ID A0A5N4EAT8_CAMDR Unreviewed; 1282 AA.
AC A0A5N4EAT8;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 08-OCT-2025, entry version 20.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN ORFNames=Cadr_000015927 {ECO:0000313|EMBL:KAB1280146.1};
OS Camelus dromedarius (Dromedary) (Arabian camel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=9838 {ECO:0000313|EMBL:KAB1280146.1, ECO:0000313|Proteomes:UP000299084};
RN [1] {ECO:0000313|EMBL:KAB1280146.1, ECO:0000313|Proteomes:UP000299084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Drom800 {ECO:0000313|EMBL:KAB1280146.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAB1280146.1};
RX PubMed=30972949; DOI=.1111/1755-0998.13020;
RA Elbers J.P., Rogers M.F., Perelman P.L., Proskuryakova A.A.,
RA Serdyukova N.A., Johnson W.E., Horin P., Corander J., Murphy D.,
RA Burger P.A.;
RT "Improving Illumina assemblies with Hi-C and long reads: an example with
RT the North African dromedary.";
RL Mol. Ecol. Resour. 19:1015-1026(2019).
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:KAB1280146.1}.
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DR EMBL; JWIN03000004; KAB1280146.1; -; Genomic_DNA.
DR STRING; 9838.ENSCDRP00005022669; -.
DR Proteomes; UP000299084; 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: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; 2.
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, ECO:0000313|EMBL:KAB1280146.1};
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:UP000299084};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 14..202
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 63..201
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 329..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..381
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..835
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..952
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..1001
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1020
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1282 AA; 134322 MW; 3AD08051B2656E74 CRC64;
MEETPPDELA SQGHLDLTEL IGVPLPSSVS FVTGYGGFPA YSFGPGANVG RPARTLIPRT
FFRDFAISVT VKPSSAQGGV LFAITDAFQK VIYLGLRLSG VQDGHQRVIL YYTEPGSQVS
HEAAAFPVPV MTHRWNRFAV VVQGEEVTLL VDCKEHSHVP FPRSSRALTF EPSAGIFVGN
AGATGLERFT GAIQQLTVHR NPRTPEMLCE AEDSSASGET SGLQETDEVA EILEAVTFTQ
APYNLLVACL NLNSPNPCSH WHQGSGEILN DTLERVHTVD GVLVTDTGSG DRGFPDVIEE
GSPTEEGLTA TAAAEVPIST AREAEVDIVP TGGPKLSTST EDSGEGVTLG PDDEEGSAAT
VAGEAEVPVS SAGEAEASSE PTRGLTLSMS IQDPGEGVTL GKSLVTVSFQ GQISEEGLTT
AAAAAEVPLI PFEEEEASGV PTDGLAPLTP TAAPEQAITS GPGDEDSVAV ATEEPFMASG
AEELGGAPPE GPLLPVPTVA PERGVPLGTR KHQDRISPRV KLRRGFLVSL DLLGPLDPRV
PQAPRAHLAY LGFQENQEPM FSLDPLDLLE RMDLLVNPVP REKEDLMAQL VKRVIPATEA
YQDPLGKTDK LALLGSGDPQ GLLDPLGPQA LDVQRDLDLR ILKALEASGC CMNPESLDQR
LQVYGPKGEK GDQGPKGDRG MDGASIVGPP GPRGPPGRIE VLSSSLVNIT HGFMNLSDIP
ELVGPPVCIH RCPRGPEGMP GLPGFPGPRG PKGDTGVPGF PGLKGEQGEK GEPGAILMGD
VPLERLRGKK GEPGAHGAPG PMGRPGLNGL KGSKGDRGVM MPGPPGLPGP PGPPGPPGAV
INIKGAIFPI PVRPHCKTLV GTTHPGNSEL ITFHGVKGEK GSWGLPGSKG EKGVQGAQGP
PGPPVDPTYL RHFLNSLKWE NEDREFKGVK GDSNSGFSVS GPPGLPGSPG LVGQKGETVV
GPQGPPGVPG LPGPPGFGRP GSPGPPGPPG PPGPPGPPGP PAILGAAVAL PGPPGPPGQP
GLPGTRNLVT ALSNMDDMLQ KAHLVIEGTF IYLRDSTEFF IRVRDGWKKL QLGELIPIPD
DSPPPPALSS NPRQPQLPLM SVSSVSYGRP ALHLVALNTP FSGDIRADFQ CFQQARAAGL
LSTYRAFLSS HLQDLSTVVR KAERYSLPIV NLKGQVLFNS WESIFSGNGG QFNTHIPIYS
FDGRDVMTDP SWPQKVVWHG SSTHGVRLVD QYCEAWRTAD MAVTGLASAL STGKILDQKA
YSCANRLIVL CIENSFMTDA RK
//
