OLFM4_MOUSE
ID OLFM4_MOUSE Reviewed; 505 AA.
AC Q3UZZ4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Olfactomedin-4;
DE Short=OLM4;
DE Flags: Precursor;
GN Name=Olfm4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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 (By
CC similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC Mitochondrion {ECO:0000250}.
CC -!- DOMAIN: The olfactomedin-like domain is involved in the interaction
CC with cadherin. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
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DR EMBL; AK133536; BAE21711.1; -; mRNA.
DR CCDS; CCDS36989.2; -.
DR AlphaFoldDB; Q3UZZ4; -.
DR SMR; Q3UZZ4; -.
DR DIP; DIP-59534N; -.
DR IntAct; Q3UZZ4; 3.
DR STRING; 10090.ENSMUSP00000086112; -.
DR GlyGen; Q3UZZ4; 2 sites.
DR PhosphoSitePlus; Q3UZZ4; -.
DR MaxQB; Q3UZZ4; -.
DR PRIDE; Q3UZZ4; -.
DR ProteomicsDB; 293845; -.
DR Antibodypedia; 24251; 273 antibodies from 32 providers.
DR Ensembl; ENSMUST00000228749; ENSMUSP00000154285; ENSMUSG00000022026.
DR UCSC; uc007utn.1; mouse.
DR MGI; MGI:2685142; Olfm4.
DR VEuPathDB; HostDB:ENSMUSG00000022026; -.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000155454; -.
DR InParanoid; Q3UZZ4; -.
DR OMA; VRIEIME; -.
DR PhylomeDB; Q3UZZ4; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR ChiTaRS; Olfm4; mouse.
DR PRO; PR:Q3UZZ4; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q3UZZ4; protein.
DR Bgee; ENSMUSG00000022026; Expressed in paneth cell and 73 other tissues.
DR ExpressionAtlas; Q3UZZ4; baseline and differential.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042581; C:specific granule; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0005198; F:structural molecule activity; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IMP:MGI.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0050777; P:negative regulation of immune response; IMP:MGI.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR003112; Olfac-like_dom.
DR InterPro; IPR031221; Olfactomedin-4.
DR PANTHER; PTHR23192:SF7; PTHR23192:SF7; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR PROSITE; PS51132; OLF; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Coiled coil; Disulfide bond; Glycoprotein; Mitochondrion;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..505
FT /note="Olfactomedin-4"
FT /id="PRO_0000311399"
FT DOMAIN 237..499
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT COILED 174..225
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 238..429
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 505 AA; 57299 MW; AAA111DBD26DAE10 CRC64;
MSYSLLFLLA LQFCLGSASR TTLTSAHSRE LTTPPTSPQA TAAWLPPGGT SWAEGGTVSQ
PLSNFTGSVD SHGTCQCSVS LPDTAFPADR VERLEYTAHI LSQKFEREFS KVKEYVQLIS
VYEKRLLNLT VRVEVMEKDS ISYTELDFEL IKLEVKEMQK LVLQLKKNFV GSTHIIDMLE
VEIRNMTLLV EKLESLDQNN VLSIRRQILA LKTKLKECEA SKSDLVPATP PPPAPGSCSH
GGVVNISAPS VIQLNWLGFS YKYGAWGRDY SPQHPERTLY WVAPLNTDAR ALEYYRLYDS
LDNLLIYSHF RDYRIRYGQG GGTVAFNNNL YVNWYNGGNI AKINLTTNVV DVNRPLPLAA
YNNRFSYANV NWQDIDLAVD EQALWAIYAT EASTGNIVIS KLNDTTLEVI STWVTKQYKP
SVSNAFMVCG VLYATRTLNT KTEEIFYYYD TNTEREGNLG ITMRKMQERI QSINYHPFDQ
KLYVYNDGYL LNYDLVFLQT PRQPV
