SAL_PIG
ID SAL_PIG Reviewed; 191 AA.
AC P81608; Q9N0K0;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Salivary lipocalin;
DE Short=SAL;
DE Flags: Precursor;
GN Name=SAL1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS, DISULFIDE BOND, AND GLYCOSYLATION AT
RP ASN-69.
RC TISSUE=Submandibular gland;
RX PubMed=10947950; DOI=10.1042/bj3500369;
RA Loebel D., Scaloni A., Paolini S., Fini C., Ferrara L., Breer H.,
RA Pelosi P.;
RT "Cloning, post-translational modifications, heterologous expression and
RT ligand-binding of boar salivary lipocalin.";
RL Biochem. J. 350:369-379(2000).
RN [2]
RP PROTEIN SEQUENCE OF 17-45.
RC TISSUE=Submandibular gland;
RX PubMed=9546674; DOI=10.1046/j.1432-1327.1998.2520563.x;
RA Marchese S., Pes D., Scaloni A., Carbone V., Pelosi P.;
RT "Lipocalins of boar salivary glands binding odours and pheromones.";
RL Eur. J. Biochem. 252:563-568(1998).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS) OF 17-191, GLYCOSYLATION AT ASN-69,
RP AND DISULFIDE BONDS.
RX PubMed=12027882; DOI=10.1046/j.1432-1033.2002.02901.x;
RA Spinelli S., Vincent F., Pelosi P., Tegoni M., Cambillau C.;
RT "Boar salivary lipocalin. Three-dimensional X-ray structure and
RT androsterol/androstenone docking simulations.";
RL Eur. J. Biochem. 269:2449-2456(2002).
CC -!- FUNCTION: Binds pheromones, the pheromones are released from the saliva
CC of males and affect the sexual behavior of females.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: In the submaxillary salivary glands of mature male
CC pigs, but absent from that of females. Expression was much lower in
CC submaxillary glands of castrated male pigs than in sexually mature
CC individuals.
CC -!- POLYMORPHISM: Two isoforms have been identified which differ by 3
CC residues.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; AJ249974; CAB93679.1; -; mRNA.
DR RefSeq; NP_998979.1; NM_213814.1.
DR PDB; 1GM6; X-ray; 2.13 A; A=17-191.
DR PDBsum; 1GM6; -.
DR AlphaFoldDB; P81608; -.
DR SMR; P81608; -.
DR STRING; 9823.ENSSSCP00000005870; -.
DR iPTMnet; P81608; -.
DR PaxDb; P81608; -.
DR Ensembl; ENSSSCT00005004156; ENSSSCP00005002461; ENSSSCG00005002720.
DR Ensembl; ENSSSCT00025084270; ENSSSCP00025036665; ENSSSCG00025061424.
DR GeneID; 396739; -.
DR KEGG; ssc:396739; -.
DR CTD; 396739; -.
DR eggNOG; ENOG502SWRK; Eukaryota.
DR InParanoid; P81608; -.
DR OrthoDB; 1475169at2759; -.
DR EvolutionaryTrace; P81608; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002971; Maj_urinary.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01221; MAJORURINARY.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:9546674"
FT CHAIN 17..191
FT /note="Salivary lipocalin"
FT /id="PRO_0000017973"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10947950,
FT ECO:0000269|PubMed:12027882"
FT DISULFID 84..176
FT /evidence="ECO:0000269|PubMed:10947950,
FT ECO:0000269|PubMed:12027882"
FT VARIANT 61
FT /note="V -> A (in isoform B)"
FT VARIANT 64
FT /note="I -> V (in isoform B)"
FT VARIANT 89
FT /note="A -> V (in isoform B)"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1GM6"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1GM6"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1GM6"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:1GM6"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:1GM6"
FT STRAND 83..95
FT /evidence="ECO:0007829|PDB:1GM6"
FT STRAND 98..115
FT /evidence="ECO:0007829|PDB:1GM6"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1GM6"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:1GM6"
FT STRAND 131..143
FT /evidence="ECO:0007829|PDB:1GM6"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:1GM6"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1GM6"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1GM6"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:1GM6"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:1GM6"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1GM6"
SQ SEQUENCE 191 AA; 21588 MW; 46324DD74749C25C CRC64;
MKLLLLLCLG LTLASSHKEA GQDVVTSNFD ASKIAGEWYS ILLASDAKEN IEENGSMRVF
VEHIRVLDNS SLAFKFQRKV NGECTDFYAV CDKVGDGVYT VAYYGENKFR LLEVNYSDYV
ILHLVNVNGD KTFQLMEFYG RKPDVEPKLK DKFVEICQQY GIIKENIIDL TKIDRCFQLR
GSGGVQESSA E
