ID A0A194PFF0_PAPXU Unreviewed; 878 AA.
AC A0A194PFF0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE SubName: Full=Collagen alpha-1(XV) chain {ECO:0000313|EMBL:KPI91748.1};
GN ORFNames=RR46_15252 {ECO:0000313|EMBL:KPI91748.1};
OS Papilio xuthus (Asian swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI91748.1, ECO:0000313|Proteomes:UP000053268};
RN [1] {ECO:0000313|EMBL:KPI91748.1, ECO:0000313|Proteomes:UP000053268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI91748.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPI91748.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
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 EMBL; KQ459606; KPI91748.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194PFF0; -.
DR STRING; 66420.A0A194PFF0; -.
DR Proteomes; UP000053268; Unassembled WGS sequence.
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; 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; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000313|EMBL:KPI91748.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000053268};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 595..640
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 677..842
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 137..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..170
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..445
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..517
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 90770 MW; A76DAFF2CE1F37B1 CRC64;
MAMVISQATK AAIGCFLALM ILVAVLVVGV AFGWFDPKRE DEDTPAKISA RLQGRTSFVT
HRAVNPEENR LPVISHSSPY FVGQKGVERD ENGSTDGIVN GDPLASGTLA KLGRSTEANL
PLSEYCQCTP NDISSILESI PGIKGPPGPP GPTGTDGTTG APGKTGQMGD PGPPGPTGMK
GDQGEKGETG TPGIEGQPGP KGDPGADGMP GPQGPTGPPG PPGPVSSALI GNVGPRGPHG
VKGERGQAGR DGLPGLPGPH GRPAEKGEKG ARGPPGPSAT YSPTLLENSI GTGLVRPGLR
DVTSLAKGGK GEKGERGEKG EKGVRGIEGP QGFPGNDGKP GERGDIGPSG LPGTQGVQGN
SGPKGDKGET GAPGPVAISR DEAVIMTKGD KGEPGPRGKR GHPGSPGIRG PPGLPGPPGI
PGTNGVSGDI GLPGWTGPPG ATGQPGPQGP KGEKGDSGFD LEKVKGEKGD RGDDGTPGVP
GREGPRGPPG PPGTPATNIQ YISAPGPPGP PGPPGAPGPG YINEPPDTLT DNPGTNRRVP
NPGKQRDALQ ILRSLNHLMQ NRQELYGLRD PTDNLEDDMD FDDDEEGKAI VGTILFKTTE
SLIKLGIACP RGTLAYIIQE QALLVRVNNG WQYVAMGSLL AIQSSSNGTP TRTPLQNILE
TSSLVHHKNP AGEGPVLRLA ALNEPHTGDM HGVSSTNYEC RRQAQRAGLE GTFGAFISSR
VQTIDSIVSW VDREIPVVNT RGDVLFNSWG EMFDGSGALF AHAPRIFSFS GKNVLVDPNW
PTKAVWHGAG PNGEPAMDAY CDAWHSSSAD KFGLASSLHS NKLLDQETYS CSTRLIVLCI
EATPADTVRR KKRSRLPVGE KLRLLKPVED RNNSRQIL
//