ID A0A8C6HT00_MUSSI Unreviewed; 1345 AA.
AC A0A8C6HT00;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 21.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
OS Mus spicilegus (Mound-building mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10103 {ECO:0000313|Ensembl:ENSMSIP00000025451.1, ECO:0000313|Proteomes:UP000694415};
RN [1] {ECO:0000313|Ensembl:ENSMSIP00000025451.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSMSIP00000025451.1}
RP IDENTIFICATION.
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 Ensembl; ENSMSIT00000032123.1; ENSMSIP00000025451.1; ENSMSIG00000021093.1.
DR GeneTree; ENSGT00940000158302; -.
DR Proteomes; UP000694415; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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; 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 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:UP000694415};
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..1345
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034469054"
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 267..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..447
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..564
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..595
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..616
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..717
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..907
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1345 AA; 138496 MW; 2DE1DA48485103A2 CRC64;
MTHRRTAQGR RPRWLLSIIS ALLSAVLQTR AATGSASQVH LDLTVLIGVP LPSSVSFTTG
YGGFPAYSFG PGANVGRPAR TLIPPTFFRD FAIGVAVKPN SAQGGVLFAI TDAFQKVIYL
GLRLSSVEDG RQRVILYYTE PGSHVSREAA VFSVPVMTNR WNRFAVTVQG EEVALFMDCE
EQSQVRFQRS SWPLTFEPSA GIFVGNAGAM GLERFTGSIQ QLTIYSDPRT PEELCEAQES
SASGEASGFQ EMDEVAEIME AVTYTQAPPK ESHVDPISVP PTSSSPAEDS ELSGEPVPEG
TPETNLSIIG HSSPEQGSGE ILNDTLEVHA MDGDPGTDDG SGDGALLNIT DGQGLSATAT
GEARVPVTTV LEAENGSMPT GSPTLTMFTQ SIREVDTPDP ENLTTTASGD GEVPTSTDGD
TEADSSPSGG PTLKPREETT LGSHGEEWLT PAVSKMPLKA FEEEEASGTA IDSLDVVFTP
TVVLEQVSRR PTDIQATLTP TVVLEETSGP PTDTQDALTP TVAPEQMFTA EPTDGGDLVA
STEEAEEEGS GSMPPSGPPL PTPTVTPKRQ VTLVEVEAEG PGPVGGLDEG SGSGDIVGNE
DLLRGPPGPP GPPGSPGIPG KPGTDVFMGP PGSPGEDGAP GEPGPQGPEG QPGLDGASGQ
QGMKGEKGAR GPNGSAGEKG DPGNRGLPGP PGKNGEVGTP GVMGPPGPPG PPGPPGPGCT
TELGFEGPKG EKGEQGAKGE RGADGTSTMG PPGPRGPPGH VEVLSSSLIN ITNGSMNFSD
IPELMGPPGP DGVPGLPGFP GPRGPKGDTG VPGFPGLKGE QGEKGEPGAI LTGDIPLEMM
KGRKGEPGIH GAPGPMGPKG PPGHKGEFGL PGRPGRPGLN GLKGAKGDRG VTLPGPPGLP
GPPGPPGPPG AVVNIKGAVF PIPARPHCKT PVGTAHPGDP ELVTFHGVKG EKGSWGLPGS
KGEKGDQGAQ GPPGPPVDPA YLRHFLNNLK GENEDASFRG ESSNNLFVSG PPGLPGHPGL
VGQKGEAVVG PQGPPGIPGL PGPPGFGRPG VPGPPGPPGP PGPPAILGAA VALPGPPGPP
GQPGLPGSRN LVTALSDMGD MLQKAHLVIE GTFIYLRDSG EFFIRVRDGW KKLQLGELIP
IPADSPPPPA LSSNPYQPQP PLNPILSANY ERPVLHLVAL NTPVAGDIRA DFQCFQQARA
AGLLSTFRAF LSSHLQDLST VVRKAERFGL PIVNLKGQVL FNNWDSIFSG DGGQFNTHIP
IYSFDGRDVM TDPSWPQKVV WHGSNPHGVR LVDKYCEAWR TTDMAVTGFA SPLSTGKILD
QKAYSCANRL IVLCIENSFM TDTRK
//
