ID A0A7K8KBZ6_9AVES Unreviewed; 1319 AA.
AC A0A7K8KBZ6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 16.
DE SubName: Full=COFA1 protein {ECO:0000313|EMBL:NXE13793.1};
DE Flags: Fragment;
GN Name=Col15a1_0 {ECO:0000313|EMBL:NXE13793.1};
GN ORFNames=LOPRUF_R04272 {ECO:0000313|EMBL:NXE13793.1};
OS Lophotis ruficrista.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Otidimorphae; Otidiformes;
OC Otididae; Lophotis.
OX NCBI_TaxID=172689 {ECO:0000313|EMBL:NXE13793.1, ECO:0000313|Proteomes:UP000533896};
RN [1] {ECO:0000313|EMBL:NXE13793.1, ECO:0000313|Proteomes:UP000533896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-CU-031-23 {ECO:0000313|EMBL:NXE13793.1};
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:NXE13793.1}.
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DR EMBL; VWYV01001156; NXE13793.1; -; Genomic_DNA.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000533896; 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:0032836; P:glomerular basement membrane development; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1094; COLLAGEN TYPE XVIII, ALPHA 1 ISOFORM X1-RELATED; 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:UP000533896};
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 193..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..565
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..597
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..652
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..711
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..721
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..946
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1037
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1059
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXE13793.1"
FT NON_TER 1319
FT /evidence="ECO:0000313|EMBL:NXE13793.1"
SQ SEQUENCE 1319 AA; 139858 MW; 43DACE320D489EBA CRC64;
TERGSKGHLD LTELIGVPLP PSVYFVTGYG GFPAYSFGPD ANIGRLTSAI IPSPFYRDFA
IVVTVKPTSD RGGVLFAITD AFQKTIYLGM RLSPVDDSTQ RIIMYYTEPG SYISREAASF
KVPVMTNRWN RFTVTIQGND VALFMDCEEY QRVQFQRSAQ ALVFEPGSGI FIGNAGATGL
EKFTGSIQHL TIKSDPRATE DHCEDDDPYA SGDSSGNGSI QEHEGISEMQ EVLAPSHHPI
RPENTLAEPV EAPPTVLSYL EENDSAVMET GRGNSESTTV TQKILREEDG SGASVLPAVS
REVCTVSVPY TLSFEDVQKK DQGPPGLPGK LGQHGQPVSN FYLLKECMYF TKSNSHLSHM
HKGLKLHSLT HCHQLYFYKW VFSPTKSTQD CHICFAHVSR AIQGPDERQS SESTRQTTDI
SKWLRVRKFE ESFSDSCHYF FLWNIIVFKI FVISAVWSHW YPIIFNALPS FHLCPPSRLH
CHFVVDRVDV ARGTLRAHLP AWKLRISQCS SMEKPFEISR EKPNHLAVFS DPLISFWLSP
PGLPGLPGKP APDSDVGPPG SPGEDGASGE PGPETYYHLQ GPQGPPGLDG VVGPPGQKGE
KGDKGLPGSA GPKGDTGVTG SRGPKGEAGA VGSPGKPGPP GPPGLPGPPG PPGPPGLSYS
LGFEVFCYYG VCCSYGLCSF FFFYHMQGPK GEKGDPGPQG EPGQDGKSIV GPPGPPGPPG
PIIAIPELLL NDTDGIFNFT GIKGLLGPPG QDGKPGLPGF PGPRGPKGAT GLPGPQGPKG
QQGEKGEPGA IIAANGSLTE ILGRKGEKGE AGVVGPVGPM GPIGPTGPKG ELGFPGRPGR
PGLNGLRGVK GDRGEAFNGL PGLPGPPGPP GPPGRIVYIK GTVFPISPRP HCKMPVGTPY
PGNQEPHNVH GAKANRDSWG PHSSADLKGE KGDRGAPGPP GPPLPPSYFS HFINSIKGEK
GDNGVTGVKG EKGEPNGGFF LTGPPGPPGR PGLVGPKGDS VVGPRGPPGL PGLPGLPGYG
KTGPPGPPGP PGPPGPPAIY GSAAAMPGPP GPPGEPGPPA TRNLVTTFQN IEGMLEKVHF
VAEGTLIYLS ETSEVFIRVR NGWRKLQLGE LIPIPADSLP PPAISSHGFQ SLPALSPVSN
MNNGKPSLHL VALNLPFSGD MRADFQCFQQ AQLAGLTSTY RAFLSSHLQD LATVVRRADR
YHLPIVNLKG ETLFNNWESI FNGNGGEFNI NVPIYSFDGR NVMTDPSWPQ KVIWHGSTAN
GIRLVSNYCE AWHTADMGAM GQASPLKTGK LLDQKVYSCS NQFIVLCIEN SFVSDPQGK
//
