ID K7GJW5_PELSI Unreviewed; 1289 AA.
AC K7GJW5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 28-JAN-2026, entry version 72.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000020576.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000020576.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSPSIP00000020576.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 EMBL; AGCU01019129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01019130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01019131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01019132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01019133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01019134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01019135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01019136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01019137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01019138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 13735.ENSPSIP00000020576; -.
DR Ensembl; ENSPSIT00000020673.1; ENSPSIP00000020576.1; ENSPSIG00000018207.1.
DR eggNOG; KOG3544; Eukaryota.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000164061; -.
DR HOGENOM; CLU_004003_1_0_1; -.
DR OMA; RATEDQC; -.
DR Proteomes; UP000007267; 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: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; 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:UP000007267};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1289
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003903167"
FT DOMAIN 38..226
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 87..225
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 226..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..484
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..517
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..571
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..977
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..990
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1010
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1028
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1289 AA; 132842 MW; A49DB0831BEDB03F CRC64;
MLSRHCWWPW NLLLLFWGSF LPVVLTAQVI EERRSKGHLD LTELIGVPLP PSVSFITGYG
GFPAYSFGPN ANIGRLTKTL IPQTFYRDFA IVVTVKPNSD DGGVLFAITD AFQKTIYLGM
RLSPVDDSTQ RIIIYYTEPR SSISREAASF KVPVMTNKWN RFTVTVQGND IVLFMDCEEY
NRVQFRRSAK ALQFESSSGI FVGNAGATGL EKFTGSIQQL MIKPDPRATE DQCEDDDPYA
SGDSSGAGSI QEQEGILETQ EVIASSPPLP AEITAEPVEA PPTVSAQLEE IDFSGHHISD
ETSESPTIKK QGNDQHERDT TTIAQEILKQ ETGSGAIILQ GEREVQGQKG DRGEKGEQGP
PGPPGPPGKS GLEDMQTGIQ GTLGPPGSPG KPGRDGEPGI PGKDGLPGER GLQGLPGLKG
EDGLKGEKGE PGVGLPGLPG PPGLSAPFRG PSRLEPEGSG SGDLDRDNEI LRGLPGPPGP
PGLPGAPGKP GSNAEPPGSP GKDGPSGEPG PPGPQGPPGL DGMVGPPGKK GEKGDQGLPG
AAGPKGDAGD IGSPGPKGQA GDDGQPGKPG LQGPPGPPGP GYGFGFEDME GSGDISLLSE
PRFPGSRMPN GPVGETGQRG PMGPKGEKGD TGPPGLAGLK GAQGADGKPG FPGVAGRPGD
AGLKGEKGDM GPKGEPGQDG ASIVGPPGPP GPPGPIVAVS QLLLNDTDGV SNFTGIKGLV
GPPGPDGRPG LPGFPGPKGP KGDIGLTGLQ GPKGQRGEKG EPGAIISADG SLRELVGRQG
QKGDRGIIGP PGPMGPEGPS GSKGELGIPG RPGRPGLNGL KGVKGERGVT LYGLPGLPGP
PGPPGPPGAI IYIKGTVFPI SPRPYCKMPV GTAHPGNQDA NIHGMKGELG AWGPLGPPGL
KGEKGEQGSP GLPGPSLPSS YFSHFVNSMK GEKGDNGETG FKGEKGEPSG GFFMSGPPGP
PGRPGLVGPK GDSIVGPRGP PGLPGLPGPP GYGIVGPPGP PGPPGPPGPP SIYGSAAFPG
PPGPPGEPGL PGARNLVTTF RNIDSMLQKV HLVAEGTLIY LSESSEVFIR VRGGWRRLQL
GELIPIPADS PPPPAISGYG FQPLPALRPV STIRKPTLHL VALNLPFSGA VRADYQCFQQ
ARATGLTSTY RAFLSSHLQD LATVVRKTDR YNLPIVNLKG EVLFNNWESV FSGSGGQFNI
QIPIYSFDGR NVMTDPSWPQ KVIWHGSTAN GIRLVNNYCE AWRTADMTVM GQASALTTGK
LLDQKPYSCN NKFIVLCIEN SFVSDIQRK
//
