ID A0AA39IK83_9BILA Unreviewed; 1439 AA.
AC A0AA39IK83;
DT 24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2024, sequence version 1.
DT 02-APR-2025, entry version 8.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0008006|Google:ProtNLM};
GN ORFNames=QR680_009433 {ECO:0000313|EMBL:KAK0425871.1};
OS Steinernema hermaphroditum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC Steinernema.
OX NCBI_TaxID=289476 {ECO:0000313|EMBL:KAK0425871.1, ECO:0000313|Proteomes:UP001175271};
RN [1] {ECO:0000313|EMBL:KAK0425871.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PS9179 {ECO:0000313|EMBL:KAK0425871.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KAK0425871.1};
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:KAK0425871.1}.
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DR EMBL; JAUCMV010000001; KAK0425871.1; -; 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..1439
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041221925"
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 902..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..949
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..999
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1011
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1047
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1439 AA; 156929 MW; 813CAB502FBD195B 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 CNEDWWKQRR
RAKLRKGDEG SGFGEIRRPS KTDDSEEENE IPRVELPPMP STPPPPPPSL FTADTALQQF
PKEKGEKGDR GDPGPPGVCA VQCRDGRDGA PGAQGLQGPM GPPGLPGPPG SPGHTFTATH
DDNRLYQPLE GLPGAAGAPG PQGAPGPRGE PGVGLPGPPG VFEGLSDADV AKIASWPGVK
GERGECGPSG LADNRIVDNP TGLPPYDSRV HRFTSKGEKG ERGAPGPAGP PGPPGRSIHA
PAPQTVAGGV VVFQTSIELF AVAESTPVGA LAFSISSQQL FIRVANGWRQ VRLEGFHPAA
HEMPSMDSQE ESVQPEVVTQ PTVTRPHYRP SPAPATVPPR HPHIHHHALQ EKDRVLHLIA
LNAPSSGNMR GVRGADLLCY QQARQAGFTT TFRAFVSSHV QDLFRVVHFG DRETPVVNLR
GERLFASWND LFQGGALAPS APIYSFSRRN VFQDPTWPLR MVWHGSERSG LRSENGYCEA
WRNADAFHSG VASELRSGRP LMDSLQTVPC NRELVILCVE NMSKFNVDRR LGKRIPRLH
//
