ID L5KBC1_PTEAL Unreviewed; 412 AA.
AC L5KBC1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Angiopoietin-related protein 4 {ECO:0000256|ARBA:ARBA00018791};
DE AltName: Full=Angiopoietin-like protein 4 {ECO:0000256|ARBA:ARBA00031877};
GN ORFNames=PAL_GLEAN10002099 {ECO:0000313|EMBL:ELK08071.1};
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:ELK08071.1, 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; KB030936; ELK08071.1; -; Genomic_DNA.
DR RefSeq; XP_006917274.1; XM_006917212.2.
DR AlphaFoldDB; L5KBC1; -.
DR STRING; 9402.L5KBC1; -.
DR GeneID; 102889337; -.
DR KEGG; pale:102889337; -.
DR CTD; 51129; -.
DR eggNOG; KOG2579; Eukaryota.
DR InParanoid; L5KBC1; -.
DR OrthoDB; 3134470at2759; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00087; FReD; 1.
DR Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR Gene3D; 4.10.530.10; Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2; 1.
DR InterPro; IPR036056; Fibrinogen-like_C.
DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR InterPro; IPR020837; Fibrinogen_CS.
DR PANTHER; PTHR19143:SF256; ANGIOPOIETIN-RELATED PROTEIN 4; 1.
DR PANTHER; PTHR19143; FIBRINOGEN/TENASCIN/ANGIOPOEITIN; 1.
DR Pfam; PF00147; Fibrinogen_C; 1.
DR SMART; SM00186; FBG; 1.
DR SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..412
FT /note="Angiopoietin-related protein 4"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003969063"
FT DOMAIN 185..407
FT /note="Fibrinogen C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51406"
FT COILED 108..149
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 412 AA; 45458 MW; 84D7AFE44F40C560 CRC64;
MRCASTAGAA LVLCAATAGL LRAQGRPAPA EPPPRFASWD EVNVLAHGLL QLGQGLREHV
ERTRGQLGAL ERRLGACGAA CEEPRASAAP PHVSASLVPH GEVAPETLRS MQMQLKAQNS
RIEQLFQKVA QQQRHLEKQH LRIQNLQSQV GLLAPMHLGH GLTQPARKKR LPKMAQLVGP
VHNISHLQRL PRDCQELFED GERQSGLFRI QPRGSLPFLV NCKMTSDGGW TIIQRRQDGS
VDFNQPWEAY KAGFGDPQGE FWLGLEKVHL ILGGRGSRLA VQLQDWEGNA ESLQFPVHLG
GEDTAYSLQL TAPVASKLGA TTVMPSGLSL PFSTWDQDHD LRGDKNCAKS LSGGWWFGTC
GHSNLNGQYF HSIPQQRQQR KKGIFWKTWR GRYYPLQATT MLIQPTVAKA AS
//
