OLFM_LITCT
ID OLFM_LITCT Reviewed; 464 AA.
AC Q07081;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Olfactomedin;
DE AltName: Full=Olfactory mucus protein;
DE Flags: Precursor;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 17-33 AND 35-37.
RC TISSUE=Olfactory neuroepithelium;
RX PubMed=8506313; DOI=10.1073/pnas.90.10.4655;
RA Yokoe H., Anholt R.R.H.;
RT "Molecular cloning of olfactomedin, an extracellular matrix protein
RT specific to olfactory neuroepithelium.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4655-4659(1993).
RN [2]
RP PROTEIN SEQUENCE OF 17-37, AND GLYCOSYLATION.
RC TISSUE=Olfactory neuroepithelium;
RX PubMed=8424933; DOI=10.1021/bi00055a008;
RA Bal R.S., Anholt R.R.H.;
RT "Formation of the extracellular mucous matrix of olfactory neuroepithelium:
RT identification of partially glycosylated and nonglycosylated precursors of
RT olfactomedin.";
RL Biochemistry 32:1047-1053(1993).
CC -!- FUNCTION: May influence the maintenance, growth, or differentiation of
CC chemosensory cilia on the apical dendrites of olfactory neurons. Major
CC component of the extracellular matrix of the olfactory neuroepithelium.
CC -!- SUBUNIT: Oligomer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in olfactory neuroepithelium.
CC -!- PTM: Most, if not all, of the six potential sites for N-glycosylation
CC carry carbohydrate moieties of 8-10 sugar residues.
CC {ECO:0000269|PubMed:8424933}.
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DR EMBL; L13595; AAA49527.1; -; mRNA.
DR PIR; A47442; A47442.
DR AlphaFoldDB; Q07081; -.
DR SMR; Q07081; -.
DR iPTMnet; Q07081; -.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Olfaction;
KW Secreted; Sensory transduction; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:8424933,
FT ECO:0000269|PubMed:8506313"
FT CHAIN 17..464
FT /note="Olfactomedin"
FT /id="PRO_0000020089"
FT DOMAIN 192..464
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:8424933"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 193..394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
SQ SEQUENCE 464 AA; 52572 MW; CE5C617E40079864 CRC64;
MYICLLTLVL IHAAAAFVAQ NATGILAGKD HCVCEVLLPD SSFPAKRVGA LEDETIRLSN
RVEDEMQKLE EQDIILDTYS EKIINLTRRV EYLEKLHPES LVEISFEVLK REIRELEMYI
SAMRVKPNGN SVQVETLYNE VKNMSKTVGQ LETLDKNNVL QAKREIVNLK KRLVDCEKNL
KAKPSLMVPL GSCQHQGLAH ISKPNLMQLN WKGNAYKSGA WGKDAAWNTT KKSLYWVAPL
NTDGRVLESI RIYPSMSDLQ MYKNPIDLPL SMLIKNKLNN TFAGQGAGVV VHNNNLYYNC
FNSHDMCRAS LTSGVYQKKP LLNALFNNRF SYAGTMFQDM DFSSDEKGLW VIFTTEKSAG
KIVVGKVNVA TFTVDNIWIT TQNKSDASNA FMICGVLYVT RSLGPKMEEV FYMFDTKTGK
EGHLSIMMEK MAEKVHSLSY NSNDRKLYMF SEGYLLHYDI ALKP