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Protein

Olfactomedin-4

Gene

OLFM4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May promote proliferation of pancreatic cancer cells by favoring the transition from the S to G2/M phase. In myeloid leukemic cell lines, inhibits cell growth and induces cell differentiation and apoptosis. May play a role in the inhibition of EIF4EBP1 phosphorylation/deactivation. Facilitates cell adhesion, most probably through interaction with cell surface lectins and cadherin.3 Publications

GO - Molecular functioni

  • cadherin binding Source: UniProtKB
  • catalytic activity Source: InterPro
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • cell adhesion Source: UniProtKB-KW
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Olfactomedin-4
Short name:
OLM4
Alternative name(s):
Antiapoptotic protein GW112
G-CSF-stimulated clone 1 protein
Short name:
hGC-1
hOLfD
Gene namesi
Name:OLFM4
Synonyms:GW112
ORF Names:UNQ362/PRO698
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:17190. OLFM4.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • mitochondrion Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • specific granule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi83 – 831C → A: Abolishes secretion. No effect on multimer formation. 1 Publication
Mutagenesisi85 – 851C → A: Abolishes secretion. No effect on multimer formation. 1 Publication
Mutagenesisi226 – 2261C → A: No effect on secretion. Affects multimer formation. 1 Publication
Mutagenesisi246 – 2461C → A: Abolishes secretion. No effect on multimer formation. 1 Publication
Mutagenesisi437 – 4371C → A: Abolishes secretion. No effect on multimer formation. 1 Publication

Organism-specific databases

PharmGKBiPA134984745.

Polymorphism and mutation databases

BioMutaiOLFM4.
DMDMi74749412.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 510490Olfactomedin-4PRO_0000311398Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi72 – 721N-linked (GlcNAc...)Sequence analysis
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence analysis
Disulfide bondi246 ↔ 437PROSITE-ProRule annotation
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ6UX06.
PaxDbiQ6UX06.
PeptideAtlasiQ6UX06.
PRIDEiQ6UX06.

PTM databases

iPTMnetiQ6UX06.
PhosphoSiteiQ6UX06.

Expressioni

Tissue specificityi

Expressed during myeloid lineage development. Much higher expression in bone marrow neutrophils than in peripheral blood neutrophils (at protein level). Strongly expressed in the prostate, small intestine and colon and moderately expressed in the bone marrow and stomach. Overexpressed in some pancreatic cancer tissues.4 Publications

Developmental stagei

Elevated expression during the early S phase of the cell cycle, followed by a gradual decrease during late S phase.1 Publication

Inductioni

By retinoic acid. This induction requires functional NFKB pathway.1 Publication

Gene expression databases

BgeeiQ6UX06.
CleanExiHS_OLFM4.
ExpressionAtlasiQ6UX06. baseline and differential.
GenevisibleiQ6UX06. HS.

Interactioni

Subunit structurei

Homomultimer; disulfide-linked. Interacts with NDUFA13. Interacts with cell surface lectins (locutions ricinus communis agglutinin I, concanavalin-A and wheat germ agglutinin) and cadherin.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC155Q8N6L03EBI-2804156,EBI-749265
LDLRAD1Q5T7003EBI-2804156,EBI-10173166
SYNE4Q8N2053EBI-2804156,EBI-7131783

GO - Molecular functioni

  • cadherin binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115813. 35 interactions.
DIPiDIP-59533N.
IntActiQ6UX06. 4 interactions.
STRINGi9606.ENSP00000219022.

Structurei

3D structure databases

ProteinModelPortaliQ6UX06.
SMRiQ6UX06. Positions 158-187, 272-503.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini245 – 507263Olfactomedin-likePROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili155 – 23480Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi31 – 7141Ser-richAdd
BLAST

Domaini

The olfactomedin-like domain is involved in the interaction with cadherin.1 Publication

Sequence similaritiesi

Contains 1 olfactomedin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiENOG410INPB. Eukaryota.
ENOG410ZRPP. LUCA.
GeneTreeiENSGT00760000119005.
HOGENOMiHOG000115264.
HOVERGENiHBG106662.
InParanoidiQ6UX06.
OMAiGTCQCSV.
OrthoDBiEOG7QVM2N.
PhylomeDBiQ6UX06.
TreeFamiTF315964.

Family and domain databases

InterProiIPR003112. Olfac-like_dom.
IPR031221. Olfactomedin-4.
IPR011041. Quinoprot_gluc/sorb_DH.
[Graphical view]
PANTHERiPTHR23192:SF7. PTHR23192:SF7. 1 hit.
PfamiPF02191. OLF. 1 hit.
[Graphical view]
SMARTiSM00284. OLF. 1 hit.
[Graphical view]
SUPFAMiSSF50952. SSF50952. 1 hit.
PROSITEiPS51132. OLF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6UX06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPGLSFLLA LLFFLGQAAG DLGDVGPPIP SPGFSSFPGV DSSSSFSSSS
60 70 80 90 100
RSGSSSSRSL GSGGSVSQLF SNFTGSVDDR GTCQCSVSLP DTTFPVDRVE
110 120 130 140 150
RLEFTAHVLS QKFEKELSKV REYVQLISVY EKKLLNLTVR IDIMEKDTIS
160 170 180 190 200
YTELDFELIK VEVKEMEKLV IQLKESFGGS SEIVDQLEVE IRNMTLLVEK
210 220 230 240 250
LETLDKNNVL AIRREIVALK TKLKECEASK DQNTPVVHPP PTPGSCGHGG
260 270 280 290 300
VVNISKPSVV QLNWRGFSYL YGAWGRDYSP QHPNKGLYWV APLNTDGRLL
310 320 330 340 350
EYYRLYNTLD DLLLYINARE LRITYGQGSG TAVYNNNMYV NMYNTGNIAR
360 370 380 390 400
VNLTTNTIAV TQTLPNAAYN NRFSYANVAW QDIDFAVDEN GLWVIYSTEA
410 420 430 440 450
STGNMVISKL NDTTLQVLNT WYTKQYKPSA SNAFMVCGVL YATRTMNTRT
460 470 480 490 500
EEIFYYYDTN TGKEGKLDIV MHKMQEKVQS INYNPFDQKL YVYNDGYLLN
510
YDLSVLQKPQ
Length:510
Mass (Da):57,280
Last modified:April 12, 2005 - v1
Checksum:iACF03365D2164900
GO

Sequence cautioni

The sequence AAC72970.1 differs from that shown. Reason: Frameshift at several positions. Curated
The sequence AAC72970.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291V → L in AAC72970 (PubMed:11867215).Curated
Sequence conflicti304 – 3041R → I in AAC72970 (PubMed:11867215).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361S → P.
Corresponds to variant rs35790097 [ dbSNP | Ensembl ].
VAR_037246

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358567 mRNA. Translation: AAQ88930.1.
AL390736 Genomic DNA. Translation: CAH71311.2.
CH471124 Genomic DNA. Translation: EAW52052.1.
BC047740 mRNA. Translation: AAH47740.1.
BC117329 mRNA. Translation: AAI17330.1.
AF097021 mRNA. Translation: AAC72970.1. Sequence problems.
CCDSiCCDS9440.1.
RefSeqiNP_006409.3. NM_006418.4.
UniGeneiHs.508113.

Genome annotation databases

EnsembliENST00000219022; ENSP00000219022; ENSG00000102837.
GeneIDi10562.
KEGGihsa:10562.
UCSCiuc001vhl.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358567 mRNA. Translation: AAQ88930.1.
AL390736 Genomic DNA. Translation: CAH71311.2.
CH471124 Genomic DNA. Translation: EAW52052.1.
BC047740 mRNA. Translation: AAH47740.1.
BC117329 mRNA. Translation: AAI17330.1.
AF097021 mRNA. Translation: AAC72970.1. Sequence problems.
CCDSiCCDS9440.1.
RefSeqiNP_006409.3. NM_006418.4.
UniGeneiHs.508113.

3D structure databases

ProteinModelPortaliQ6UX06.
SMRiQ6UX06. Positions 158-187, 272-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115813. 35 interactions.
DIPiDIP-59533N.
IntActiQ6UX06. 4 interactions.
STRINGi9606.ENSP00000219022.

PTM databases

iPTMnetiQ6UX06.
PhosphoSiteiQ6UX06.

Polymorphism and mutation databases

BioMutaiOLFM4.
DMDMi74749412.

Proteomic databases

EPDiQ6UX06.
PaxDbiQ6UX06.
PeptideAtlasiQ6UX06.
PRIDEiQ6UX06.

Protocols and materials databases

DNASUi10562.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219022; ENSP00000219022; ENSG00000102837.
GeneIDi10562.
KEGGihsa:10562.
UCSCiuc001vhl.4. human.

Organism-specific databases

CTDi10562.
GeneCardsiOLFM4.
HGNCiHGNC:17190. OLFM4.
MIMi614061. gene.
neXtProtiNX_Q6UX06.
PharmGKBiPA134984745.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INPB. Eukaryota.
ENOG410ZRPP. LUCA.
GeneTreeiENSGT00760000119005.
HOGENOMiHOG000115264.
HOVERGENiHBG106662.
InParanoidiQ6UX06.
OMAiGTCQCSV.
OrthoDBiEOG7QVM2N.
PhylomeDBiQ6UX06.
TreeFamiTF315964.

Miscellaneous databases

ChiTaRSiOLFM4. human.
GenomeRNAii10562.
PROiQ6UX06.
SOURCEiSearch...

Gene expression databases

BgeeiQ6UX06.
CleanExiHS_OLFM4.
ExpressionAtlasiQ6UX06. baseline and differential.
GenevisibleiQ6UX06. HS.

Family and domain databases

InterProiIPR003112. Olfac-like_dom.
IPR031221. Olfactomedin-4.
IPR011041. Quinoprot_gluc/sorb_DH.
[Graphical view]
PANTHERiPTHR23192:SF7. PTHR23192:SF7. 1 hit.
PfamiPF02191. OLF. 1 hit.
[Graphical view]
SMARTiSM00284. OLF. 1 hit.
[Graphical view]
SUPFAMiSSF50952. SSF50952. 1 hit.
PROSITEiPS51132. OLF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon and PNS.
  5. "Identification and characterization of a novel member of olfactomedin-related protein family, hGC-1, expressed during myeloid lineage development."
    Zhang J., Liu W.-L., Tang D.C., Chen L., Wang M., Pack S.D., Zhuang Z., Rodgers G.P.
    Gene 283:83-93(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-510, TISSUE SPECIFICITY, PTM.
  6. "GW112, a novel antiapoptotic protein that promotes tumor growth."
    Zhang X., Huang Q., Yang Z., Li Y., Li C.-Y.
    Cancer Res. 64:2474-2481(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NDUFA13.
  7. "The glycoprotein hGC-1 binds to cadherin and lectins."
    Liu W., Chen L., Zhu J., Rodgers G.P.
    Exp. Cell Res. 312:1785-1797(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DOMAIN, SUBUNIT, INTERACTION WITH CELL SURFACE LECTINS AND CADHERIN, MUTAGENESIS OF CYS-83; CYS-85; CYS-226; CYS-246 AND CYS-437.
  8. "Olfactomedin 4 promotes S-phase transition in proliferation of pancreatic cancer cells."
    Kobayashi D., Koshida S., Moriai R., Tsuji N., Watanabe N.
    Cancer Sci. 98:334-340(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  9. "Olfactomedin 4 is a novel target gene of retinoic acids and 5-aza-2'-deoxycytidine involved in human myeloid leukemia cell growth, differentiation, and apoptosis."
    Liu W., Lee H.W., Liu Y., Wang R., Rodgers G.P.
    Blood 116:4938-4947(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.

Entry informationi

Entry nameiOLFM4_HUMAN
AccessioniPrimary (citable) accession number: Q6UX06
Secondary accession number(s): O95362, Q5VWG0, Q86T22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: April 12, 2005
Last modified: July 6, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.