TRIC_TRIVU
ID TRIC_TRIVU Reviewed; 180 AA.
AC Q29147;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Trichosurin;
DE Flags: Precursor;
OS Trichosurus vulpecula (Brush-tailed possum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Diprotodontia; Phalangeridae; Trichosurus.
OX NCBI_TaxID=9337;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=9493361; DOI=10.1007/pl00006313;
RA Piotte C.P., Hunter A.K., Marshall C.J., Grigor M.R.;
RT "Phylogenetic analysis of three lipocalin-like proteins present in the milk
RT of Trichosurus vulpecula (Phalangeridae, Marsupialia).";
RL J. Mol. Evol. 46:361-369(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 16-180, SUBUNIT, AND DISULFIDE
RP BOND.
RX PubMed=17685895; DOI=10.1042/bj20070567;
RA Watson R.P., Demmer J., Baker E.N., Arcus V.L.;
RT "Three-dimensional structure and ligand binding properties of trichosurin,
RT a metatherian lipocalin from the milk whey of the common brushtail possum
RT Trichosurus vulpecula.";
RL Biochem. J. 408:29-38(2007).
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17685895}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Milk.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; U40376; AAA84739.1; -; mRNA.
DR PDB; 2R73; X-ray; 2.50 A; A/B/C/D=16-180.
DR PDB; 2R74; X-ray; 1.90 A; A/B=16-180.
DR PDB; 2RA6; X-ray; 1.50 A; A/B/C/D=16-180.
DR PDBsum; 2R73; -.
DR PDBsum; 2R74; -.
DR PDBsum; 2RA6; -.
DR AlphaFoldDB; Q29147; -.
DR SMR; Q29147; -.
DR EvolutionaryTrace; Q29147; -.
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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Milk protein; Secreted; Signal;
KW Transport.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..180
FT /note="Trichosurin"
FT /id="PRO_0000017989"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 87..180
FT /evidence="ECO:0000269|PubMed:17685895"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:2R73"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:2RA6"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2RA6"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:2RA6"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:2RA6"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:2RA6"
FT STRAND 102..116
FT /evidence="ECO:0007829|PDB:2RA6"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:2RA6"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:2RA6"
FT STRAND 135..147
FT /evidence="ECO:0007829|PDB:2RA6"
FT HELIX 151..162
FT /evidence="ECO:0007829|PDB:2RA6"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:2RA6"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:2RA6"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2RA6"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:2RA6"
SQ SEQUENCE 180 AA; 21025 MW; 012E1B0F2B39B0E1 CRC64;
MKLLLLSMGL ALVCGLQPEC SRSEEDLSDE KERKWEQLSR HWHTVVLASS DRSLIEEEGP
FRNFIQNITV ESGNLNGFFL TRKNGQCIPL YLTAFKTEEA RQFKLNYYGT NDVYYGSSKP
NEYAKFIFYN YHDGKVNVVA NLFGRTPNLS NEIKKRFEED FMNRGFRREN ILDISEVDHC