ID A0A7L3S8G8_CEPGR Unreviewed; 1349 AA.
AC A0A7L3S8G8;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
DE Flags: Fragment;
GN Name=Col15a1_1 {ECO:0000313|EMBL:NXV24073.1};
GN ORFNames=CEPGRY_R09026 {ECO:0000313|EMBL:NXV24073.1};
OS Cepphus grylle (Black guillemot) (Alca grylle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes; Alcidae;
OC Cepphus.
OX NCBI_TaxID=28697 {ECO:0000313|EMBL:NXV24073.1, ECO:0000313|Proteomes:UP000578766};
RN [1] {ECO:0000313|EMBL:NXV24073.1, ECO:0000313|Proteomes:UP000578766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUT-0020 {ECO:0000313|EMBL:NXV24073.1};
RC TISSUE=Liver {ECO:0000313|EMBL:NXV24073.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Restin potently inhibits angiogenesis.
CC {ECO:0000256|ARBA:ARBA00058706}.
CC -!- FUNCTION: Structural protein that stabilizes microvessels and muscle
CC cells, both in heart and in skeletal muscle.
CC {ECO:0000256|ARBA:ARBA00058695}.
CC -!- SUBUNIT: Interacts moderately with EFEMP2.
CC {ECO:0000256|ARBA:ARBA00065596}.
CC -!- SUBUNIT: Trimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00061770}.
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:NXV24073.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; VZUD01000964; NXV24073.1; -; Genomic_DNA.
DR Proteomes; UP000578766; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
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; 3.40.1620.70:FF:000002; Collagen alpha 1 (XV) chain; 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; 3.40.50.12690; -; 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; IPR001791; Laminin_G.
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; 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:UP000578766};
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 403..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1037..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..425
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..589
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..630
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..685
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..739
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..749
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..979
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1067
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1086
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NXV24073.1"
FT NON_TER 1349
FT /evidence="ECO:0000313|EMBL:NXV24073.1"
SQ SEQUENCE 1349 AA; 141976 MW; 71AD0A48CEF46D1D CRC64;
TERGSKGHLD LTELIGVPLP PSVYFVTGYG GFPAYSFGPD ANIGRLTSAI VPLPFYRDFS
IAVTVKPNSD RGGVLFAITD AFQKTIYLGM RLSPVDDSTQ RIIMYYTEPG SHVSREAASF
KVPVMTDRWN RFTVTVQGNY VALFMDCEEY QKVQFQRSAQ ALVFESGSGI FVGNAGATGL
EKFTGSIQHL TIKSDPRATE DHCEDDDPYA SGDTSGNGSI QEHEGISETQ EVLAPSHLPI
RPEDTLAEPV EAPPTILSYL EENDFSGNHR SEEISGAAKL KEQGTTSFFY LVGEWRGWSF
MFSSGQGNSE STTATQEILR EEDGSGASVL PGVSREETSG CRVCPALTPV SDGNDGHACR
RCAQVEDLLQ LVMELREEVS KLRSIRECER EIDSWSRILH PVTEAQQADR TPATESSLSS
VTSTEGGNLE DRGQWQEVPA RRNRRRTRDC PVTTPSSQMP LFNRYSALQR NLDDDEHNIS
PISPTLEPSA RSSQISPCIK TSAIKKKRRV LVIGDSLLKG AEGPICRPDP VHREVCCLPG
ARVKDVKRML PSLVRPSDYY PLLLFQVGSD EGLPGPPGPP GLPGLPGKPA PNSGVGPPGS
PGEDGASGER GPEGPQGPPG LDGVVGPPGQ KGEKGDRGLP GSVGPKGDTG VTGSIGPKGQ
AGAVGSPGKP GPPGPPGPPG PPGPPGLSYS LGFEVFCYYR VCCSYGSSFL QSRGSGPKGE
KGDPGPQGEP GQDGNSIVGP PGPPGPPGPI IAIPELLVND TDGIFNFTGI KGLLGPPGPD
GKPGLPGFPG PRGPQGDTGL PGLQGRKGQQ GEKGEPGAII TSNGSLTELL GRKGEKGEAG
VVGPVGPMGP IGPTGPKGEL GFPGRPGRPG LNGVRGVKGD RGEAFNGLPG LPGPPGPPGP
PGRIVYIKGT VFPVSPRPHC KMPVSHTENL LLAKCMAMTV HNQSAKANKD SWGLHRSADL
KGEKGDKGAP GPPGPPLPPS YFSHFINSIK GEKGDNGVSG VKGEKGEPNG GFFLTGPPGP
PGRPGLVGPK GDSVVGPRGP PGLPGLPGLP GYGKIGPPGP PGPPGPPAIY GSAATMPGPP
GPPGEPGSPA TRNLVTTFQN IEGMLEKVHL VAEGTLIYLS ETSEVFIRVR NGWRKLQLGE
LIPIPADSLP PPAISSHGFQ SLPALSPVSN MNNGRPALHL VALNSPFSGD MRADFQCFQQ
AQLAGLSATY RAFLSSHLQD LATVVRKTDR YHLPIVNLKG ETLFNNWEYI FNGNGGQFNV
HVPIYSFDGR NVMTNPSWPQ KVIWHGSTAN GIRLVSNYCE AWHTADMGAM GQASPLKTGK
LLDQKVFSCN NKFIVLCIEI SFVSDPQGK
//
