ID   KALM_COTJA              Reviewed;         674 AA.
AC   Q90369;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Anosmin-1 {ECO:0000250|UniProtKB:P23352};
DE   AltName: Full=Kallmann syndrome protein homolog {ECO:0000250|UniProtKB:P23352};
DE   Flags: Precursor;
GN   Name=ANOS1 {ECO:0000250|UniProtKB:P23352}; Synonyms=KAL, KAL1;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8406507; DOI=10.1006/geno.1993.1360;
RA   Legouis R., Cohen-Salmon M., del Castillo I., Levilliers J., Capy L.,
RA   Mornon J.-P., Petit C.;
RT   "Characterization of the chicken and quail homologues of the human gene
RT   responsible for the X-linked Kallmann syndrome.";
RL   Genomics 17:516-518(1993).
CC   -!- FUNCTION: May be an adhesion-like molecule with anti-protease activity.
CC   -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}.
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DR   EMBL; L13976; AAA88500.1; -; mRNA.
DR   RefSeq; NP_001310114.1; NM_001323185.1.
DR   AlphaFoldDB; Q90369; -.
DR   MEROPS; I17.004; -.
DR   GeneID; 107306124; -.
DR   KEGG; cjo:107306124; -.
DR   CTD; 3730; -.
DR   Proteomes; UP000694412; Unplaced.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00063; FN3; 3.
DR   Gene3D; 2.60.40.10; -; 3.
DR   Gene3D; 4.10.75.10; -; 1.
DR   InterPro; IPR042447; Anosmin-1.
DR   InterPro; IPR040957; Anosmin-1_Cys_box.
DR   InterPro; IPR036645; Elafin-like_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008197; WAP_dom.
DR   PANTHER; PTHR14131; PTHR14131; 1.
DR   Pfam; PF17869; Cys_box; 1.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF00095; WAP; 1.
DR   PRINTS; PR00003; 4DISULPHCORE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00217; WAP; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   SUPFAM; SSF57256; SSF57256; 1.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS51390; WAP; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Protease inhibitor;
KW   Reference proteome; Repeat; Serine protease inhibitor; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..674
FT                   /note="Anosmin-1"
FT                   /id="PRO_0000041397"
FT   DOMAIN          121..170
FT                   /note="WAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DOMAIN          180..281
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          286..392
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          418..515
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          545..652
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          388..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        465
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        548
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        559
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        47..71
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        80..99
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        84..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        110..114
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
SQ   SEQUENCE   674 AA;  76439 MW;  52ACDB45C75C0392 CRC64;
     MVRRAPGASL ALLLWVTAVS CSPAGPGAAT ARRQDEAFST ARLTSRCLSL QITRISAFFK
     HFQDNGSLAW CQNYKQCSKC LEPCKESWDL KRNHCQSFCE PLFPKKNYEC LTSCEFLKYI
     LSVKQGDCPA PEKASGFAAA CFESCEADSE CSGVKKCCSN GCGHTCQVPK NLYKGVPLKP
     RKELKFIELQ SGDLEVKWSS KFNISIEPVI YVVQRRWNQG IHPSEDDATN WQTVAQTTDE
     RVQLSDIRAS RWYQFRVAAV NVHGTRGFTA PSKHFRSSKD PSAPPAPSNI RIANISANND
     GTVNVMITWD LPEEPDIPVH HYKVFWSWTY SKYVIPAKKK RRKITDGPQN YVVLEGLQPN
     SNYNVELQAV TRWGQIRLKS AKVSLHFSTT QDNRNNNEQT SVEKPPKGVV DPYPTFQRRK
     PTRFLKIGTP FYQDNQLQVK IYWKKSGINM NQFQVHSLLE SCTHNDTKGL EKVTELTYEN
     YMILKDLSFS CKYKVTVLPA KSKSRFKAES IFFVTPPCST FKEKTHKHIN CAAEEVPVLP
     KVLAKPENLS ASFIVQEGNI TGHFSWKISK AVLHQPMTGF QVTWAEVTTE SRQNSLPNSI
     ISQSQILPAD HYVLTVPNLR PSMLYRLEVQ VLTTGGEGPA TIKLFRTPDL PPFLPHRPHL
     KHHPHRYKPP PEKY