ID A0A7K9D3M7_9AVES Unreviewed; 1331 AA.
AC A0A7K9D3M7;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE SubName: Full=COFA1 protein {ECO:0000313|EMBL:NXG59099.1};
DE Flags: Fragment;
GN Name=Col15a1_1 {ECO:0000313|EMBL:NXG59099.1};
GN ORFNames=HEMCOM_R09142 {ECO:0000313|EMBL:NXG59099.1};
OS Hemiprocne comata.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Strisores; Apodiformes; Apodidae;
OC Hemiprocninae; Hemiprocne.
OX NCBI_TaxID=243314 {ECO:0000313|EMBL:NXG59099.1, ECO:0000313|Proteomes:UP000518305};
RN [1] {ECO:0000313|EMBL:NXG59099.1, ECO:0000313|Proteomes:UP000518305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-001-23 {ECO:0000313|EMBL:NXG59099.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NXG59099.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) 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:NXG59099.1}.
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DR EMBL; VWZJ01005410; NXG59099.1; -; Genomic_DNA.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000518305; Unassembled WGS sequence.
DR GO; GO:0005594; C:collagen type IX trimer; 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; 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; IPR000477; RT_dom.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF372; COLLAGEN ALPHA-1(XVI) CHAIN; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF00078; RVT_1; 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:UP000518305};
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 544..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..590
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..721
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..796
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..855
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..961
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1049
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1068
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXG59099.1"
FT NON_TER 1331
FT /evidence="ECO:0000313|EMBL:NXG59099.1"
SQ SEQUENCE 1331 AA; 141364 MW; CFF36D3F5C28AEC8 CRC64;
TERGSEGHLD LTELIGVPLP PSVYFVTGYG GFPAYSFGPD ANIGRLTSAI IPLPFYRDFA
IMVTVKPNSD HGGVLFAITD AFQKTIYLGM RLSPADDSTQ RIILYYTEPG SHISQEAASF
QVPVMTNRWN KFTVTVQGND VALFMDCEEY QRSQFQRSAR ALVFDSGSGI FVGNAGAAGL
EKFTGSIQHL IIKSNTKATE DHCEDDDPYA SGDLSGNASV QEHEGISETQ EVLAPSHLPI
RPEDILAEPV EAPPTILSYL EEKVFSGNHS SEETSEAAKL KEQGTASFVP YPTWPLTLPG
MEFPQLLWAA CSSVSLPSPS QNFLLISKHK SLLLQFKTIT PCPLTTSPCN KSLHSFPVGP
LQVLKGHYEI SLEPSLLQAE QLQLSQPVFI GEVLQHSYHL HGPPLDCLQE LHRGRMTSLD
LLATLFFMQP RIPLAFLATR AHCWLMDTFL SIRTPRSFSS ELLSSRSTPI LYWCLGFFLP
RFPTLALIER HEVLLCPTLQ PVQVTLNSST GLWSVSHPSQ FGIISNLLRI HSVPSSRSLM
NKLNKTRPSI DPWGTPLGLP GPPGPPGPPG LPGKPAPSSE GGSPGIPGED GPSGEPGPEV
SRATDIIYPD LSKAFHTVSH NILVSKLEQY GSDGWTTHWI RNWLTGHTQR VVINGSVSKW
KHVTSGVPQG SVVGPVLFTS LLATWTVESS ASSVSLLMTP NCGPKGEKGD PGPQGEPGQD
GNSIVVLPEP PGPPGTIIAI PELLLNNTYG IFNFTGIKGL LGPPGPEGKP GLLGFPGPQG
PKGDAGLPGS QGPKGQQGEK GEPGAIIAAD GSLTELLGRK GEKGEAGVMG PVGPMGPIGP
TGPKGELGFP GRPGRPGLNG LRGMKGDRGK AFTGLPGLPG PPGPPGPPGR IVHIKGTVFP
VSSRPHCKMP VSHIESVFSK MHGHDSAKAS RDSLGLHSSV DFKGEKGDRG APGPPGPPLP
PSYFSHFISS IKGEKGDNGV TGVKGEKGEP NGGFFLAGPP GLPGRPGLVG PKGDSVVGPR
GPPGLPGLPG LPGYGRIGPP GPPGPPGPPA IYGSAAAMPG PPGPPGEPGS PATSNLVTTF
RNIEGMLEKV HFVAQGTLTY LTETSEIFIR VQNGWKKLQL GELIPIPADS LPPPAISSHG
FQSLPALSPI SNMNNGKPAL HLVALNLPFS GDMQADFQCF QQAQLAGLTS TYRAFLSSHL
QDLATVVRKT DRYHLPIVNL KGEILFNNWE SVFNGDGGQF NLDVPIYSFD GRNIMTDPSW
PQKVIWHGST ANGIRLVSNY CKAWHTADMG AMGQASPLKT GKLLDQNVYS CSNQLIVLCI
ENSFVSNPQG K
//
