ID A0AA39IK90_9BILA Unreviewed; 1428 AA.
AC A0AA39IK90;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 02-APR-2025, entry version 6.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0008006|Google:ProtNLM};
GN ORFNames=QR680_009433 {ECO:0000313|EMBL:KAK0425872.1};
OS Steinernema hermaphroditum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=289476 {ECO:0000313|EMBL:KAK0425872.1, ECO:0000313|Proteomes:UP001175271};
RN [1] {ECO:0000313|EMBL:KAK0425872.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PS9179 {ECO:0000313|EMBL:KAK0425872.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KAK0425872.1};
RA Schwarz E.M., Heppert J.K., Baniya A., Schwartz H.T., Tan C.-H.,
RA Antoshechkin I., Sternberg P.W., Goodrich-Blair H., Dillman A.R.;
RT "Genomic analysis of the entomopathogenic nematode Steinernema
RT hermaphroditum.";
RL Submitted (JUN-2023) 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:KAK0425872.1}.
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DR EMBL; JAUCMV010000001; KAK0425872.1; -; Genomic_DNA.
DR Proteomes; UP001175271; Unassembled WGS sequence.
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 GO; GO:0016020; C:membrane; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR048287; TSPN-like_N.
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 Pfam; PF00041; fn3; 2.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50060; MAM_2; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP001175271};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1428
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041423524"
FT DOMAIN 25..120
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 134..230
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 243..406
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT REGION 890..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1210..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..938
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..988
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1000
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1036
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1428 AA; 155421 MW; F1BA7149EBF1928C CRC64;
MAPSALLLAF FALFGFVSTQ SEWRVPDPPQ NVRTQTTDST ITLWWDPPDS SEEILVRGYT
ISYGVGTPSR KIVIEGVDTN AFTIEFLKPN TTYVFAVTAY NEAEDEDSVK VLLTATTALP
RRRQSSERLF YLSAPLHVRA NAVAPSEVEV RWKDPNEGIE AENAVQRNIY VVQYGVLHTE
KYERLTSESR RVRITNLEPG TEYEVAVKTI VPNGGESAWS IREIVATPRF GDDEIGGGNG
ITEICRFETP SICAFESEAS APLQFRRVLS GADAPLAPNG QIGGHYLAVE TTTLPYDDYG
RLYSRPLDFS VSRYSCLRLL LFVRGDSVGR LLVGTLEKSR PLAERRILFV GALQDQPKTA
WHPFALSIGA RHAPFKVVIE VKKSSSRDHF WLGVDDVSVE SGVCEADSSR DPAMVGNFTG
ASPAPPTRLR ALIAADGYDE HRRRLIAAIP SRAVLYSMSR CATTPTRIGL LLLLLHFFAS
TDGLQTPADE ETDVDLLVPI ESLVNADPRV YRTKGLDGLP AVGMQRGIEI AVPYRLYLPK
RFFRNFAVVA TVKPKDRQGG FLFAVLNAFD TVVDLGVSVE SAGGAQTNIS LFYTDSRVEA
SSRVLASFLV PEFANQWTQL ALEVSDDSVA LYFRCVRFAT RQVNRMPLQL EMDDAHKLYI
GSAGPIVGGA FEVGDAQTLL SDDGGGPDGA AGYDVPRRRL GRYSAPLKTI RTLTQRAIPC
TLPVVAMRVA AVCGLLLFVA GVMVAAETRR RKLSSMAELD ESWDARKPEE LIVEEGLILG
APRRVTAKPL EEEGKGAARR RQKRDLAAVQ IGHGAEVTML TEAPELPLFE AIIVSDDDEY
EEDAEGDLLP GQITIHTVAP PHERTTHVAD EDAVFTELKL FDDPAEAVNQ CNEDWGDEGS
GFGEIRRPSK TDDSEEENEI PRVELPPMPS TPPPPPPSLF TADTALQQFP KEKGEKGDRG
DPGPPGVCAV QCRDGRDGAP GAQGLQGPMG PPGLPGPPGS PGHTFTATHD DNRLYQPLEG
LPGAAGAPGP QGAPGPRGEP GVGLPGPPGV FEGLSDADVA KIASWPGVKG ERGECGPSGL
ADNRIVDNPT GLPPYDSRVH RFTSKGEKGE RGAPGPAGPP GPPGRSIHAP APQTVAGGVV
VFQTSIELFA VAESTPVGAL AFSISSQQLF IRVANGWRQV RLEGFHPAAH EMPSMDSQEE
SVQPEVVTQP TVTRPHYRPS PAPATVPPRH PHIHHHALQE KDRVLHLIAL NAPSSGNMRG
VRGADLLCYQ QARQAGFTTT FRAFVSSHVQ DLFRVVHFGD RETPVVNLRG ERLFASWNDL
FQGGALAPSA PIYSFSRRNV FQDPTWPLRM VWHGSERSGL RSENGYCEAW RNADAFHSGV
ASELRSGRPL MDSLQTVPCN RELVILCVEN MSKFNVDRRL GKRIPRLH
//
