061; gene.
DR neXtProt; NX_Q6UX06; -.
DR PharmGKB; PA134984745; -.
DR eggNOG; NOG297900; -.
DR HOGENOM; HOG000115264; -.
DR HOVERGEN; HBG106662; -.
DR InParanoid; Q6UX06; -.
DR OMA; GTCQCSV; -.
DR OrthoDB; EOG7QVM2N; -.
DR PhylomeDB; Q6UX06; -.
DR ChiTaRS; OLFM4; human.
DR GenomeRNAi; 10562; -.
DR NextBio; 40085; -.
DR PRO; PR:Q6UX06; -.
DR Bgee; Q6UX06; -.
DR CleanEx; HS_OLFM4; -.
DR Genevestigator; Q6UX06; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:GOC.
DR InterPro; IPR003112; Olfac-like.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
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; Complete proteome; Disulfide bond;
KW Glycoprotein; Mitochondrion; Polymorphism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1 20 Potential.
FT CHAIN 21 510 Olfactomedin-4.
FT /FTId=PRO_0000311398.
FT DOMAIN 245 507 Olfactomedin-like.
FT COILED 155 234 Potential.
FT COMPBIAS 31 71 Ser-rich.
FT CARBOHYD 72 72 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 136 136 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 253 253 N-linked (GlcNAc...) (Potential).
FT DISULFID 246 437 By similarity.
FT VARIANT 36 36 S -> P (in dbSNP:rs35790097).
FT /FTId=VAR_037246.
FT MUTAGEN 83 83 C->A: Abolishes secretion. No effect on
FT multimer formation.
FT MUTAGEN 85 85 C->A: Abolishes secretion. No effect on
FT multimer formation.
FT MUTAGEN 226 226 C->A: No effect on secretion. Affects
FT multimer formation.
FT MUTAGEN 246 246 C->A: Abolishes secretion. No effect on
FT multimer formation.
FT MUTAGEN 437 437 C->A: Abolishes secretion. No effect on
FT multimer formation.
FT CONFLICT 129 129 V -> L (in Ref. 5; AAC72970).
FT CONFLICT 304 304 R -> I (in Ref. 5; AAC72970).
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
//
MIM
614061
*RECORD*
*FIELD* NO
614061
*FIELD* TI
*614061 OLFACTOMEDIN 4; OLFM4
;;GCSF-STIMULATED CLONE 1; GC1;;
GW112
*FIELD* TX
CLONING
read more
Using cDNA representation difference analysis to identify genes
upregulated in inflamed colonic mucosa, Shinozaki et al. (2001)
identified OLFM4, which they designated GW112. In situ hybridization of
colonic biopsy specimens detected GW112 in crypt epithelial cells in
active ulcerative colitis, but not in normal colonic mucosa.
By differential display to identify genes upregulated in human
peripheral blood mononuclear cells by GCSF (CSF3; 138970), followed by
5-prime and 3-prime RACE of a bone marrow cDNA library and EST database
analysis, Zhang et al. (2002) cloned OLFM4, which they called GC1. The
deduced 510-amino acid protein has an N-terminal signal sequence, a
C-terminal olfactomedin (OLFM1; 605366)-like domain, and 6 evenly
distributed potential N-glycosylation sites. The predicted mature
protein contains 490 amino acids. GC1 shares high amino acid sequence
similarity and predicted secondary structure with olfactomedin. Northern
blot analysis detected a 2.8-kb GC1 transcript in small intestine,
colon, prostate, bone marrow, and stomach, but not in other tissues
examined. GC1 was expressed in myeloid lineage cell lines, but not in
erythroid or megakaryocytic lineage cell lines. GC1 expressed in
transfected 293 cells had an apparent molecular mass of about 64 kD,
which was reduced to 54 kD following N-glycanase treatment.
GENE FUNCTION
By RT-PCR, Zhang et al. (2002) found that GC1 was expressed in human
peripheral blood mononuclear cells induced to differentiate along the
granulocyte lineage by retinoic acid (RA). The multipotent
prepromyelocytic cell line HL-60 also expressed GC1 upon RA-induced
granulocytic differentiation.
RA inhibits cell growth and induces differentiation in hematopoietic
progenitor cells. Liu et al. (2010) identified a role for OLFM4 in
RA-induced cellular effects. They found that the dimeric RA receptor
made up of RARA (180240) and RXRA (180245) bound to an RA response
element in the OLFM4 promoter and mediated RA-induced transactivation of
the OLFM4 gene. OLFM4 overexpression in HL-60 cells inhibited cell
growth, induced cell differentiation and apoptosis, and potentiated RA
induction of these effects. Conversely, downregulation of endogenous
OLFM4 in acute myeloid leukemia-193 cells compromised RA-induced growth
inhibition, differentiation, and apoptosis. Overexpression of OLFM4 in
HL-60 cells inhibited constitutive and RA-induced phosphorylation of the
eukaryote initiation factor 4EBP1 (EIF4EBP1; 602223), whereas
downregulation of OLFM4 protein increased 4EBP1 phosphorylation. Liu et
al. (2010) concluded that OLFM4 has a role in RA-regulated cell growth,
differentiation, and apoptosis.
GENE STRUCTURE
Zhang et al. (2002) determined that the OLFM4 gene contains 5 coding
exons and spans over 23 kb.
MAPPING
By FISH and radiation hybrid analysis, Zhang et al. (2002) mapped the
OLFM4 gene to chromosome 13q14.3.
ANIMAL MODEL
Liu et al. (2010) found that Olfm4 -/- mice were fertile, viable, and
developmentally normal. Helicobacter pylori colonization of gastric
mucosa was significantly lower in Olfm4 -/- mice compared with wildtype
littermates. Reduced bacterial load was associated with enhanced
infiltration of inflammatory cells into the gastric mucosa. Production
and expression of proinflammatory cytokines and chemokines, such as Il1b
(147720), Il5 (147850), Il12 p70 (see IL12A; 161560), and Mip1a (CCL3;
182283), was increased in Olfm4 -/- mice. H. pylori induced Nfkb (see
164011) activation and Olfm4 expression in a dose-dependent manner in a
mouse gastric epithelial cell line. Dominant-negative mutants of Ikba
(NFKB1A; 164008) or kinase-deficient Ikk1 (CHUK; 600664), Ikk2 (IKBKB;
603258), or Nik (MAP3K14; 604655) blocked H. pylori induction of Olfm4
activity. Olfm4 had a negative feedback effect on Nfkb activation
through direct association with Nod1 (605980) and Nod2 (605956). Liu et
al. (2010) concluded that OLFM4 is involved in host defense against H.
pylori infection acting through NOD1- and NOD2-mediated NFKB activation
and subsequent cytokine and chemokine production, which in turn inhibit
host immune responses and contribute to the persistence of H. pylori
colonization.
*FIELD* RF
1. Liu, W.; Lee, H. W.; Liu, Y.; Wang, R.; Rodgers, G. P.: Olfactomedin
4 is a novel target gene of retinoic acids and 5-aza-2-prime-deoxycytidine
involved in human myeloid leukemia cell growth, differentiation, and
apoptosis. Blood 116: 4938-4947, 2010.
2. Liu, W.; Yan, M.; Liu, Y.; Wang, R.; Li, C.; Deng, C.; Singh, A.;
Coleman, W. G., Jr.; Rodgers, G. P.: Olfactomedin 4 down-regulates
innate immunity against Helicobacter pylori infection. Proc. Nat.
Acad. Sci. 107: 11056-11061, 2010.
3. Shinozaki, S.; Nakamura, T.; Iimura, M.; Kato, Y.; Iizuka, B.;
Kobayashi, M.; Hayashi, N.: Upregulation of Reg 1-alpha and GW112
in the epithelium of inflamed colonic mucosa. Gut 48: 623-239, 2001.
4. Zhang, J.; Liu, W.-L.; Tang, D. C.; Chen, L.; Wang, M.; Pack, S.
D.; Zhuang, Z.; Rodgers, G. P.: Identification and characterization
of a novel member of olfactomedin-related protein family, hGC-1, expressed
during myeloid lineage development. Gene 283: 83-93, 2002.
*FIELD* CN
Paul J. Converse - updated: 4/12/2012
*FIELD* CD
Patricia A. Hartz: 6/23/2011
*FIELD* ED
mgross: 05/03/2012
terry: 4/12/2012
mgross: 6/23/2011
*RECORD*
*FIELD* NO
614061
*FIELD* TI
*614061 OLFACTOMEDIN 4; OLFM4
;;GCSF-STIMULATED CLONE 1; GC1;;
GW112
*FIELD* TX
CLONING
read more
Using cDNA representation difference analysis to identify genes
upregulated in inflamed colonic mucosa, Shinozaki et al. (2001)
identified OLFM4, which they designated GW112. In situ hybridization of
colonic biopsy specimens detected GW112 in crypt epithelial cells in
active ulcerative colitis, but not in normal colonic mucosa.
By differential display to identify genes upregulated in human
peripheral blood mononuclear cells by GCSF (CSF3; 138970), followed by
5-prime and 3-prime RACE of a bone marrow cDNA library and EST database
analysis, Zhang et al. (2002) cloned OLFM4, which they called GC1. The
deduced 510-amino acid protein has an N-terminal signal sequence, a
C-terminal olfactomedin (OLFM1; 605366)-like domain, and 6 evenly
distributed potential N-glycosylation sites. The predicted mature
protein contains 490 amino acids. GC1 shares high amino acid sequence
similarity and predicted secondary structure with olfactomedin. Northern
blot analysis detected a 2.8-kb GC1 transcript in small intestine,
colon, prostate, bone marrow, and stomach, but not in other tissues
examined. GC1 was expressed in myeloid lineage cell lines, but not in
erythroid or megakaryocytic lineage cell lines. GC1 expressed in
transfected 293 cells had an apparent molecular mass of about 64 kD,
which was reduced to 54 kD following N-glycanase treatment.
GENE FUNCTION
By RT-PCR, Zhang et al. (2002) found that GC1 was expressed in human
peripheral blood mononuclear cells induced to differentiate along the
granulocyte lineage by retinoic acid (RA). The multipotent
prepromyelocytic cell line HL-60 also expressed GC1 upon RA-induced
granulocytic differentiation.
RA inhibits cell growth and induces differentiation in hematopoietic
progenitor cells. Liu et al. (2010) identified a role for OLFM4 in
RA-induced cellular effects. They found that the dimeric RA receptor
made up of RARA (180240) and RXRA (180245) bound to an RA response
element in the OLFM4 promoter and mediated RA-induced transactivation of
the OLFM4 gene. OLFM4 overexpression in HL-60 cells inhibited cell
growth, induced cell differentiation and apoptosis, and potentiated RA
induction of these effects. Conversely, downregulation of endogenous
OLFM4 in acute myeloid leukemia-193 cells compromised RA-induced growth
inhibition, differentiation, and apoptosis. Overexpression of OLFM4 in
HL-60 cells inhibited constitutive and RA-induced phosphorylation of the
eukaryote initiation factor 4EBP1 (EIF4EBP1; 602223), whereas
downregulation of OLFM4 protein increased 4EBP1 phosphorylation. Liu et
al. (2010) concluded that OLFM4 has a role in RA-regulated cell growth,
differentiation, and apoptosis.
GENE STRUCTURE
Zhang et al. (2002) determined that the OLFM4 gene contains 5 coding
exons and spans over 23 kb.
MAPPING
By FISH and radiation hybrid analysis, Zhang et al. (2002) mapped the
OLFM4 gene to chromosome 13q14.3.
ANIMAL MODEL
Liu et al. (2010) found that Olfm4 -/- mice were fertile, viable, and
developmentally normal. Helicobacter pylori colonization of gastric
mucosa was significantly lower in Olfm4 -/- mice compared with wildtype
littermates. Reduced bacterial load was associated with enhanced
infiltration of inflammatory cells into the gastric mucosa. Production
and expression of proinflammatory cytokines and chemokines, such as Il1b
(147720), Il5 (147850), Il12 p70 (see IL12A; 161560), and Mip1a (CCL3;
182283), was increased in Olfm4 -/- mice. H. pylori induced Nfkb (see
164011) activation and Olfm4 expression in a dose-dependent manner in a
mouse gastric epithelial cell line. Dominant-negative mutants of Ikba
(NFKB1A; 164008) or kinase-deficient Ikk1 (CHUK; 600664), Ikk2 (IKBKB;
603258), or Nik (MAP3K14; 604655) blocked H. pylori induction of Olfm4
activity. Olfm4 had a negative feedback effect on Nfkb activation
through direct association with Nod1 (605980) and Nod2 (605956). Liu et
al. (2010) concluded that OLFM4 is involved in host defense against H.
pylori infection acting through NOD1- and NOD2-mediated NFKB activation
and subsequent cytokine and chemokine production, which in turn inhibit
host immune responses and contribute to the persistence of H. pylori
colonization.
*FIELD* RF
1. Liu, W.; Lee, H. W.; Liu, Y.; Wang, R.; Rodgers, G. P.: Olfactomedin
4 is a novel target gene of retinoic acids and 5-aza-2-prime-deoxycytidine
involved in human myeloid leukemia cell growth, differentiation, and
apoptosis. Blood 116: 4938-4947, 2010.
2. Liu, W.; Yan, M.; Liu, Y.; Wang, R.; Li, C.; Deng, C.; Singh, A.;
Coleman, W. G., Jr.; Rodgers, G. P.: Olfactomedin 4 down-regulates
innate immunity against Helicobacter pylori infection. Proc. Nat.
Acad. Sci. 107: 11056-11061, 2010.
3. Shinozaki, S.; Nakamura, T.; Iimura, M.; Kato, Y.; Iizuka, B.;
Kobayashi, M.; Hayashi, N.: Upregulation of Reg 1-alpha and GW112
in the epithelium of inflamed colonic mucosa. Gut 48: 623-239, 2001.
4. Zhang, J.; Liu, W.-L.; Tang, D. C.; Chen, L.; Wang, M.; Pack, S.
D.; Zhuang, Z.; Rodgers, G. P.: Identification and characterization
of a novel member of olfactomedin-related protein family, hGC-1, expressed
during myeloid lineage development. Gene 283: 83-93, 2002.
*FIELD* CN
Paul J. Converse - updated: 4/12/2012
*FIELD* CD
Patricia A. Hartz: 6/23/2011
*FIELD* ED
mgross: 05/03/2012
terry: 4/12/2012
mgross: 6/23/2011