ID L5L1J2_PTEAL Unreviewed; 189 AA.
AC L5L1J2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Apolipoprotein D {ECO:0000256|ARBA:ARBA00019890, ECO:0000256|PIRNR:PIRNR036893};
DE Short=Apo-D {ECO:0000256|PIRNR:PIRNR036893};
GN ORFNames=PAL_GLEAN10007388 {ECO:0000313|EMBL:ELK17614.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK17614.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR036893}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000256|ARBA:ARBA00006889, ECO:0000256|PIRNR:PIRNR036893}.
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DR EMBL; KB030403; ELK17614.1; -; Genomic_DNA.
DR RefSeq; XP_006906222.1; XM_006906160.2.
DR AlphaFoldDB; L5L1J2; -.
DR STRING; 9402.L5L1J2; -.
DR GeneID; 102887976; -.
DR KEGG; pale:102887976; -.
DR CTD; 347; -.
DR eggNOG; KOG4824; Eukaryota.
DR InParanoid; L5L1J2; -.
DR OrthoDB; 3783962at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR GO; GO:0042246; P:tissue regeneration; IEA:InterPro.
DR CDD; cd19437; lipocalin_apoD-like; 1.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR026222; ApoD_vertbrte.
DR InterPro; IPR002969; ApolipopD.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR022271; Lipocalin_ApoD.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR10612; APOLIPOPROTEIN D; 1.
DR PANTHER; PTHR10612:SF34; APOLIPOPROTEIN D; 1.
DR Pfam; PF08212; Lipocalin_2; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PRINTS; PR02058; APODVERTBRTE.
DR PRINTS; PR01219; APOLIPOPROTD.
DR PRINTS; PR00179; LIPOCALIN.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Lipoprotein {ECO:0000313|EMBL:ELK17614.1};
KW Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR036893};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT CHAIN 21..189
FT /note="Apolipoprotein D"
FT /evidence="ECO:0000256|PIRNR:PIRNR036893"
FT /id="PRO_5013436118"
FT DOMAIN 37..181
FT /note="Lipocalin/cytosolic fatty-acid binding"
FT /evidence="ECO:0000259|Pfam:PF08212"
SQ SEQUENCE 189 AA; 21287 MW; B7B9443889B9B976 CRC64;
MVTALLLLSA LAGLFGVAKG QAFHLGKCPT PPVQENFDVN KYLGKWYEIE KIPVSFEKGS
CIQANYSLME NGNIKVLNQE LRSDGTINQI EGEASQANLT EAAKLGVKFF WLMPSAPYWV
LATDYKNYAL VYSCTTILWL FHVDHVWILG RNPYLPQETV TYLKDILTSN NIDIEKMTVT
DQANCPKFL
//
