OLFL3_HUMAN
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 03-AUG-2022, entry version 158.
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}.
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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; 12.
DR IntAct; Q9NRN5; 7.
DR MINT; Q9NRN5; -.
DR STRING; 9606.ENSP00000322273; -.
DR GlyConnect; 1587; 52 N-Linked glycans (2 sites).
DR GlyGen; Q9NRN5; 2 sites, 55 N-linked glycans (2 sites).
DR iPTMnet; Q9NRN5; -.
DR PhosphoSitePlus; Q9NRN5; -.
DR BioMuta; OLFML3; -.
DR DMDM; 37999795; -.
DR EPD; Q9NRN5; -.
DR jPOST; Q9NRN5; -.
DR MassIVE; Q9NRN5; -.
DR PaxDb; Q9NRN5; -.
DR PeptideAtlas; Q9NRN5; -.
DR PRIDE; 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; 74 antibodies from 20 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 CTD; 56944; -.
DR DisGeNET; 56944; -.
DR GeneCards; OLFML3; -.
DR HGNC; HGNC:24956; OLFML3.
DR HPA; ENSG00000116774; Low tissue specificity.
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; SQWHDQS; -.
DR PhylomeDB; Q9NRN5; -.
DR TreeFam; TF352000; -.
DR PathwayCommons; Q9NRN5; -.
DR SignaLink; Q9NRN5; -.
DR BioGRID-ORCS; 56944; 234 hits in 1062 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 101 other tissues.
DR ExpressionAtlas; Q9NRN5; baseline and differential.
DR Genevisible; Q9NRN5; HS.
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 InterPro; IPR031230; OLFML3.
DR PANTHER; PTHR23192:SF8; PTHR23192:SF8; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR PROSITE; PS51132; OLF; 1.
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
