ID A0A6P3QG47_PTEVA Unreviewed; 482 AA.
AC A0A6P3QG47;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE SubName: Full=Neutrophil gelatinase-associated lipocalin isoform X4 {ECO:0000313|RefSeq:XP_011362517.2};
GN Name=LCN2 {ECO:0000313|RefSeq:XP_011362517.2};
OS Pteropus vampyrus (Large flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Pteropodinae; Pteropus.
OX NCBI_TaxID=132908 {ECO:0000313|Proteomes:UP000515202, ECO:0000313|RefSeq:XP_011362517.2};
RN [1] {ECO:0000313|RefSeq:XP_011362517.2}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_011362517.2};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000256|ARBA:ARBA00006889}.
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DR RefSeq; XP_011362517.2; XM_011364215.2.
DR AlphaFoldDB; A0A6P3QG47; -.
DR GeneID; 105294823; -.
DR CTD; 3934; -.
DR Proteomes; UP000515202; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR CDD; cd19457; lipocalin_2-like; 1.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR003087; LCN2/LCN12.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11430; LIPOCALIN; 1.
DR PANTHER; PTHR11430:SF13; NEUTROPHIL GELATINASE-ASSOCIATED LIPOCALIN; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00179; LIPOCALIN.
DR PRINTS; PR01275; NGELATINASE.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000515202};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 332..474
FT /note="Lipocalin/cytosolic fatty-acid binding"
FT /evidence="ECO:0000259|Pfam:PF00061"
FT REGION 41..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 52439 MW; D1FD576A82987883 CRC64;
MGVGLWPGGR GLRCRPALFC PASVREVVTA FHLRAALAAP EPVTSDPDGD AGMPVEAGAR
GENDGFREAE DGVKLPLRRS GLSRVTSFPR GQYAKEKEEE SCRETPDHTP QPGDQAPTTL
PPGLGTLLGT QGTKENQPFR RARPVLTQAT SRGPARGLGS KDPGMAEVEM PSAGVLGATA
QAGEGCRAGR SRPVTAQPAG HLEPTANPAQ STGLQPPCGH RGPSHLHGCS PYTPQPGLGL
SRGLLEVRDD SSTRSEPLTT NRANQSRRNG YRECQGTLCP CQRCGSPGLL WLGLTLLGAL
QTQAQASTPN LIPAPPLLKV PLQQDFQDDQ FQGKWYVVGL AGNAVSKEEQ GKFKMYSTTY
QLKEDHSYNV TSILFRDQNC DYFIRTFVPS SQPGQFSLGN IKAYPEVQSY TVRVVATNYH
QFAMVFFKKV SKNKEYFKIT LYGRTKELTP ELKEDFVRFT KSLGLTDDHI LFPVPIDKCI
DE
//
