ID A0A8B8FGL1_9HEMI Unreviewed; 1038 AA.
AC A0A8B8FGL1;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE SubName: Full=Collagen alpha-1(XVIII) chain-like isoform X2 {ECO:0000313|RefSeq:XP_025409485.1};
GN Name=LOC112682925 {ECO:0000313|RefSeq:XP_025409485.1};
OS Sipha flava (yellow sugarcane aphid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Sternorrhyncha; Aphidomorpha;
OC Aphidoidea; Aphididae; Sipha.
OX NCBI_TaxID=143950 {ECO:0000313|Proteomes:UP000694846, ECO:0000313|RefSeq:XP_025409485.1};
RN [1] {ECO:0000313|RefSeq:XP_025409485.1}
RP IDENTIFICATION.
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_025409485.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_025409485.1; XM_025553700.1.
DR AlphaFoldDB; A0A8B8FGL1; -.
DR GeneID; 112682925; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000694846; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF914; OTOLIN-1; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP000694846};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1038
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034341578"
FT DOMAIN 37..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 229..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..658
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..706
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 108582 MW; 0E55F9B86047AB7E CRC64;
MTFRWILIIG VVLWKFVAAD EFSDAKFVTD EIDLQTAIKL PFDDPNLYFD NGDDGFPAFG
IKPGSDIKSP YRLFLPEKLY PEFSIVVNFK LNSANGGFLF AVVNPLENVV QLGVQVVPSS
SNRMNVSFLY TDVNKYSSAS NVLATFSVPW KTGRFTRLSL KVTREAVELI GRCLEPQTVA
VVRDPVELLF DSASTLYIGQ AGPLIKGAFD GAIQEMKIYA SPNYADIQCT GTLQPDDDNN
PGNTEDLANG YSDRPPAPPP PPPSNENHSY QTPNIKGDKG DPGQKGESIR GPPGPPGPPG
SPFSGDFATD EELVKSGVSG PRGPPGVCSC NLTTLFAPGN IPELLPGPPG NPGADGQMGM
TGLPGAAGLP GERGPEGVKG DKGERGDVGQ RGSEGIQGPK GDAGMDGERG LQGPPGPPGP
PGGSDFSNND PSWKPRPIYK DIGFESNVGR PGPPGPKGDP GVDGAPGLKG VKGIQGNKGL
RGEAGTKGSK GDKGHAGSTG PQGFKGERGA RGFDGTPGMP GENARPAPKG EKGDTGTPGP
PGPPGPAVIS GVKIDKSDTT VVKTVKGDKG VKGDRGEKGT VGNLGPGGNP GPPGLTGPKG
ERGEPGLPAP VVSAADLGAH IKGDKGEMGK RGRRGKPGPV GPPGPPGDIG LPGLRGLPGK
AGGLKGEKGE RGESVKGDKG EPGKDGLPGT GGTYLPVPGP PGPPGIPGLS MEGQKGEPGE
PGFSSSPLRS EMNNDAVAVP GALTFPNKKS MINVTDRTQV GTIAFVIEEE ALLVRVARGW
QYISLGSLIP TGTDPAPTNA PMPTRAPLES SNLVHNHPAK DSTMWHPKML RIAALNEPYS
GNMHGVQSVD YSCYRQSQRA GLHGAFKAFL SSRLNNLKTI VHESDRDLPV VNIKGDVLFN
SWNDIFTENG AFISQQPRIY SFSGKNVLAD FSWPQKTIWH GSDPSGYSAV DGNCDAWNSE
SADKRGLGSS LVPRPGAPAK LLDQETAYDC RNFFVVLCVE ITPHSGAMFS RKRRSGAGRH
EEPMSRQEYE RLIDDIRA
//
