ID A0A8I5UHB4_PONAB Unreviewed; 1339 AA.
AC A0A8I5UHB4;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 19.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000045210.1, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000045210.1, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000045210.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000045210.1}
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; ENSPPYT00000041795.1; ENSPPYP00000045210.1; ENSPPYG00000011521.3.
DR GeneTree; ENSGT00940000158212; -.
DR Proteomes; UP000001595; Chromosome 21.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-ARBA.
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; 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; 4.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
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:UP000001595};
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..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1339
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035195649"
FT DOMAIN 41..229
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 230..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..395
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..431
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..459
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..499
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..527
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..606
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..650
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..711
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..738
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..853
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..881
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..953
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..999
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1021
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1136
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1339 AA; 136153 MW; DB2634D4786D3DA0 CRC64;
MAPRCPWLWP RRRRLLDVLA PLVLLLGVRA ASAEPERVSE EVGLLQLLGD PPPQQVTQTD
DPDVGLAYVF GPDANSGQVA RYHFPSLFFR DFSLLFHIRP ATEGPGVLFA ITDSAQAVVL
LGVKLSGVQD GHQDISLLYT EPGAGQTHTA ASFRLPAFVG QWTHLALSVE GGYVTLYVDC
EEFQRMLLAR SSRGLELEPG AGLFVAQAGG ADPDKFQGMI AELKVRGDPQ VSPMHCLDEE
GDDSDGASGD FGSGLGDARE LLREETGAAL KPRLPMPPPV TTPPLAGGSS TEDSRSKEIE
EQTTVASLGG QTLPGSDSVS TWDGSVRTPG DRVREGGLKG QKGEPGVPGP PGRAGPPGSP
CLPGPPGLPC PVSPLGPAGP ALQPVPGPQG PPGPPGRDGT PGRDGEPGDP GEDGKPGDTG
PQGFPGTPGD VGPKGDKGDP GVGERGPPGP QGPPGPPGPS FRHDKLTFID MEGSGFGGDL
EALRGPRGFP GPPGPPGVPG LPGEPGLFGV NSSDVPGPAG LPGVPGREGP PGFPGLPGPP
GPPGREGPPG RTGQKGSLGE AGAPGHKGSK GDPGPAGARG ESGLAGSPGP AGPPGPPGPP
GPPGPGLPAG FDDMEGSGGP FWSTARSADG PQGPPGLPGL KGDPGMPGLP GAKGEVGADG
APGFPGLPGR EGIAGPQGPK GDRGSQGEKG DPGKDGVGQP GLPGPPGPPG PVVYVSEQDG
SVLSVPGPEG RPGFAGFPGP AGPKGDLGSK GERGSPGPKG EKGEPGSIFR PDGGALGPVQ
KGAKGEPGFR GPPGPYGRPG YKGEIGFPGR PGRPGMNGLK GEKGEPGDAS LGFGMRGMPG
PPGPPGPPGP PGTPVYDSNV FAESSRPGPP GLPGNQGPPG PKGAKGEVGP PGPPGQFPFD
FLQLEAEMKG EKGDRGDAGQ KGERGEPGGG GFFGSRLPGP PGPPGPPGYP GIPGPKGESI
RGQPGPPGPQ GPPGIGYEGR QGPPGPPGPP GPPGPPSFPG PHRQTISVPG PPGPPGPPGP
PGTVGASSGV RLWATRQAML GQVHEVPEGW LIFVAEQEEL YVRVRNGFRK VQLEARTPLP
RGTDNEVAAL QPPVVQLHDS NPYPRREHPH PTARPWRADD ILASPPRLPE PQPYPGAPHH
SSYVHLRPAR PTSPPAHTHR DFQPVLHLVA LNSPLSGSMR GIRGADFQCF QQARAVGLAG
TFRAFLSSRL QDLYSIVRRA DRAAVPIVNL KDELLFPSWE ALFSGSEGPL KPGARIFSFD
GKDVLRHPTW PQKSVWHGSD PNGRRLTESY CETWRTEAPS ATGQASSLLG GRLLGQNAAS
CHHAYIVLCI ENSFMTASK
//
