ID A0A8B8XXJ0_BALMU Unreviewed; 1302 AA.
AC A0A8B8XXJ0;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN Name=COL15A1 {ECO:0000313|RefSeq:XP_036712034.1,
GN ECO:0000313|RefSeq:XP_036712035.1};
OS Balaenoptera musculus (Blue whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=9771 {ECO:0000313|Proteomes:UP000694857, ECO:0000313|RefSeq:XP_036712035.1};
RN [1] {ECO:0000313|RefSeq:XP_036712034.1, ECO:0000313|RefSeq:XP_036712035.1}
RP IDENTIFICATION.
RC TISSUE=Epidermis and Blubber {ECO:0000313|RefSeq:XP_036712034.1,
RC ECO:0000313|RefSeq:XP_036712035.1};
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}.
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 RefSeq; XP_036712034.1; XM_036856139.1.
DR RefSeq; XP_036712035.1; XM_036856140.1.
DR GeneID; 118897191; -.
DR CTD; 1306; -.
DR Proteomes; UP000694857; Chromosome 6.
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: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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 1.
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_036712034.1};
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:UP000694857};
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..1302
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044668150"
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 222..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..658
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..837
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..863
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..978
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1021
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1040
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1302 AA; 133244 MW; 35EE8A47CF397366 CRC64;
MAQRRDTQCW RLLWLLSISA LLPAVTRTRS ATELASQGHL DLTELIGVPL PSSVSFVTGY
GGFPAYSFGP GANVGRPART LIPPTFFRDF AISVMAKPSS ARGGVLFAIT DAFQKVIYLG
LRLSGVEDGN QRVILYYTEP GSKVSREAAA FPVPVMTHRW NRFAMVVQGE EVTLLVDCEE
HSHVPFPRSS RALAFEPSAG IFVGNAGATG LERFTGSIQQ LTIHPDPRTP EELCEAEESS
ASGEASGLQE TERVAEILEA ITYTQAPSRE ARVGPINTPP TLSSPSEDAE LSGEPVPERA
QETTNMSAVP HSSPKQGSGE ILNDTLETVD TVDASPITDT GSADGAFLHV IEEGPDNEEG
SAGTAAREAE VPVSGAGEAE ASSVPTGGLT LSMPTQDPGE GVTLGPISEE SLTIAAAAAK
VPLSTFEEEE ASGFPTDGLV PLTPTAAPKQ VVTSGPGDED LAAATTEQPL PAAGAEELGG
ALPEAPPLPI PTVAPERGVP PGEAGEGLPG PLGPAGPTVG VEAEGSSLGW GLDVGSGDPV
RSEELLRGPP GPPGPPGLPG IPGKPGTDVF TGPPGSPGED GPAGEPGPPG PEGKPGLDGA
SGLPGMKGEK GARGPNGSVG EKGDPGNRGL PGPPGKNGQV GAPGVMGPPG PPGPPGPQGP
GCAMGLGFED TEGSGGIRLL PEPGISGPTA SSGPKGEKGD QGPKGERGMD GASVVGPPGP
RGLPGRIEVL SSPLINITHG FMNLSDIPEL VGPPGPRGPK GDTGVPGFPG LKGEQGEKGE
PGAILTGDIP LERLRSQKGE SGERGAPGPM GPRGPPGHKG EFGLPGRPGR PGLNGLKGTK
GDRGIMMPGP PGLPGPPGPP GPPGAVINIK GAVFPVPVRP HCKTPVGTTY PGNSELITFH
GVKGEKGSWG LPGSKGEKGD QGAQGPPGPP VDPTYLRHFL NSLKGENRDR GIKGEKGDSD
SGFSESGPPG LPGSPGLAGQ KGETIVGPQG PPGAPGMPGP PGFGRPGSPG PPGPPGPPGP
PAILGAAVAI PGPPGPPGQP GLPGSRNLVT AFSSMADMLQ KAHLVIEGTF IYLRDSTEFF
IRVRDGWKKL QLGELIPIPD DSPPPPALSS NSHQLQLPLT SVSSVNYDSP ALHLVALNTP
FSGAIRADFQ CFQQARAAGL LSTYEAFLSS HLQDLSTVVR KEERYNLPIV NLKGQVLFNN
WDSIFSGHGG QFNTHVPIYS FDGRDVMTDP SWPQKVVWHG SSTHGVRLVD QYCEAWRTAD
MAVMGLASPL STGKILDQKA YSCANRLIVL CIENSFMTDV RK
//
