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Database: UniProt
Entry: A0AA97MPQ3_9PASS
LinkDB: A0AA97MPQ3_9PASS
Original site: A0AA97MPQ3_9PASS 
ID   A0AA97MPQ3_9PASS        Unreviewed;      1330 AA.
AC   A0AA97MPQ3;
DT   27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT   27-MAR-2024, sequence version 1.
DT   08-OCT-2025, entry version 8.
DE   SubName: Full=COFA1 protein {ECO:0000313|EMBL:NXE96279.1};
DE   Flags: Fragment;
GN   Name=Col15a1_1 {ECO:0000313|EMBL:NXE96279.1};
GN   ORFNames=MENNOV_R07190 {ECO:0000313|EMBL:NXE96279.1};
OS   Menura novaehollandiae (superb lyrebird).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Menuridae; Menura.
OX   NCBI_TaxID=47692 {ECO:0000313|EMBL:NXE96279.1};
RN   [1] {ECO:0000313|EMBL:NXE96279.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B10K-CU-030-46 {ECO:0000313|EMBL:NXE96279.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:NXE96279.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
CC   -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC       {ECO:0000256|ARBA:ARBA00061275}.
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:NXE96279.1}.
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DR   EMBL; VWPS01000369; NXE96279.1; -; Genomic_DNA.
DR   Proteomes; UP000521578; 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:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR   CDD; cd00247; Endostatin-like; 1.
DR   FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR   FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR   FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR   Gene3D; 2.60.120.200; -; 1.
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; IPR050149; Collagen_superfamily.
DR   InterPro; IPR010515; Collagenase_NC10/endostatin.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR048287; TSPN-like_N.
DR   InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR   PANTHER; PTHR24023:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   Pfam; PF20010; Collagen_trimer; 1.
DR   Pfam; PF06482; Endostatin; 1.
DR   SMART; SM00282; LamG; 1.
DR   SMART; SM00210; TSPN; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Collagen {ECO:0000256|ARBA:ARBA00023119};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW   Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000521578};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          8..196
FT                   /note="Thrombospondin-like N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00210"
FT   DOMAIN          57..195
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|SMART:SM00282"
FT   REGION          198..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..674
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..737
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          984..1006
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1021..1073
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..566
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..669
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..735
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..795
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1039..1051
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1070
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NXE96279.1"
FT   NON_TER         1330
FT                   /evidence="ECO:0000313|EMBL:NXE96279.1"
SQ   SEQUENCE   1330 AA;  139538 MW;  14A4541ACCF6161D CRC64;
     AERGSKGHLD LTELIGVPLP PSVYFVTGYG GFPAYSFGPD SNIGRLTSAI IPSPFYRDFA
     IVVTVKPNSD RGGVLFAITD AFQKTIYLGL RISPVDDSTQ RIIMYYTEPG SHISREAASF
     KVPVMTNRWN RFTVTVQGND VALFMDCEEY QRLQFQRSAR TLAFESGSGI FVGNAGATGL
     EKFTGSIQHL TIKFDPRATE DHCEDDDPYA SGDSSGNGSI QEHEVSEAQE ALAPSHLPQR
     PEDTLAEPVE APPTILSYLE ENYFSGNHRS EETSEAAKFK EQGTTWGAAV IETGQGNRES
     TSVTQKILRE EDGSGAGVLP GVSGVLYNGF ITSQIFFFHL CLVLLLPRCR IWHLFSFSFM
     LLITAQCFNL SRSLCKASCS SRLPAAPPSL LLANANLLML LSTPASRSLR HILNRTGPRI
     ESQETPLGTG YQPDVALFTA SLELCPSDSS SSKNLRRSFQ TTVTICSNGT LRFSKYFVIS
     AVVVQLAHCR VQMQPAKCPP KQPSLPLYCG KSRCGERHIL DTASCIEVQN PVSPPTAQTK
     NYNLAPLDPA SAAKCPPGLP GLPGKPAPDS GVGPPGSPGE DGASGGPGPE YNLQGPQGPP
     GHDGVVGPRG WKGEKGDQGL PGSAGPKGDT GVTGSIGPKG EAGPVGSPGK PGPPGPPGPP
     GSPGPPGPPG LSYSLGSELE KTHFIIFPFK SLMLFFFYHL QGPKGEKGDP GHQGEPGQDG
     SSIVGPPGPP GPPGPVIAIP ELLLNDTDGI FNVTEIKGLL GPPGADGKPG LPGFPGPRGP
     KGDTGLPGSQ GPKGQQGEKG EPGAIIAADG SLTGLLGRKG EKGEAGVVGP AGPMGPIGPT
     GPKGELGFPG RPGRPGLNGL RGVKGDRGEA FNGLPGLPGP PGPPGPPGRI LYIKGTVFPV
     PPRPRCKTPV STPYPGNQEV FNDHGAKANR DSWGLHSLAH LKGEKGDRGA PGPPGPPLPP
     SYFSHFINSI KGEKGDNGVT GVKGEKGEPN GGVLLTGPPG PPGRPGLVGP KGDSVVGPRG
     PSGLPGLPGL PGYGKIGLPG PPGPPGPPGP PAIHGSAAAM PGPPGPPGEP GSPATRNLVT
     TFQNIEGMLE KVHYVAEGTL IYLRETSEVF IRVQNGWRKL QLGELIPIPA DSLPPPAISS
     HGFQSIPVLR SISNMNNGKP ALHLVALNFP FSGDMRADFQ CFQQAQLAGL TSTYRAFLSS
     HLQDLATVVR KTDRYHLPIV NLQGETLFSN WESIFDGNGG QFNIHVPIYS FDGRNVMTDS
     SWPQKVIWHG STANGIRLVS NYCEAWHTAD MGAMGQASPL KTGKLLDQKV YSCNNQFIVL
     CIENSFVSDP
//
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