ID A0A2R8ZKW1_PANPA Unreviewed; 1369 AA.
AC A0A2R8ZKW1;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 28-JAN-2026, entry version 31.
DE RecName: Full=Thrombospondin-like N-terminal domain-containing protein {ECO:0000259|SMART:SM00210};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000003376.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000003376.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000003376.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSPPAP00000003376.1}
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 EMBL; AJFE02084006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02084007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02084008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02084009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02084010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02084011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02084012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02084013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPPAT00000015529.1; ENSPPAP00000003376.1; ENSPPAG00000014049.1.
DR GeneTree; ENSGT00940000158212; -.
DR OMA; VQDQHQN; -.
DR Proteomes; UP000240080; Chromosome 21.
DR Bgee; ENSPPAG00000014049; Expressed in liver and 6 other cell types or tissues.
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: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; IPR010363; DUF959_COL18_N.
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; 1.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06121; DUF959; 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:UP000240080};
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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1369
FT /note="Thrombospondin-like N-terminal domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015305485"
FT DOMAIN 221..409
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 40..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..635
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..675
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..701
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..845
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1058
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1369 AA; 141200 MW; AC42B9232B738838 CRC64;
MAPYPCGCHI LLLLFCCLAA ARADLLNLNW LWFSNEDTSH TATTIPEPQG PLPVQPTADT
TTHVTPRNGS TEPATAPGSP EPPSELLEDG QETPTSAESP DAPEENIAGV GAEILNVAKG
IRSFVQLWND TVPTESLARA ETLVLETPVG PLALAGPSST PQENGTTLWP SRGIPSSLGA
HTTEAGTLPA PTPSPPSLGR PWAPLTGPSV PPPSSERVSE EVGLLQLLGD PPPQQVTQTD
DPDVGLAYVF GPDANSGQVA RYHFPSLFFR DFSLLFHIRP ATEGPGVLFA ITDSAQAVVL
LGVKLSGVQD GHQDISLLYT EPGAGQTHTA ASFRLPAFVG QWTHLALSVA GGFVALYVDC
EEFQRMPLAR SSRGLELEPG AGLFVAQAGG ADPDKFQGVI AELKVRRDPQ VSPMHCLDEE
GDDSDGASGD SGSGLGDARE LLREETGAAL KPRLPTPPPV TTPPLAGGSS TEDSRSEEIE
EQTTVASLGA QTLPGSDSVS TWDGSVRTPG GRVKEGGLKG QKGEPGVPGP PGQAGPPGSP
CLPGPPGLPC PVSPLGPAGP ALQPVPGPQG PPGPPGRDGT PGRDGEPVSP HAPPSPWGLC
ACPGHDGLVL CSQGDPGVGE RGPPGPQGPP GPPGPSYRHD KLTFIDMEGS GFGGDLEALR
GPRGFPGPPG PPGVPGLPGE PGRFGVNSSD VPGPAGLPGV PGREGPPGFP GLPVSPASHR
QCREPCLLGA PTCLVCLFQD DMEGSGGPFW STARSAAGPQ GDPGVPGLPG AKGEVGADGV
PGFPGLPGRE GIAGPQVTPC GVGDTGEGGG PAQGPVFLRQ RLPLGSGSVL SVPGPEGRPG
FAGFPGPAGP KGNLGSKGER GSPGPKGEKG EPGSIFSPDG GALGPAQKGA KVRGPYGRPG
YKGEIGFPGR PGRPGMNGLK GEKGEPGDAS LGFGMRGMPG PPGPPGPPGP PGTPVYDSNV
SPRGTHCPAA TLEGPQANPP VLGAAEGTRR CQTPPQRDPA CLSLAGQFPF DFLQLEAEMK
GEKGDRGDAG QKGERGEPGG GGFFSSSLPG PPGPPGPRGY PGIPVSPSLC RQTPHLCIWS
QQVRLWATRQ AMLGQVHEVP EGWLIFVAEQ EELYVRVRNG FRKVQVSALP RVSHLQDNEV
AALQPPVVQL HDSNPYPRRE HPHPTARPWR ADDILASPLA SPLGRACPHR CGAGVLHLVA
LNSPLSGSMR GIRGADFQCF QQARAVGLAG TFRAFLSSRL QDLYSIVRRA DRTAVPIVNL
KDELLFPSWE ALFSGSEGPL KPGARIFSFD GKDVLRHPTW PQKSVWHGSD PNGRRLTESY
CETWRTEAPS ATGQASSLLG GRLLGQSAVS CHHAYIVLCI ENSFMTASK
//
