ID A0A7K4Q7W3_MELMO Unreviewed; 1308 AA.
AC A0A7K4Q7W3;
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:NWQ57064.1};
DE Flags: Fragment;
GN Name=Col15a1_0 {ECO:0000313|EMBL:NWQ57064.1};
GN ORFNames=MELMEL_R07711 {ECO:0000313|EMBL:NWQ57064.1};
OS Melospiza melodia (Song sparrow) (Fringilla melodia).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Passerellidae; Melospiza.
OX NCBI_TaxID=44397 {ECO:0000313|EMBL:NWQ57064.1, ECO:0000313|Proteomes:UP000560247};
RN [1] {ECO:0000313|EMBL:NWQ57064.1, ECO:0000313|Proteomes:UP000560247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUT-0008 {ECO:0000313|EMBL:NWQ57064.1};
RC TISSUE=Blood {ECO:0000313|EMBL:NWQ57064.1};
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:NWQ57064.1}.
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DR EMBL; VZSA01001439; NWQ57064.1; -; Genomic_DNA.
DR Proteomes; UP000560247; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; IPR050938; Collagen_Structural_Proteins.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR37456:SF6; COLLAGEN ALPHA-1(XXIII) CHAIN-LIKE ISOFORM X2; 1.
DR PANTHER; PTHR37456; SI:CH211-266K2.1; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 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:UP000560247};
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 REGION 191..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..568
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..709
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..769
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..935
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1026
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1045
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWQ57064.1"
FT NON_TER 1308
FT /evidence="ECO:0000313|EMBL:NWQ57064.1"
SQ SEQUENCE 1308 AA; 136768 MW; F9AF3E3FA25796FC CRC64;
TERGSKGHLD LTELIGVPLP PSVYFVTGYG GFPAYSFGPD SNIGRLTSAI IPSPFYSDFA
IAATVKPNSD RGGVLFAITD AFQKTIYLGL RISPVDDSTQ RIIIYYTEPG SHISREAASF
KVPVMTNRWN KFTVTVEGNY IALFMDCEEY QRLQFQRPAR TLVFESGSGI FVGNAGATGL
EKFTGSIQHL TIKSDPRTTE DHCEDDDPYA SGDSSGNGSI QEHDSSEAQE ALAPSHLPIR
PEDSLAEPVE APPTILVYLE ENDFSGNHRS EETSEAAKFK EQGTASTVME TGQDNNESTT
VTQKMLREED GSGAGILPGV SREELLLPLL SQLLLCFMLL TSAQCSNLSL CKASCPSGAP
PAPPSLESSA NLLMEVEDGS TESLGGSGIE DVENKDQGPP RSPGKPGQLG QPVSIFSLLK
RTCILERVIV IHHTCMERWN CTALHTVTSY TSVRWVLAQQ LRRILPALHT CQGQGPGGSH
QKAKANSCCA DTEMFSEQQF HQLFGQYCST LPAVMSECGQ RCRTHRSPSG LPGPPGPPGL
PGLPGNPAPD SSVGPPGSSG EDGASGEPGP EGPQGPPGRD GVAGSPGWKG EKGDQGLPGS
AGPKGDTGVT GSIGPKGEAG PIGSPGKPGP PGPPGPPGPP GPPGPPGPSY SLGFEVFCYS
EACCKYGYIS SRRKTGPKGE KGDPGPRGEP GQDGNSIVGP PGPPGPPGPV IAIPELLLNE
IDGISNFTEI KGLLGPPGPD GKPGLPGFSG PRGPKGDTGL PGSQGPKGQQ GEKGEPGAIF
SADGSLTKLL GRKGEKGEAG VMGPVGPMGP IGPTGPKGEL GFPGRPGRPG LNGLRGVKGD
RGEAFNGLPG LPGPPGPPGP PGRILYIKGT VFPVPPRPHC KMPPLLFPSS YEFVMLFMAG
AKANRDSWGL HSSAHLKGEK GDRGAPGPPG PPLPPSYFSH FINSIKGEKG DNGVTGVKGE
KGEPNGGFFL TGPPGPPGRP GLIGPKGDSV VGPRGPPGLP GLPGLPGYGK IGPPGPPGPP
GPPGPPAIYG SAVAMPGPPG PPGEPGSPAT RNLVTTFQNI EGMLEKVHYV AEGTLIYLRE
TSEVFIRVQK GWRKLQLGEL IPIPADSPPP PAISSHGFQS IPALRPISYM NNGKPALHLV
ALNFPLSGDM RADFQCFRQA QLAGLTSTYR AFLSSHLQDL ATVVRKTDRH HLPVVNLQGQ
TLFSNWESIF DGNGGQFNIH VPIYSFDGRN VMTDSSWPQK IIWHGSTANG IRLVSNYCEA
WHTADMGAMG QASPLNTGKL LDQKVYSCNN QFIVLCIENS FVSDPQGK
//
