ID G5AZ16_HETGA Unreviewed; 1256 AA.
AC G5AZ16;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 28-JAN-2026, entry version 56.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN ORFNames=GW7_05033 {ECO:0000313|EMBL:EHB02286.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB02286.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB02286.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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; JH167586; EHB02286.1; -; Genomic_DNA.
DR AlphaFoldDB; G5AZ16; -.
DR FunCoup; G5AZ16; 218.
DR STRING; 10181.G5AZ16; -.
DR eggNOG; KOG3546; Eukaryota.
DR InParanoid; G5AZ16; -.
DR Proteomes; UP000006813; 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 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; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF891; COLLAGEN ALPHA-1(XVII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 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:EHB02286.1};
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1..133
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 182..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..501
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..528
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..602
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..975
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1256 AA; 128804 MW; 9B55EC402480B292 CRC64;
MAKPSSTRGG VLFAVTDAFQ KVIYLGLRLS GVQDGHQRVI LYYTEPGSHL SHEAAVFSVP
VMTNRWNHFA VIIQGEEVTL LMDCEEHSHV LFQRSSQPLT FEPSTGIFVG SAGATGLDKF
TGSIQQLTIH ADPRVPEELC EAQELSASGE GSGLQETDTV AETLEAITYT QALPKEAKVE
PINIPPISSS PPPLEDMELS GEPVPEGTPE TNLSISQHNS PEQGKCIPGS GEILNDTLEQ
VHSLDGDAIS DVGSGDRTFL GATEEQGSAA TAIGEDEVTI TTAREAEVSS VPTGGPTLVM
STLNPREGTA PPEVPVSTAG EVESGSVSTV GPTLTMSTQS PREETTLGPG KEWLTSVAAP
TEVPLSTPGE EEASGASTDN LAVLTPTVAP AHASRASTDG LAVLTPTVAL RQVVTSVPDD
KEDLEPLATA GREETGSAPP DGLPLPVPTA APEGRVTLVG TEAVGSGLGW ALDIGSGSGD
LVDQEEFLRG PPGPPGPPGL PGIPGKPGTD VLMGPPGSPG EDGAAGEPGL PGPEGEPGLD
GAVGRPGMKG EKGARGPNGS VGEKGDPGNR GLPGPPGKNG QAGTPGVTGP PGPPGPPGPP
GPGCATGLEF EDTEGSGNIR LLNEPRISRP TVSSGLKGDK GDQGPKGERG LDGISTVGPP
GPRGPPGRIE ILSSSLVNIT HGSLNFSNIP ELLGPPGPDG VPGLPGFPGP RGPKGDTGLP
GFPGLKGEQG EKGEPGAILT GDVPLERLKG KKGEPGLHGA PGPMGPKGPP GHKGEFGLPG
RPGRPGLNGI KGAKGDRGIM MQGPPGLPGP PGPPGPPGAV VNIKGAVFPV PVRPHCKMPL
GTTQPGDPEL ITFHGVKGEK GSWGLPGSKG EKGDQGAQGP PGPPVDPAYL RHFLNSLKGE
NGDRGFKGEK GDSNGNFFVA GSPGLPGNPG LAGQKGETII GPQGPPGIPG LPGPPGFGRP
GAPGPPGPPG PPGPPAILGA AVALPGPPGP PGQPGLPGSR NLVTAFSSMD DMLQKAHLVI
EGTFIYLRDS TEFFIRVRDG WRKLQLGELI PIPADSPPPP ALSSNSYQLQ PPLNPILSAN
YENPVLHLVA LNMPFSGDIR ADFQCFQQAR AAGLLSTFRA FLSSHLQDLS TVVRKAERYS
LPIVNLKGQV LFNNWDSIFS GDGGQFNTHV PIYSFDGRDV LTDPSWPQKV VWHGSTTHGV
RLVDKYCEAW RTADMAVTGF ASPLNTGKIL DQKAYNCANR LIVLCIENSF MTDARK
//
