TSP4_XENLA
ID TSP4_XENLA Reviewed; 955 AA.
AC Q06441;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Thrombospondin-4;
DE Flags: Precursor;
GN Name=thbs4; Synonyms=tsp4;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8432726; DOI=10.1083/jcb.120.4.1059;
RA Lawler J., Duquette M., Whittaker C.A., Adams J.C., McHenry K.,
RA Desimone D.W.;
RT "Identification and characterization of thrombospondin-4, a new member of
RT the thrombospondin gene family.";
RL J. Cell Biol. 120:1059-1067(1993).
CC -!- FUNCTION: Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions and may be involved in various processes including
CC cellular proliferation, migration, adhesion and attachment. May play a
CC role in ER stress response (By similarity). May participate in the
CC genesis and function of cardiac and skeletal muscle. {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Sarcoplasmic
CC reticulum {ECO:0000250}. Secreted {ECO:0000250}. Secreted,
CC extracellular space {ECO:0000250}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Initial expression during neurulation. Increase
CC during tailbud stages but decrease by the feeding tadpole stage.
CC -!- SIMILARITY: Belongs to the thrombospondin family. {ECO:0000305}.
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DR EMBL; Z19091; CAA79518.1; -; mRNA.
DR PIR; A45441; A45441.
DR RefSeq; NP_001081597.1; NM_001088128.1.
DR AlphaFoldDB; Q06441; -.
DR SMR; Q06441; -.
DR GeneID; 397943; -.
DR KEGG; xla:397943; -.
DR CTD; 397943; -.
DR Xenbase; XB-GENE-17336850; thbs4.L.
DR OrthoDB; 120983at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 397943; Expressed in camera-type eye and 11 other tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR Gene3D; 4.10.1080.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR024665; Thbs/COMP_coiled-coil.
DR InterPro; IPR003367; Thrombospondin_3-like_rpt.
DR InterPro; IPR017897; Thrombospondin_3_rpt.
DR InterPro; IPR008859; Thrombospondin_C.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR Pfam; PF11598; COMP; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 5.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF103647; SSF103647; 3.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS51234; TSP3; 8.
DR PROSITE; PS51236; TSP_CTER; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Disulfide bond; EGF-like domain;
KW Endoplasmic reticulum; Extracellular matrix; Glycoprotein; Growth factor;
KW Mitogen; Reference proteome; Repeat; Sarcoplasmic reticulum; Secreted;
KW Signal; Unfolded protein response.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..955
FT /note="Thrombospondin-4"
FT /id="PRO_0000035856"
FT DOMAIN 25..192
FT /note="Laminin G-like"
FT DOMAIN 281..320
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 321..358
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 374..415
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 418..459
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 460..492
FT /note="TSP type-3 1"
FT REPEAT 493..528
FT /note="TSP type-3 2"
FT REPEAT 529..551
FT /note="TSP type-3 3"
FT REPEAT 552..587
FT /note="TSP type-3 4"
FT REPEAT 588..610
FT /note="TSP type-3 5"
FT REPEAT 611..648
FT /note="TSP type-3 6"
FT REPEAT 649..688
FT /note="TSP type-3 7"
FT REPEAT 689..724
FT /note="TSP type-3 8"
FT DOMAIN 728..942
FT /note="TSP C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00635"
FT REGION 610..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..669
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 256
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 259
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 285..296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 290..305
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 308..319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 325..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 330..345
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 348..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 378..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 386..401
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 404..416
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 422..435
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 429..445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 447..458
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 474..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 484..504
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 520..540
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 543..563
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 579..599
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 602..622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 640..660
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 680..700
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 716..937
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 955 AA; 104918 MW; 0AAE9FBBD9E9187B CRC64;
MPRRKGLCLF LQMLLLHLYG VCQAQPNYQV FDLLSVSVQR QVTSFLQSAL SNPSMNEVYV
LSTFKLQPKS TVTLFGLYST SDNSRFFEFT VMGRLNKASL RYLRSDGKLH SVFFNKLDIA
DGKQHALLLH LSGLHRGATF AKLYIDCNPT GVVEDLPRPL SGIRLNTGSV HLRTLQKKGQ
DSMDELKLVM GGTLSEVGAI QECFMQKSEA GQQTGDVSRQ LIGQITQMNQ MLGELRDVMR
QQVKETMFLR NTIAECQACG LGPDFPLPTK VPQRLATTTP PKPRCDATSC FRGVRCIDTE
GGFQCGPCPE GYTGNGVICT DVDECRLNPC FLGVRCINTS PGFKCESCPP GYTGSTIQGI
GINFAKQNKQ VCTDTNECEN GRNGGCTSNS LCINTMGSFR CGGCKPGYVG DQIKGCKPEK
SCRHGQNPCH ASAQCSEEKD GDVTCTCSVG WAGNGYLCGK DTDIDGYPDE ALPCPDKNCK
KDNCVYVPNS GQEDTDKDNI GDACDEDADG DGILNEQDNC VLAANIDQKN SDQDIFGDAC
DNCRLTLNND QRDTDNDGKG DACDDDMDGD GIKNILDNCQ RVPNVDQKDK DGDGVGDICD
SCPDIINPNQ SDIDNDLVGD SCDTNQDSDG DGHQDSTDNC PTVINSNQLD TDKDGIGDEC
DDDDDNDGIP DTVPPGPDNC KLVPNPGQED DNNDGVGDVC EADFDQDTVI DRIDVCPENA
EITLTDFRAY QTVVLDPEGD AQIDPNWIVL NQGMEIVQTM NSDPGLAVGY TAFNGVDFEG
TFHVNTMTDD DYAGFIFGYQ DSSSFYVVMW KQTEQTYWQA TPFRAVAEPG IQLKAVKSKS
GPGEHLRNAL WHTGDTNDQV RLLWKDPRNV GWKDKVSYRW FLQHRPQVGY IRARFYEGTE
LVADSGVTVD TTMRGGRLGV FCFSQENIIW SNLKYRCNDT IPEDFQAFQA QQFSS
