ID A0A452HIR9_9SAUR Unreviewed; 1384 AA.
AC A0A452HIR9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=Collagen type XV alpha 1 chain {ECO:0008006|Google:ProtNLM};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000014804.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000014804.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGAGP00000014804.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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 STRING; 38772.ENSGAGP00000014804; -.
DR Ensembl; ENSGAGT00000016916.1; ENSGAGP00000014804.1; ENSGAGG00000011213.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
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; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 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:SF1034; COLLAGEN ALPHA-1(XVIII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 5.
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 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:UP000291020};
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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1384
FT /note="Collagen type XV alpha 1 chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019167700"
FT DOMAIN 119..307
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 168..306
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 307..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..533
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..582
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..669
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..910
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1036
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..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 1384 AA; 141781 MW; 067A476AFAF44E9D CRC64;
MFSKLAWIIF VMQSGFIEGQ WWWQWLWGTT QTTTPPVATA VNTIALNIRT TVSARAPAGS
ITSTASSGAT GVSYESTLPG GAAVTNFSRE KALSGLELKT GKKISQGKHK KTERGSKGHL
DLTELIGVPL PLSVSFITGY GGFPAYSFGP DANIGRLTST LIPLTFYNDF AIIVTVKPNS
DDGGVLFAIT DAFQKTIYLG MRLSPVDDGT QRIIMYYTEP GSYISREAAS FKVPVMTNKW
NRFTVTVQGN DTVLFMDCEE YNRVQFQRSS QALQFGSNSG IFVGNAGATG LEKFTGSIQQ
LMIKPDPRAT EDQCEDDDPY ASGDSSGTGS IQELEGLPET EEVIASSQPL PEETTAGPVG
APPTISAQSE EMDFSGHHIL DETPEPPTIK EQGSTSAGND QHESDATTVA QEILKSETGS
GAIVLQGVSR EKGQKGERGE KGEQGPQGPP GPPGKSKLEK MQTGIQGPPG PLGKPGRDGE
PGIPGKDGLP GERGLQGLPG LKGEDGLKGE KGEPGVGLPG PQGLPGPPGP PAPFRGLSRL
EPEGSGSGDL DRDREVLRGL PGPPGPPGLP GAPGKPDSNS GPPGSPGKDG KDGPSGEPGP
PGPQGHPGLD GMVGPPGKKG EKGDQGLPGA VGPKGDAGDI GSPGPEGQAG ADGQPGKPGP
QGPPGPPGPG YGFGFEDMEG SGSISLLSEP RIPGSRGPNG PAGETGQRGP MGPKGEKGDT
GPPGIAGLKG EQGADGKPGF PGVAGRPGDA GPKGDKGDTG SKGEPGQDGA SIVGPPGPPG
PPGPIIAVPQ LLLNDTDGIS NFTGVKGLLG PPGPDGRPGL PGFPGPRGPK GAIGLTGLQG
PKGQRGEKGE PGFIISANGS LRELTGRQGQ KGERGAMGPP GPMGPVGPSG PKGELGIPGR
PGRPGLNGLK GVKGERGVTL YGPPGLPGPP GPPGPPGAVI HIKGTVFPIS PRPHCKMPVG
TAHPGNQEAN IYGMKGEPGS WGLHGPPGLK GEKGERGSPG LPGAPLPSAY FSHLVNSMKG
EKGDNGETGF KGEKGEPSGG FFMSGPPGPP GLPGRPGLVG PKGDSIVGPR GPPGLPGLPG
SPGYGIVGPP GPPGPPGPPG PPAIYGSAAA VPGPPGPPGE PGLPGTRNLV TTFRNIDGML
RKVHLVAEGT LIYLSESSEV FIRVRGGWRR LQLGELIPIP ADSPPPPAIS GYGFQSLPAL
RPVSAINHGK PTLHLVALNL PLSGAMRADY QCFQQARAAG LMSTYRAFLS SHLQDLSTVV
RKSDRFNLPI VNLKGEILFN NWESVFTGSG GQFNIQIPIY SFDGRNIMTD PSWPHKIIWH
GSTANGSRLV SNYCEAWRTA DMTVMGQASP LTTGKLLDQK PYSCSNKFIV LCIENSFVSD
IRRK
//
