ID A0A452HIS3_9SAUR Unreviewed; 1370 AA.
AC A0A452HIS3;
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:ENSGAGP00000014807.1, 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:ENSGAGP00000014807.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGAGP00000014807.1}
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 Ensembl; ENSGAGT00000016919.1; ENSGAGP00000014807.1; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 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..1370
FT /note="Collagen type XV alpha 1 chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019562798"
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..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1112
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 1005..1022
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1088
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1107
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1370 AA; 140189 MW; 511E692AD0B916B3 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 HIKGVGTAHP GNQEANIYGM
KGEPGSWGLH GPPGLKGEKG ERGSPGLPGA PLPSAYFSHL VNSMKGEKGD NGETGFKGEK
GEPSGGFFMS GPPGPPGLPG RPGLVGPKGD SIVGPRGPPG LPGLPGSPGY GIVGPPGPPG
PPGPPGPPAI YGSAAAVPGP PGPPGEPGLP GTRNLVTTFR NIDGMLRKVH LVAEGTLIYL
SESSEVFIRV RGGWRRLQLG ELIPIPADSP PPPAISGYGF QSLPALRPVS AINHGKPTLH
LVALNLPLSG AMRADYQCFQ QARAAGLMST YRAFLSSHLQ DLSTVVRKSD RFNLPIVNLK
GEILFNNWES VFTGSGGQFN IQIPIYSFDG RNIMTDPSWP HKIIWHGSTA NGSRLVSNYC
EAWRTADMTV MGQASPLTTG KLLDQKPYSC SNKFIVLCIE NSFVSDIRRK
//
