ID A0A8C1QYY1_CYPCA Unreviewed; 1015 AA.
AC A0A8C1QYY1;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
DE SubName: Full=Collagen type XVIII alpha 1 chain a {ECO:0000313|Ensembl:ENSCCRP00010075266.1};
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962 {ECO:0000313|Ensembl:ENSCCRP00010075266.1, ECO:0000313|Proteomes:UP000694427};
RN [1] {ECO:0000313|Ensembl:ENSCCRP00010075266.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCCRP00010075266.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR AlphaFoldDB; A0A8C1QYY1; -.
DR Ensembl; ENSCCRT00010083408.1; ENSCCRP00010075266.1; ENSCCRG00010032826.1.
DR Proteomes; UP000694427; Unplaced.
DR GO; GO:0005594; C:collagen type IX trimer; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
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:SF372; COLLAGEN ALPHA-1(XVI) CHAIN; 1.
DR Pfam; PF01391; Collagen; 1.
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 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000694427};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1015
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034207364"
FT DOMAIN 32..221
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 244..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..350
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..381
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..398
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..538
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..587
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..629
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..653
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..675
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 107648 MW; 817C123459C9F200 CRC64;
MARRWVAFLE LLLCCLLIAL SPAASQRREE SGVSLLQLIG DPPPVGVSKV FDHDNSPGYV
FDQSSNVGQS AAAHLPNPFF RDFSLIFNIK PTSSKPGVIF SITDPTQNIM YVGVKLSAVE
KGKQYIIFYY TEPDSESSYE AARFSVPSMV NTWTRFSISV LNERVSLYFN CDSDPQVISF
ERSPDDMDLD VGAGVFVGHA SGADPNKFLG VIGDVRVLKD PGAAERHCEE DEDDFDAVRL
KAHKLSNKSP TPPSSRPIQQ PPVTSRPLVE KQLTGGKGEK GDRGEKGAKG ERGLVGPKGD
SGSGSGGSAK AEKGDAGEKG MKGSSGFGYP GSKGDRGPPG PPGPPGPPGP SAEVELRGDG
SVLQKVAGPR GPPGPEGPPG PAGAEGEPVS PPGQNGAPGQ PGPVGPKGVR GEPGSPGYGI
KVCKQKPIDI AKYEVFKNLK FTIVTSFYLQ GEKGEPGLIL GPDGNPLYHG GLTGLKVLYY
FGPAGPPGLK GEFGMPGRPG RPGVNGYKGE KGESGSGSGY GYPGPPGPPG PPGPPGPALP
LDRFSVSAFL FGHFFPTGFS SNVDIYALKN EMKGEQGEPG LKGEKGEPGG GFYDPRFGAV
QGPPGNPGPT GPKGDSIRGP PGPQGPPGAP GVGYDGRPGN PGPPGPPGPP GSPSLPGAYR
PQLSIPGPPG PPGPPGVSGT GSGVTFLRSY DIMMATARRQ SEGALIYILD RNDLYLRVRD
GVRQVMLGDY KTFYGELDNE VAAVQPPPVV HYSQDHTADN GAEQISPPHQ PIEFPRREPE
NRNPSPTDSR YPDPQYPPYT DPVQPHRHPV QPERNPITPA RRPSPPVNQP EGHTHTSGPG
LHLIALNSPQ VGNMRGIRGA DFLCFQQARA VGLKGTFRAF LSSKLQDLYS IVRRSDRETL
PIVNLKDQVL FRSWESLFSD SESRMKDNAP IYSFDGRDVL RDSAWPEKMI WHGSSGRGHR
QTDNYCETWR AGDRAVTGLA SSLQAGQLLQ QTSSSCSSSY IVLCIENSYM TQSKK
//
