ID   OLFL3_RAT               Reviewed;         406 AA.
AC   B0BNI5;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Olfactomedin-like protein 3;
DE   Flags: Precursor;
GN   Name=Olfml3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the OLFML3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI58839.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC158838; AAI58839.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; B0BNI5; -.
DR   SMR; B0BNI5; -.
DR   STRING; 10116.ENSRNOP00000026075; -.
DR   GlyGen; B0BNI5; 1 site.
DR   PaxDb; B0BNI5; -.
DR   PeptideAtlas; B0BNI5; -.
DR   PRIDE; B0BNI5; -.
DR   UCSC; RGD:1311106; rat.
DR   RGD; 1311106; Olfml3.
DR   eggNOG; KOG3545; Eukaryota.
DR   InParanoid; B0BNI5; -.
DR   PhylomeDB; B0BNI5; -.
DR   PRO; PR:B0BNI5; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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   Coiled coil; Developmental protein; Disulfide bond; Glycoprotein;
KW   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_0000361561"
FT   DOMAIN          134..401
FT                   /note="Olfactomedin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT   COILED          22..101
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"
SQ   SEQUENCE   406 AA;  45961 MW;  23D29D4AC3731769 CRC64;
     MGPSAPLLLF FLLSWPGSLQ GQQHHLVEYM ERRLAALEER LAQCQDQSSR HAAELRDFKN
     KMLPLLEVAE KERETLRTEA DSISGRVDRL EREVDYLETQ NPALPCVELD EKVTGGPGTK
     GKGRRNEKYD MVTDCSYTIS QVRSMKILKR FGGSAGLWTK DPLGPAEKIY VLDGTQNDTA
     FVFPRLRDFT LTMAARKASR IRVPFPWVGT GQLVYGGFLY YARRPPGGAG GGGELENTLQ
     LIKFHLANRT VVDSSVFPAE RLIPPYGLTV DTYIDLAADE EGLWAVYATR EDDRHLCLAK
     LDPQTLDTEQ QWDTPCPREN AEAAFVICGT LYVVYNTRPA SRARIQCSFD ASGTLTPERA
     ALSYFPRRYG AHASLRYNPR ERQLYAWDDG YQIVYKLEMK KKEEEV