KALM_CHICK
ID KALM_CHICK Reviewed; 675 AA.
AC P33005; Q9PSH7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8513320; DOI=10.1038/ng0593-19;
RA Rugarli E.I., Lutz B., Kuratani S.C., Wawersik S., Borsani G., Ballabio A.,
RA Eichele G.;
RT "Expression pattern of the Kallmann syndrome gene in the olfactory system
RT suggests a role in neuronal targeting.";
RL Nat. Genet. 4:19-26(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-236, AND TISSUE SPECIFICITY.
RX PubMed=8460158; DOI=10.1073/pnas.90.6.2461;
RA Legouis R., Lievre C.A., Leibovici M., Lapointe F., Petit C.;
RT "Expression of the KAL gene in multiple neuronal sites during chicken
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2461-2465(1993).
CC -!- FUNCTION: May be an adhesion-like molecule with anti-protease activity.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in neurons of the central nervous
CC system during the second half of embryonic life. Expressed in mitral
CC neurons of the olfactory bulbs, striatal neurons, Purkinje cells of the
CC cerebellum, retinal neurons and neurons of the brainstem and spinal
CC cord. {ECO:0000269|PubMed:8460158}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L12144; AAA51435.1; -; mRNA.
DR EMBL; L10920; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B47222; B47222.
DR RefSeq; NP_990755.1; NM_205424.1.
DR AlphaFoldDB; P33005; -.
DR STRING; 9031.ENSGALP00000026766; -.
DR PaxDb; P33005; -.
DR GeneID; 396395; -.
DR KEGG; gga:396395; -.
DR CTD; 3730; -.
DR VEuPathDB; HostDB:geneid_396395; -.
DR eggNOG; KOG4802; Eukaryota.
DR InParanoid; P33005; -.
DR OrthoDB; 979841at2759; -.
DR PhylomeDB; P33005; -.
DR PRO; PR:P33005; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
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 GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
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..675
FT /note="Anosmin-1"
FT /id="PRO_0000041396"
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 654..675
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 43..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
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"
FT CONFLICT 3
FT /note="R -> SE (in Ref. 1; AAA51435)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="S -> P (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="H -> Y (in Ref. 1; AAA51435)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 76289 MW; 784393E4D603E2EA CRC64;
MVRRAPGASL ALLLWVTAVS GSPAGPGAAT ARRQDEAFST ARCTSRCLSL QITRISAFFK
HFQNNGSLAW CQNHKQCSKC LEPCKESWDL KKNHCQSFCE PLFPKKNYEC LTSCEFLKYI
LSVKQGDCPA PEKASGFAAA CVESCEADSE CSGVKKCCSN GCGHTCQVPK NLYKGVPLKP
RKELKFIELQ SGDLEVKWSS KFNISIEPVI YVVQRRWNQG IHPSEDDATN WQTVAQTTDE
RVQLSDIRAS RWYQFRVAAV NVHGTRGFTA PSKHFRSSKD PSAPPAPSNI RIANISANND
GTVNVMITWD LPEEPDIPVH HYKVFWSWTY SKYVIPAKKK RRKITDGPQN YVVLEGLQPN
SNYNVELQAV TRWGQIRLKS AKVSLHFSTA QDNRNNNEQT SAGKPPKGLV DPYPTFQRRK
PTRFLKIGTP FYQDNQLQVK VYWKKTDINM NQFQVHSLLE SCVHNDTKGL EKVTELTYEN
YMILKDLSFS CKYKVTVLPA KSKSRFKAES IFFVTPSCSA FKEKTHKHIN CAAEEVPVLP
KVLAKPENLS ASFIVQEGNI TGHFSWKISK AVLHQPMTGF QVTWAEVTTE SRQNSLPNSI
ISQSQILPAD HYVLTVPNLR PSMLYRLEVQ VLTTGGEGPA TIKLFRTPDL PPFLPHRPHL
KQHHPHHYKP PPEKY
