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Database: UniProt
Entry: A0A8B7ZK18_ACAPL
LinkDB: A0A8B7ZK18_ACAPL
Original site: A0A8B7ZK18_ACAPL 
ID   A0A8B7ZK18_ACAPL        Unreviewed;      1822 AA.
AC   A0A8B7ZK18;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 18.
DE   SubName: Full=Collagen alpha-1(II) chain-like isoform X1 {ECO:0000313|RefSeq:XP_022105968.1};
GN   Name=LOC110987500 {ECO:0000313|RefSeq:XP_022105968.1};
OS   Acanthaster planci (Crown-of-thorns starfish).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC   Valvatacea; Valvatida; Acanthasteridae; Acanthaster.
OX   NCBI_TaxID=133434 {ECO:0000313|Proteomes:UP000694845, ECO:0000313|RefSeq:XP_022105968.1};
RN   [1] {ECO:0000313|RefSeq:XP_022105968.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   RefSeq; XP_022105968.1; XM_022250276.1.
DR   GeneID; 110987500; -.
DR   KEGG; aplc:110987500; -.
DR   OrthoDB; 5983381at2759; -.
DR   Proteomes; UP000694845; Unplaced.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR050938; Collagen_Structural_Proteins.
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; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR   PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR   Pfam; PF01391; Collagen; 7.
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:UP000694845};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..1822
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5034069432"
FT   DOMAIN          42..233
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   REGION          232..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..1020
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1032..1275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1288..1551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        609..621
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..798
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..900
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..911
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        961..971
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1004..1013
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1051
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1063..1074
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1120..1134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1163..1173
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1184..1193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1335..1347
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1470..1480
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1822 AA;  183667 MW;  407021D64F927433 CRC64;
     MELRPALAAL RPHLLLVCLV GLLAAPSQTA ARKYVQSYDK LDFLILTGYP LPNGVKFAEG
     LHGASAFHLE KGTNIGRMAF VIFPTDFTER FSDFTLLVTI KPESEDVGPL LVVTDNLQKT
     VILALNVTQA GQDRHRVELV MRDVVTGTPA SASFLVPSLT DRWSQFSLSI INDMATLFFN
     CSTYDSASLA RPEGWRLTIP QSGAVLVGNQ GSRLGTVASF EGTIQTLEMS NDPDAAEVRC
     DSEPEPPKQR LYKRESSSSA LADALITNKD IPAQPSNSML NGSVHVAMQT SGFNSGGVKS
     KYFSGGKEIE LGSAVGSGSP AGQGITEEPM ISSGMFESSM ESFLQTGTPP VSPDFLHGMD
     TLSETPDMRT TSVSPPGISK AATDLPSKME TASKASIGME MVSQTPPGME MASKVSSGME
     TSSKALSGIG PSSLPPDGMG MSSKVTPRME TVTKPFPVLG TTPETHSERT TTESPVTLPA
     PTEKPDKFTE APSVTDAVTS SPPTVLTVTL PTVAPTGPIM SQLPSEMPVM TAKVSSPQMA
     SDGQESVVVT TSTPLVKVIS ETPVSEDKVM SSPADHATPI PTEKATPKPT EKITPTPTGK
     AAPSSTVNAT PAKTAEATTA PGDKFVSAPT GKAAPTTTDK AMPIPSRTLS SAPVEVVTPT
     PIVKVISGSP GVPGVPGEPG PKGDPGIDGK DGAPGTNGKP GPPGTSGEKG EKGDKGSPGI
     QGPKGALGDP GLTGPSGPEG LPGVAGPPGD KGVPGDTGPI GPSGSKGQKG EPGIGEPGPP
     GQTVTPDPEK IRGAKGEQGK TGVPGPKGEK GDRGGIGLVG PQGDIGLQGA KGEKGDPGEG
     LIGLQGPIGP IGPQGPQGDT GPVAELPEFF DLFEGSGLAD FRGQRGKKGQ DGQPGQAGPQ
     GPVGPPGPPG PQGNQGAPGS PGMPGVPGTP GRPGTVGMNY TGLNGLCCRD GLNGSQGPPG
     IQGPPGPPGP PGQNGTAGTS GETGKPGVPG IEGPPGMKGD PGIAGPPGPP GPPGKIYIMP
     TDATPTAISK LFTDGDASAG SGSPPQITKS PVNGGVDLIP GEPGAPGPPG PQGPPGATGE
     RGEIGLLGER GPKGDKGSPG TQGIQGPKGD TGPQGLPGKN GKDGREGPQG KQGERGVGLP
     GDKGDAGSMG PSGMPGEQGI MGPPGPPGPP GPPGEVMIDV DGQMSEKGEK GDSGEVGPRG
     PRGQKGEAGL NGIPGFHGTK GDRGERGPAG MDGAPGAQGD MGPKGDQGPE GIQGRDGLDG
     MPGPRGPQGE KGEPYIPDES ALVLLKGMRG PRGPRGPKGH FGIPGRPGNH GDIGPPGLSG
     PAGADGVPGI GIPGEKGEQG MKGEKGEPAI IGTALPLASG VKGEKGDPGE RGPSGKRGPA
     GPQGVPGFPG VNGLNGPKGE PGEPGEEGRP GAMGHPGVDG VPGSTGPQGP KGDKGSPGIG
     LKGEQGRPGN PGPPGFGVPG IDGPQGPQGL PGPPGPPGPR GPTGASDLPE GSYIPIEGLP
     GPQGFPGIDG EDGAPGEPGR PGDPGLRGPE GRPGEPGPRG FPGPASSGQL TSFSSINDMI
     QQAASLTPGT IAFVTDVQEL YLRRDNGMTQ ILLGATFNLD PVPPLLTTST TTPSPQTHST
     TEKVFTIPST KPGLPGPDLE LGDQPMLYMY ALNHPMTGDT YSEDSIGGLS GADSHCFQQA
     QQARLPGTYR AFLSSRVQDV KSVVNKDYHH LPVANAKDEI MFQSWAGIFN GKGATFDSDK
     HIYSFDGKDV MTDDEWDQKY IWHGSYVDGR RMADSYCEEW RTYDGSASGQ ASPLGSHKLL
     GQETQLCSNA LVVLCVQVSP DT
//
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