ID OLFL3_HUMAN Reviewed; 406 AA. AC Q9NRN5; Q53FR1; Q53HV9; Q5SQL6; Q69AX9; Q8NBJ2; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 167. DE RecName: Full=Olfactomedin-like protein 3; DE AltName: Full=HNOEL-iso; DE AltName: Full=hOLF44; DE Flags: Precursor; GN Name=OLFML3; ORFNames=PSEC0035, PSEC0173, PSEC0244, UNQ663/PRO1294; 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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND FUNCTION. RX PubMed=15280020; DOI=10.1016/j.febslet.2004.06.059; RA Zeng L.-C., Liu F., Zhang X., Zhu Z.-D., Wang Z.-Q., Han Z.-G., Ma W.-J.; RT "hOLF44, a secreted glycoprotein with distinct expression pattern, belongs RT to an uncharacterized olfactomedin-like subfamily newly identified by RT phylogenetic analysis."; RL FEBS Lett. 571:74-80(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Dendritic cell; RA Huang C., Ren S., Tu Y., Gu W., Wang Y., Han Z., Chen Z.; RT "Novel genes expressed in human dendritic cells."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adipose tissue, and Gastric mucosa; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Teratocarcinoma; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; 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). CC -!- FUNCTION: Secreted scaffold protein that plays an essential role in CC dorsoventral patterning during early development. Stabilizes axial CC formation by restricting chordin (CHRD) activity on the dorsal side. CC Acts by facilitating the association between the tolloid proteases and CC their substrate chordin (CHRD), leading to enhance chordin (CHRD) CC degradation (By similarity). May have matrix-related function involved CC in placental and embryonic development, or play a similar role in other CC physiological processes. {ECO:0000250, ECO:0000269|PubMed:15280020}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15280020}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9NRN5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NRN5-2; Sequence=VSP_014128, VSP_014129; CC Name=3; CC IsoId=Q9NRN5-3; Sequence=VSP_014130, VSP_014131; CC -!- TISSUE SPECIFICITY: Abundant in placenta, moderate in liver and heart, CC whereas fairly weak in other tissues examined. On term placenta, mainly CC localized extracellularly surrounding the syncytiotrophoblastic cells CC and very rarely expressed in the maternal decidua layer. CC {ECO:0000269|PubMed:15280020}. CC -!- SIMILARITY: Belongs to the OLFML3 family. {ECO:0000305}. 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; AY464015; AAR88262.1; -; mRNA. DR EMBL; AF201945; AAF86881.1; -; mRNA. DR EMBL; AY358954; AAQ89313.1; -; mRNA. DR EMBL; AK075544; BAC11687.1; -; mRNA. DR EMBL; AK223221; BAD96941.1; -; mRNA. DR EMBL; AK222471; BAD96191.1; -; mRNA. DR EMBL; AK075353; BAC11564.1; -; mRNA. DR EMBL; AK075479; BAC11644.1; -; mRNA. DR EMBL; AL731797; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC009920; AAH09920.1; -; mRNA. DR CCDS; CCDS65618.1; -. [Q9NRN5-2] DR CCDS; CCDS870.1; -. [Q9NRN5-1] DR RefSeq; NP_001273281.1; NM_001286352.2. [Q9NRN5-2] DR RefSeq; NP_064575.1; NM_020190.4. [Q9NRN5-1] DR RefSeq; XP_016857337.1; XM_017001848.1. [Q9NRN5-2] DR AlphaFoldDB; Q9NRN5; -. DR SMR; Q9NRN5; -. DR BioGRID; 121268; 13. DR IntAct; Q9NRN5; 7. DR MINT; Q9NRN5; -. DR STRING; 9606.ENSP00000322273; -. DR GlyConnect; 1587; 52 N-Linked glycans (2 sites). DR GlyCosmos; Q9NRN5; 2 sites, 55 glycans. DR GlyGen; Q9NRN5; 3 sites, 55 N-linked glycans (2 sites), 1 O-linked glycan (1 site). DR iPTMnet; Q9NRN5; -. DR PhosphoSitePlus; Q9NRN5; -. DR BioMuta; OLFML3; -. DR DMDM; 37999795; -. DR EPD; Q9NRN5; -. DR jPOST; Q9NRN5; -. DR MassIVE; Q9NRN5; -. DR PaxDb; 9606-ENSP00000322273; -. DR PeptideAtlas; Q9NRN5; -. DR ProteomicsDB; 82393; -. [Q9NRN5-1] DR ProteomicsDB; 82394; -. [Q9NRN5-2] DR ProteomicsDB; 82395; -. [Q9NRN5-3] DR ABCD; Q9NRN5; 3 sequenced antibodies. DR Antibodypedia; 53757; 88 antibodies from 21 providers. DR DNASU; 56944; -. DR Ensembl; ENST00000320334.5; ENSP00000322273.4; ENSG00000116774.12. [Q9NRN5-1] DR Ensembl; ENST00000369551.5; ENSP00000358564.1; ENSG00000116774.12. [Q9NRN5-2] DR GeneID; 56944; -. DR KEGG; hsa:56944; -. DR MANE-Select; ENST00000320334.5; ENSP00000322273.4; NM_020190.5; NP_064575.1. DR UCSC; uc001eer.3; human. [Q9NRN5-1] DR AGR; HGNC:24956; -. DR CTD; 56944; -. DR DisGeNET; 56944; -. DR GeneCards; OLFML3; -. DR HGNC; HGNC:24956; OLFML3. DR HPA; ENSG00000116774; Tissue enhanced (ovary). DR MIM; 610088; gene. DR neXtProt; NX_Q9NRN5; -. DR OpenTargets; ENSG00000116774; -. DR PharmGKB; PA134913777; -. DR VEuPathDB; HostDB:ENSG00000116774; -. DR eggNOG; KOG3545; Eukaryota. DR GeneTree; ENSGT00940000158083; -. DR InParanoid; Q9NRN5; -. DR OMA; QQQFMEY; -. DR OrthoDB; 2876896at2759; -. DR PhylomeDB; Q9NRN5; -. DR TreeFam; TF352000; -. DR PathwayCommons; Q9NRN5; -. DR SignaLink; Q9NRN5; -. DR BioGRID-ORCS; 56944; 243 hits in 1142 CRISPR screens. DR ChiTaRS; OLFML3; human. DR GeneWiki; OLFML3; -. DR GenomeRNAi; 56944; -. DR Pharos; Q9NRN5; Tbio. DR PRO; PR:Q9NRN5; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9NRN5; Protein. DR Bgee; ENSG00000116774; Expressed in gall bladder and 102 other cell types or tissues. DR ExpressionAtlas; Q9NRN5; baseline and differential. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR InterPro; IPR003112; Olfac-like_dom. DR PANTHER; PTHR23192:SF8; OLFACTOMEDIN-LIKE PROTEIN 3; 1. DR PANTHER; PTHR23192; OLFACTOMEDIN-RELATED; 1. DR Pfam; PF02191; OLF; 1. DR SMART; SM00284; OLF; 1. DR PROSITE; PS51132; OLF; 1. DR Genevisible; Q9NRN5; HS. PE 2: Evidence at transcript level; KW Alternative splicing; Coiled coil; Developmental protein; Disulfide bond; KW Glycoprotein; Reference proteome; Secreted; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..406 FT /note="Olfactomedin-like protein 3" FT /id="PRO_0000020092" FT DOMAIN 134..401 FT /note="Olfactomedin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446" FT COILED 25..101 FT /evidence="ECO:0000255" FT CARBOHYD 177 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 248 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 135..328 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446" FT VAR_SEQ 1..20 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_014128" FT VAR_SEQ 21..38 FT /note="GQQHHLVEYMERRLAALE -> MAQWHCSQRTQAGGHGVG (in isoform FT 2)" FT /evidence="ECO:0000305" FT /id="VSP_014129" FT VAR_SEQ 134..287 FT /note="DCGYTISQVRSMKILKRFGGPAGLWTKDPLGQTEKIYVLDGTQNDTAFVFPR FT LRDFTLAMAARKASRVRVPFPWVGTGQLVYGGFLYFARRPPGRPGGGGEMENTLQLIKF FT HLANRTVVDSSVFPAEGLIPPYGLTADTYIDLAADEEGLWAVY -> GKQSESRPLTLL FT RTDILPSLLLTLFFTLSQSIVALSSGICFRETSVMPGLLRRGSGDPGRCGTRSFSILPK FT IGGNRWANAHYSPDHPPWGSSCWRHLILASISFSCAFLIRLWLHNLSSEINEDSEAIWW FT PSWSMDQGSTGANREDLRVRWDTE (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_014130" FT VAR_SEQ 288..406 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_014131" FT CONFLICT 118 FT /note="G -> E (in Ref. 5; BAD96191)" FT /evidence="ECO:0000305" FT CONFLICT 131 FT /note="M -> K (in Ref. 5; BAD96941)" FT /evidence="ECO:0000305" FT CONFLICT 182 FT /note="V -> F (in Ref. 5; BAD96191)" FT /evidence="ECO:0000305" FT CONFLICT 277 FT /note="A -> V (in Ref. 3; AAQ89313)" FT /evidence="ECO:0000305" SQ SEQUENCE 406 AA; 46010 MW; 0B5DB1A803BB99D6 CRC64; MGPSTPLLIL FLLSWSGPLQ GQQHHLVEYM ERRLAALEER LAQCQDQSSR HAAELRDFKN KMLPLLEVAE KEREALRTEA DTISGRVDRL EREVDYLETQ NPALPCVEFD EKVTGGPGTK GKGRRNEKYD MVTDCGYTIS QVRSMKILKR FGGPAGLWTK DPLGQTEKIY VLDGTQNDTA FVFPRLRDFT LAMAARKASR VRVPFPWVGT GQLVYGGFLY FARRPPGRPG GGGEMENTLQ LIKFHLANRT VVDSSVFPAE GLIPPYGLTA DTYIDLAADE EGLWAVYATR EDDRHLCLAK LDPQTLDTEQ QWDTPCPREN AEAAFVICGT LYVVYNTRPA SRARIQCSFD ASGTLTPERA ALPYFPRRYG AHASLRYNPR ERQLYAWDDG YQIVYKLEMR KKEEEV //