ID A0A7L3T2Y6_RISTR Unreviewed; 1332 AA.
AC A0A7L3T2Y6;
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:NXV34220.1};
DE Flags: Fragment;
GN Name=Col15a1_1 {ECO:0000313|EMBL:NXV34220.1};
GN ORFNames=RISTRI_R10425 {ECO:0000313|EMBL:NXV34220.1};
OS Rissa tridactyla (Black-legged kittiwake) (Larus tridactyla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes; Laridae; Rissa.
OX NCBI_TaxID=75485 {ECO:0000313|EMBL:NXV34220.1, ECO:0000313|Proteomes:UP000540089};
RN [1] {ECO:0000313|EMBL:NXV34220.1, ECO:0000313|Proteomes:UP000540089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUT-0021 {ECO:0000313|EMBL:NXV34220.1};
RC TISSUE=Blood {ECO:0000313|EMBL:NXV34220.1};
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:NXV34220.1}.
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DR EMBL; VZUC01000107; NXV34220.1; -; Genomic_DNA.
DR Proteomes; UP000540089; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1109; COLLAGEN ALPHA-4(IV) CHAIN-LIKE; 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:UP000540089};
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..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..591
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..666
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..719
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..729
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..772
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 950..959
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1050
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1070
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXV34220.1"
FT NON_TER 1332
FT /evidence="ECO:0000313|EMBL:NXV34220.1"
SQ SEQUENCE 1332 AA; 140441 MW; 7034BF16CF7F03EB CRC64;
TERGSKGHLD LTELIGVPLP PSVYFVTGYG GFPAYSFGPD ANIGRLTSAI IPLPFYRDFS
IAVTVKPNSD RGGVLFAITD AFQKTIYLGM RLSPVDDSTQ RIIMYYTEPG SHVSREAASF
KVPVMTDRWN RFTVTVQGNY VALFMDCEEY QKVQFQRSAQ ALVFESGSGI FVGNAGATGL
EKFTGSIQHL TIKSDPRATE DHCEDDDPYA SGDTSGNGSI QEHEGISETQ EVLAPSHLPI
RPEDTLAEPV EAPPAILSYL EENDFSGNHR SEEISGAAKL KEQGTASFFI WLGAVTESGQ
DNSESTTATQ EILREENGSG ASVLPGVSRE EVSKQSASLT LHRHMLPCRL LPSSAVTNFP
DVPLNSCAVI QLHLLLHRSC FPFSAFFYFT LSSVAFDSCT YLCNFTIGFI WLHSAIKLVC
TRFISAMCLP LFYELDTGYS IGKIIIGEKK TFSLTDTFFS LGTISQCKFC TCLIHHIQQC
FVGNTGGFIS ISKKDLRECE WGRSVRKKED NKEIMARGLF KMRKFFYSDS EKTIKRREKT
NRFPLFSDPL ISFWLSPPGL PGLPGKPAPN SGVGPPGSPG EDGASGELGP EGPQGPPGLD
GVVGSPGQKG EKGDQGLPGS VGPKGDTGVT GSIGPKGQAG AVGSPGKPGP PGPPGPPGPP
GPPGPPGLSY SLGFEVFCYY GVCCSYGSTS FRGGTGPKGE KGDPGPQGEP GQDGNSIVGP
PGPPGPPGPI IAIPELLLND TGGIFNFTGI KGLLGPPGPD GKPGLPGFPG PRGPKGDTGL
PGLQGRKGQQ GEKGEPGAII AANGSLTELL GRKGEKGEAG VVGPMGPMGP IGPTGPKGEL
GFPGRPGRPG LNGVRGVKGD RGEAFNGLPG LPGPPGPPGP PGRIVYIKGT VFPVSPRPHC
KMPVSHPQNL HLAKCMAMTV HNQSAKANRD SWGLHRSADL KGEKGDKGAP GPPGPPLPPS
YFSHFINSIK GEKGDNGVTG VKGEKGEPNG GFYLTGPPGP PGRPGLVGPK GDAVVGPRGP
PGLPGLPGLP GYGKIGPPGP PGPPGPPGPP AIYGSAATMP GPPGPPGEPG PPATRNLVTT
FQNIKGMLEK VHLVAEGTLI YLSEISEVFI RVRNGWRKLQ LGELIPIPAD SLPPPAISSH
GFQSLPALSP VSNMNNGRPA LHLVALNSPF SGDMRADFQC FQQAQQAGLS ATYRAFLSSH
LQDLATVVRK TDRYHLPIVN LKGETLFNNW EFIFNGNGGQ FNVHVPIYSF DGRNVMTDPS
WPQKVIWHGS TANGIRLVSN YCEAWHTADM GAMGQASPLK TGKLLDQKVF SCNNKFIVLC
IEISFVSDPQ GK
//
