ID   OLFL3_XENLA             Reviewed;         392 AA.
AC   B5MFE9; Q5U5B5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Olfactomedin-like protein 3;
DE   AltName: Full=Olfactomedin-noelin-tiarin factor 1;
DE   Flags: Precursor;
GN   Name=olfml3; Synonyms=ont1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CHRD AND BMP1.
RX   PubMed=18775317; DOI=10.1016/j.cell.2008.07.008;
RA   Inomata H., Haraguchi T., Sasai Y.;
RT   "Robust stability of the embryonic axial pattern requires a secreted
RT   scaffold for chordin degradation.";
RL   Cell 134:854-865(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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 protease BMP1
CC       and its substrate chordin (CHRD), leading to enhance chordin (CHRD)
CC       degradation by BMP1. {ECO:0000269|PubMed:18775317}.
CC   -!- SUBUNIT: Interacts (via coiled coil domain) with BMP1 and (via
CC       olfactomedin-like domain) CHRD. {ECO:0000269|PubMed:18775317}.
CC   -!- INTERACTION:
CC       B5MFE9; P98070: bmp1; NbExp=3; IntAct=EBI-1997734, EBI-1997775;
CC       B5MFE9; Q91713: chrd; NbExp=6; IntAct=EBI-1997734, EBI-1997746;
CC       B5MFE9; B5MFE9: olfml3; NbExp=2; IntAct=EBI-1997734, EBI-1997734;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the OLFML3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH84769.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB440138; BAG71407.1; -; mRNA.
DR   EMBL; BC084769; AAH84769.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001088445.1; NM_001094976.1.
DR   AlphaFoldDB; B5MFE9; -.
DR   SMR; B5MFE9; -.
DR   IntAct; B5MFE9; 4.
DR   GeneID; 495309; -.
DR   KEGG; xla:495309; -.
DR   CTD; 495309; -.
DR   Xenbase; XB-GENE-6022244; olfml3.L.
DR   OrthoDB; 421994at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 495309; Expressed in internal ear and 14 other tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   InterPro; IPR011043; Gal_Oxase/kelch_b-propeller.
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   SUPFAM; SSF50965; SSF50965; 1.
DR   PROSITE; PS51132; OLF; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Developmental protein; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..392
FT                   /note="Olfactomedin-like protein 3"
FT                   /id="PRO_0000361565"
FT   DOMAIN          131..387
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT   COILED          52..100
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        174
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        132..314
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT   CONFLICT        113
FT                   /note="S -> T (in Ref. 1; BAG71407)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   392 AA;  45110 MW;  14466FFBBD41A7A8 CRC64;
     MMAGIVACIL LVFVTVITAQ PQAVFLEYIQ GRMGVLEERI AQWHDQSSRF SGELRDFKNQ
     VLKMLENIEK ERDSLRNEME NTNVRVNRLE REVDYIETQN PAPPCVEIDE KLSDHHGAKK
     KKKEKYQKIT DCSDTISQVT AMKILKRFGS SAGLWTKDLA GNSDRIYVFD GAGNDTVYMY
     PRMKEFTLSS PTRKAAKIRL PFPWIGTGHI VYDGNLYYIR QDNEFQVIKF SLANKTIIDS
     AVLPIEQQVP VYGLSKFNYI DIVADEEGLW VIYATKENEK NICLAKLDPS SLSIEQMWDT
     PCPIENAESA FVVCGSLYVV YNTKLPSRSR IQCVFDVSGT ISSENVPIVY FPKRYGSHSS
     MKYNPREKQI YAWDDGYQII YKLNMKHRDE LY