ID M3Y5J2_MUSPF Unreviewed; 1381 AA.
AC M3Y5J2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 28-JAN-2026, entry version 71.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|Ensembl:ENSMPUP00000006593.1,
GN ECO:0000313|RefSeq:XP_044937557.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000006593.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000006593.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2024) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_044937557.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_044937557.1};
RG RefSeq;
RL Submitted (APR-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}.
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DR EMBL; AEYP01022390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01022391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01022392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01022393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_044937557.1; XM_045081622.1.
DR STRING; 9669.ENSMPUP00000006593; -.
DR Ensembl; ENSMPUT00000006706.1; ENSMPUP00000006593.1; ENSMPUG00000006647.1.
DR GeneID; 101691009; -.
DR KEGG; mpuf:101691009; -.
DR CTD; 1306; -.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000158302; -.
DR HOGENOM; CLU_004003_0_0_1; -.
DR OMA; RATEDQC; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
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 CDD; cd00110; LamG; 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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 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 ECO:0000313|RefSeq:XP_044937557.1};
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:UP000000715};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1381
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044735937"
FT DOMAIN 39..227
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 88..226
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 266..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..444
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..605
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..628
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..729
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..838
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..884
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..918
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1059
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1070..1102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1112..1121
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1381 AA; 140142 MW; DFCAB775223D1DEE CRC64;
MAPRRNARCW RLLLLLSISA LLPAVSRTRS ATELASQGHL DLTELIGVPL PSSVSFVTGY
GGFPAYSFGP GANVGRPART LIPPTFIRDF AISVTVKPSS DNGGVLFAIT DAFQKIIYLG
LRLSGIEDGR QRVILYYTEP GSHVSHEAAA FPVPVMTHRW NRFSVIIQGE EVALLMDCEE
QGHILFQRSS RPLAFEPSAG IFVGNAGATG LERFTGSIQQ LTIHPDPRIP EELCESEESS
ASGEASGLQE TEGVAEILEA VTYTQAPSKE AEVEPINTPP TPSPPSDDAE LSGEPVPEGT
PETANLSITE HSSLEQGSGE VLNDTLEGVH TMDGAPVTDG VPITDGVPVT DVGSGGGAFI
HVTEESVRAE EGLAATAAVG EAELPPSPTG EAEASSVPTG GPALSLSTED TGEGVTLGVD
ADAEEGSAAP AAGEAGSTTG EVEASSVPAG GVTSPMPIQD AGEGITWGAT REAMFTTPAA
AAEVTPSTSE EEETRGFPTG GLAPPTPTVA PEQAVASGSG EEEDLAAAAT GEPLPGTVAE
ELDGSPPEGP PLSIPTVASE RGVTLAEAGE GLPGHPEPAR PTGPTVGAET EGSGLGWGSD
VGSGSGDLVR SEELLRGPPG PPGPPGSPGI PGKPGTDVFM GPPGSPGEDG AAGEPGPPGP
EGQPGADGAS GLPGMKGEKG ARGPNGSVGE KGDPGNRGLP GPPGKNGQVG SPGVMGPPGP
PGPPGPPGPG CTAGLGLEDP EGSGSIRLLH EPGLSGPVAP SGPKGEKGDQ GPKGERGMDG
ASIVGPPGPR GPPGRIEVLS SSLTNITHGF MNLSDVPELA GPPGPEGIPG LPGFPGPRGP
KGDTGVPGFP GLKGEQGEKG EPGAILTGDI PLERLQGKKG EPGEHGAPGP MGPKGPPGHK
GEFGLPGRPG RPGLNGLKGA KGDRGIMMPG PPGLPGPPGP PGPPGAVVNI KGAVFPIPVR
PHCKTPVDIS HPGNSELITF HGVKGEKGSW GLPGSKGEKG DQGAQGPPGP PVDPAYLRHF
LNSLKGENGD QGIKGEKGDS HSDFSVSGPP GLPGSPGLVG QKGESVIGPQ GPPGAPGLPG
PPGFGRPGPP GPPGPPGPPG PPAILGAAVA LPGPPGPPGQ PGLPGSRNLV TAFSTMDDML
QSAHLVIEGT FIYLRDSTEF FIRVRDGWKK LQLGELIPIP ADSPPPPALS SNPHLPPLMP
LSSVSYDRPV LHLVALNTPF SGDFRADFQC FQQARAAGLL STYRAFLSSH LQDLSTVVRK
AERYSLPIVN LRGQVLFNNW DTIFSGHGGQ FNTHIPIYSF DGRDVMTDPS WPQKVIWHGS
SPHGVRLVDN YCEAWRTADM AVTGLASPLS TGKILDQKTY SCANRLIVLC IENSFMTDAR
K
//
