ID A0A914E5D7_9BILA Unreviewed; 654 AA.
AC A0A914E5D7;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE SubName: Full=Collagen alpha-1(XV) chain {ECO:0000313|WBParaSite:ACRNAN_scaffold57.g13072.t1};
OS Acrobeloides nanus.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Cephalobomorpha; Cephaloboidea; Cephalobidae; Acrobeloides.
OX NCBI_TaxID=290746 {ECO:0000313|Proteomes:UP000887540, ECO:0000313|WBParaSite:ACRNAN_scaffold57.g13072.t1};
RN [1] {ECO:0000313|WBParaSite:ACRNAN_scaffold57.g13072.t1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2022) to UniProtKB.
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DR AlphaFoldDB; A0A914E5D7; -.
DR WBParaSite; ACRNAN_scaffold57.g13072.t1; ACRNAN_scaffold57.g13072.t1; ACRNAN_scaffold57.g13072.
DR Proteomes; UP000887540; Unplaced.
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 Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 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:UP000887540};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 360..403
FT /note="Collagen type XV/XVIII trimerization"
FT /evidence="ECO:0000259|Pfam:PF20010"
FT DOMAIN 455..618
FT /note="Collagenase NC10/endostatin"
FT /evidence="ECO:0000259|Pfam:PF06482"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 654 AA; 72246 MW; 40B3EE34A6D02B04 CRC64;
MDEAEEYELE HPHDSYESVE GKGHIKDIII EDPNTQLPPI EEWVVDFDIE DDYFDEFANL
STGKEHHVEN EPAPISISGQ IGHDRYEAVE GKGHIKVIII DDLNTQLPPI EEWGGDLEIE
DGYFDEFANL STGKEHRVKN EPAPISISGL AGEGTNESLP PQDDLHTTEV PKPHSKSDEE
ADEETPPQVN TSHNKHPWRS KLSFQVPENQ KFEGTQGEKG DKGEKGDKGD KGEPGEKGDQ
GEKGEPGAPG VCMAQCSNAF SHLAGPQGPQ GPPGQVGLPG PPGPPGFNST LDPKNIETLI
DNKIQIAKNE IKTSSGIKGE KGDCACKKPI KGDRGAKGAK GDPGIAGPPG PPSPFGSRAT
LYENIASLFA STRSVPLGTL AYSISDGRLF IRADDGWYEI KLDHFRSTEL RSQPVEVKTF
PSYPYDNNLP RSEALTLESH PRLDQARAHH PDNVLHLIAL NKLMAGNMSG IRGADFACYC
QARKAGFKTT FRAFISTRIQ DLHQVVHPAD REAPIVNLHG ERLFDTWNSI FQGTRVKNAS
IYSYNNKNVF TDPTWFERRF WHGSTEAGHR IAESSCDDWT TSSCSKRGMT SSLRPGETIF
HDNQASNCRR EVGVLCIEVM SKFTAGQRIR KRALWENFKR HNKISNETTT EDSS
//
