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Database: UniProt
Entry: A0AA39M9W7_9BILA
LinkDB: A0AA39M9W7_9BILA
Original site: A0AA39M9W7_9BILA 
ID   A0AA39M9W7_9BILA        Unreviewed;      1456 AA.
AC   A0AA39M9W7;
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:KAK0425870.1};
OS   Steinernema hermaphroditum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=289476 {ECO:0000313|EMBL:KAK0425870.1, ECO:0000313|Proteomes:UP001175271};
RN   [1] {ECO:0000313|EMBL:KAK0425870.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PS9179 {ECO:0000313|EMBL:KAK0425870.1};
RC   TISSUE=Whole animal {ECO:0000313|EMBL:KAK0425870.1};
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:KAK0425870.1}.
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DR   EMBL; JAUCMV010000001; KAK0425870.1; -; 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..1456
FT                   /note="Collagen alpha-1(XV) chain"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041369387"
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          1231..1259
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        1231..1241
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1246..1256
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1456 AA;  158962 MW;  1066808DF94EDA54 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
     HEMPSMPLNL DSYSNSNDLY SYWDSQEESV QPEVVTQPTV TRPHYRPSPA PATVPPRHPH
     IHHHALQEKD RVLHLIALNA PSSGNMRGVR GADLLCYQQA RQAGFTTTFR AFVSSHVQDL
     FRVVHFGDRE TPVVNLRGER LFASWNDLFQ GGALAPSAPI YSFSRRNVFQ DPTWPLRMVW
     HGSERSGLRS ENGYCEAWRN ADAFHSGVAS ELRSGRPLMD SLQTVPCNRE LVILCVENMS
     KFNVDRRLGK RIPRLH
//
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