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Database: UniProt
Entry: A0A8S3XIG0_PARAO
LinkDB: A0A8S3XIG0_PARAO
Original site: A0A8S3XIG0_PARAO 
ID   A0A8S3XIG0_PARAO        Unreviewed;       942 AA.
AC   A0A8S3XIG0;
DT   12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT   12-OCT-2022, sequence version 1.
DT   28-JAN-2026, entry version 11.
DE   SubName: Full=(apollo) hypothetical protein {ECO:0000313|EMBL:CAG5025102.1};
GN   ORFNames=PAPOLLO_LOCUS18276 {ECO:0000313|EMBL:CAG5025102.1};
OS   Parnassius apollo (Apollo butterfly) (Papilio apollo).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Parnassiinae; Parnassini; Parnassius; Parnassius.
OX   NCBI_TaxID=110799 {ECO:0000313|EMBL:CAG5025102.1, ECO:0000313|Proteomes:UP000691718};
RN   [1] {ECO:0000313|EMBL:CAG5025102.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tunstrom K.;
RL   Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CAG5025102.1}.
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DR   EMBL; CAJQZP010001172; CAG5025102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8S3XIG0; -.
DR   OrthoDB; 5983381at2759; -.
DR   Proteomes; UP000691718; Unassembled WGS sequence.
DR   GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR   GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR   Pfam; PF01391; Collagen; 4.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000691718};
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          656..701
FT                   /note="Collagen type XV/XVIII trimerization"
FT                   /evidence="ECO:0000259|Pfam:PF20010"
FT   DOMAIN          738..903
FT                   /note="Collagenase NC10/endostatin"
FT                   /evidence="ECO:0000259|Pfam:PF06482"
FT   REGION          79..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..199
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..221
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..417
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..450
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        475..499
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        519..531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..554
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..577
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   942 AA;  97480 MW;  41F31DB2731D10CF CRC64;
     MAMVISQATK AAIGGFLALM ILGAVLVVGT AFGWFDPKRE DEDTPAKISA RLQGRTSFVT
     HRAVNPEENR LPVISHSSPY FIGQKGQKDE NGSTNETMNR DSGTSGTLDK LNEPTDVNMP
     LSDYCQCSVN DISRILESLP ELKGLPGPPG QTGIDGTTGA PGKTGQMGDP GPPGPPGIKG
     EQGERGESGS PGKEGEAGPK GEPGADGTPG LQGPPGPPGP PGAVVSALVK TESTGLYGSS
     NHGNPGTPGE RCPMGLPGPQ GERGYPGNKG EKGLHGSKGD KGDRGYVGIR GPYGAKGERG
     QPGRDGLPGL PGPHGRPAEK GEKGARGLPG PPGILNPGLL ENSVGSSLER SGLRDVSLHS
     KGAKGEKGEQ GEKGEKGVRG IEGPQGFPGN DGKPGERGEI GPSGVPGPQG VPGLNGPKGD
     KGEAGAPGPV AISKDEAVIM TKGDKGEPGP RGKRGHPGPP GLKGSPGLPG PPGIPGTNGI
     SGDIGLPGWT GPPGATGQPG APGPKGDKGD SGIAPFDFGK IKGEKGDRGD DGSPGLPGRD
     GPRGPPGPPG PPGTPATNIQ YVSAPGPPGP PGPPGPPGSF NVNELSGNSL TDSPGVNRRG
     PSVGKQRDAL QILKSLNHLM QSRQEIYGFR DPLDTLEDDT DFDDEDEGKA IVGTILFKTT
     ESLLKLGTPC PRGTLAYILR EQALLVRVNN GWQYVAMGSL LAIQTSPNGE PTRTPLQNVL
     ETSSLIHHKN PAGEGPVLRL SALNEPHTGD MHGVSSTNYE CRRQAQRAGL EGTFRAFISS
     RVQTIDSIVN WVDREIPVVN TRGDVLFNSW GEMFDGSGAL FAHAPRIFSF SGKNVLADVN
     WPTKAVWHGA SPNGEPAMDA YCDAWHSSSA DKFGLASSLH SNKLLDQQTY SCSTRLIVLC
     IEATPADTVR RKKRSNKVTF QVGDKSGLFK DDEENNRTRQ IL
//
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