ID I3IVH1_ORENI Unreviewed; 370 AA.
AC I3IVH1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Asporin {ECO:0000256|PIRNR:PIRNR002490};
GN Name=aspn {ECO:0000313|Ensembl:ENSONIP00000000611.1};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000000611.1, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000000611.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|PIRNR:PIRNR002490}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class I subfamily. {ECO:0000256|ARBA:ARBA00009811,
CC ECO:0000256|PIRNR:PIRNR002490}.
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DR AlphaFoldDB; I3IVH1; -.
DR STRING; 8128.ENSONIP00000000611; -.
DR Ensembl; ENSONIT00000000610.2; ENSONIP00000000611.1; ENSONIG00000000479.2.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000157444; -.
DR HOGENOM; CLU_000288_186_0_1; -.
DR InParanoid; I3IVH1; -.
DR OMA; NRIQKDA; -.
DR TreeFam; TF334562; -.
DR Proteomes; UP000005207; Linkage group LG5.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR InterPro; IPR016352; SLRP_I_decor/aspor/byglycan.
DR PANTHER; PTHR45712; AGAP008170-PA; 1.
DR PANTHER; PTHR45712:SF2; ASPORIN; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF01462; LRRNT; 1.
DR PIRSF; PIRSF002490; SLRP_I; 1.
DR SMART; SM00369; LRR_TYP; 5.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002490-1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530,
KW ECO:0000256|PIRNR:PIRNR002490};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..370
FT /note="Asporin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013062282"
FT DOMAIN 64..96
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
FT REGION 39..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 65..71
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 69..78
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 323..356
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
SQ SEQUENCE 370 AA; 42195 MW; E91320796878E7E0 CRC64;
MRIFLLLCLL ALGNAKPYQP INVMDYLKNY DTKIHEIMMS DSNDDDDDDE VDDDDDDDDY
NDEDCPAHCH CSPRVVQCSD QGLISVPDKI PEDTVMIDLQ NNDITEIQQD DFKGLNKLYG
LFLINNKISR IHPKAFKNMD NLRLLYLSYN MLNEIPANLP PNVIELRFHE NQIDRIQKDA
FKGLRKLHVL ELGANPLTNS GIEIGAFNGL STLYIGIAEA KLTSIPKDFP SSITELSLDY
NKISKVEIED FIRYKNLQRL GLAFNQIKYV ENGSLANTPK IREIYLDNNR MRKVPPGLSS
LRYLQVIFLH GNKISSVGIN DFCPIRADSK KNPYTGISLF ANPVKYWAIQ PATFRCVTGR
RGVQLGNFRK
//