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Database: UniProt
Entry: A0A194PFF0_PAPXU
LinkDB: A0A194PFF0_PAPXU
Original site: A0A194PFF0_PAPXU 
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).
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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
//
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