ID F1LPD0_RAT Unreviewed; 1323 AA.
AC F1LPD0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 28-JAN-2026, entry version 99.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=Col15a1 {ECO:0000313|Ensembl:ENSRNOP00000017217.8,
GN ECO:0000313|RGD:1310820};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000017217.8, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0007829|PubMed:16641100}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000017217.8}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000017217.8};
RA Doris P.A., Kalbfleisch T., Li K., Howe K., Wood J.;
RT "GRCr8: a new rat reference genome assembly contstructed from accurate long
RT reads and long range scaffolding.";
RL Submitted (JAN-2024) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSRNOP00000017217.8}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000017217.8};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSRNOP00000017217.8}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000017217.8};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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 ---------------------------------------------------------------------------
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 STRING; 10116.ENSRNOP00000017217; -.
DR Ensembl; ENSRNOT00000017217.9; ENSRNOP00000017217.8; ENSRNOG00000060381.3.
DR AGR; RGD:1310820; -.
DR RGD; 1310820; Col15a1.
DR VEuPathDB; HostDB:ENSRNOG00000060381; -.
DR GeneTree; ENSGT00940000158302; -.
DR HOGENOM; CLU_004003_0_0_1; -.
DR InParanoid; F1LPD0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000039197; Expressed in skeletal muscle tissue and 7 other cell types or tissues.
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; 3.10.100.10; 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:SF1019; COLLAGEN ALPHA-5(IV) CHAIN ISOFORM X1; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF13385; Laminin_G_3; 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 1: Evidence at protein level;
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:UP000002494};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1323
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035224242"
FT DOMAIN 40..228
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 89..227
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 269..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 931..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..287
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..594
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 136072 MW; 3C7003B84ECF5154 CRC64;
MTHRRTAQGR RPRWLLSIIS TLLSTVLQTR AATGSASQDH LDLTELIGVP LPSSVSFVTG
YGGFPAYSFR PGANVGRPAR TLIPSTFFRD FAIGVAVKPS SAQGGVLFAV TDAFQKVIYL
GLRLSRVEDG RQRVILYYTE PGSHVSQEAA AFSVPVMTNR WNRFAVTVQG EEAVLFMDCE
EHSQVLFQRS SRPLTFEPSA GIFVGNAGAT GLERFTGSIQ QLIIYSDPRT PEELCEAQES
SASGEASGFQ EMDEVAEIME AVTYTQAPPK EAHVDPISMP PTSSSPTEDT ELSGEPVPEG
TPGTDLSITG HSSPEQGSGE ILNDTLEVRT VDGNPSTDGG SGDGALLNVT DGQGLSATAT
GETRVPVTTA LEVENGSMPT GSPTLAMFTQ SFREVDMLDL ENLTTASGDG EVPTSTDVDT
EAGTLPTGGP TLKPREEATL GSLGEEWSTT VVSKVPLNAF EEEEASGTAI DSLDAFTPTV
VLEQASGTPT DIQAALTTTV APEQVFTAAP TDGEDLVTST EESDEEGSGS TLPIGPPLSK
PTVTPERQVT LAGVEAEGSD PVWGVDVGSG SGDIVGNEDL LRGPPGPPGP PGSPGIPGKP
GTDVFVGPPG SPGEDGAPGE PGPQGPEGQP GLDGASGQPG MKGEKGARGP NGSVGEKGDP
GSRGLPGPPG KNGEVGIPGA MGPPGPPGPP GPPGPGCTTK LGFEGPKGEK GEQGAKGERG
TDGISTMGPP GPRGPPGRVE VLSSSLINIT NGSMNFSDIP ELMGPPGPDG VPGLPGFPGP
RGPKGDTGVP GFPGLKGEQG EKGEPGAILT GDIPLEMVKG RKGEPGVHGA PGPMGPKGPP
GHKGEFGLPG RPGRPGLNGL KGAKGDRGIM LPGPPGLPGP PGPPGPPGAV VNIKGAVFPI
PARPHCKTPV GTAHPGDPEL VTFHGVKGEK GSWGLPGTKG EKGDQGAQGP PGPPVDPAYL
RHFLNSLKGE NGDAAFRGES SHNLFVSGPP GLPGHPGLAG QKGEAVVGPQ GPPGIPGLPG
PPGFGRPGVP GPPGPPGPPG PPAILGAAVP LPGPPGPPGQ PGLPGSRNLV TALSDMGDML
QKAHLVIEGT FIYLRESGEF FLRVRDGWKK LQLGELIPIP ADSPPPPALS SNPYQPQPPL
NPILSANYER PVLHLVALNT PVAGDIRADF QCFQQARAAG LLSTFRAFLS SHLQDLSTVV
RKAERFSLPI VNLKGQVLFN NWDSIFSGDG GQFNTHIPIY SFDGRDVMTD PSWPQKVVWH
GSNPHGVRLV DKYCEAWRTT DMAVTGFASP LSTGKILDQK AYSCANRLIV LCIENSFMTD
ARK
//
