ID A0A915C787_PARUN Unreviewed; 1082 AA.
AC A0A915C787;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Collagen alpha-1(XVIII) chain {ECO:0000313|WBParaSite:PgR094_g002_t03, ECO:0000313|WBParaSite:PgR094_g002_t11};
OS Parascaris univalens (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Parascaris.
OX NCBI_TaxID=6257 {ECO:0000313|Proteomes:UP000887569, ECO:0000313|WBParaSite:PgR094_g002_t11};
RN [1] {ECO:0000313|WBParaSite:PgR094_g002_t03, ECO:0000313|WBParaSite:PgR094_g002_t11}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2022) to UniProtKB.
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 AlphaFoldDB; A0A915C787; -.
DR WBParaSite; PgR094_g002_t03; PgR094_g002_t03; PgR094_g002.
DR WBParaSite; PgR094_g002_t11; PgR094_g002_t11; PgR094_g002.
DR Proteomes; UP000887569; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24637; COLLAGEN; 1.
DR Pfam; PF01391; Collagen; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000887569};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1082
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041111768"
FT DOMAIN 546..591
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 899..1064
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 64..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..103
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..132
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..245
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..351
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..397
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..527
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1082 AA; 120783 MW; 3D3D1E282BC43DE9 CRC64;
MPLQRALLFT FVATFIVVYY ASAAVTKSPA NSHNKETATV QRDVEDLIVN EGFLLTTIKQ
NQFNNQPTAQ PKKPPSFSGP PSLKPLNASL NRTRRPLRRR KRLRPNDVTG PVTNLSRPSS
RLPMKRLVKV APRKVTNGTD QRMRRKAKAQ NEEEGSDSRE PIPLDAAFLE QFGGNAQISV
VAPRGEGPTI ASSENGPIHD EIEEPHIIEE EEESVFPIAF EEVEVIEPEG GDFSAEYDQE
SELDENAPTQ TFLPDDRLEG SGLEEEAEAI SKAVEPEPAT PSAQRPPYPQ AKAERGEKGD
KGDKGDKGEQ GERGERGEPG PPGPVGPPGV CMAECRDGRD GMPGPRGEQG PMGPPGPPGP
QGPPGQVVQQ SFEDSAYPVR TVVGPPGPQG PPGPQGPMGP RGDAGIGIQG PPGPPGRYMG
LTQEDIDRIV SDPRIKGDRG ECCTSPAKQF PGTDAVPGEL PVYNPALHRF TTKGEKGERG
EHGPMGAMGP MGPQGPMGPM GPMGLQGPPG PMGPAGPAGP PGPPGPAGPS QLTSPSCPQT
STPGCVQVFQ TSIELFSSAS GVSLGSLSFS ISSQQLFIRV NGGWKEVRLE GFHPTLEQRP
SLEVDVHPLP YQPPRQPEVH PQEHPQYRPE YWPDRRLEHR PDQRPAYRPE HRLEYQPQQR
PDYGVTIRPH PRVEYRPEPR PHHRPGQRPE ITIERRPQHP HLKPSEVQPE TRPEYHPERR
PGHRPQQHLQ PRPELVTEQR PEPQEHRPPE YRTEQYPEAP TVQQERPGQV LEQRPETRTR
QRPDEPHVPQ QPQQAPYDER LELQTDRAPE QQPLPELQTE QQLQQVASQE QDRAIDHSLH
QGPYEHPVQT PYPPYPERPR HPEPEQQPHY RERPTPELQH ARHPPTRRPF TLGEKDHVLH
LIALNSPMSG NMRGVRGADL ACYQQARQAG FRTTFRAFLS SHVQDLNKVV HFGDRDTPVV
NLRGERLFNS WSDIFRERPM FDAPLYSFNR RNVFEDNIWR EKRVWHGSDS SGTRSESGYC
NAWRSSDRSQ VGSSSPIGPR LPLLDGCQNI ECSHEFVVLC VENMSKYSVD KRLGKKRMHY
EE
//
