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-APR-2013, entry version 97.
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;
OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC 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
RT of the thrombospondin gene family.";
RL J. Cell Biol. 120:1059-1067(1993).
CC -!- FUNCTION: May act as an extracellular mitogen and may stimulate
CC early erythroid progenitors proliferation (By similarity).
CC Adhesive glycoprotein that mediates cell-to-cell and cell-to-
CC matrix interactions. Can bind to fibrinogen, fibronectin, laminin
CC and type V collagen. May participate in the genesis and function
CC of cardiac and skeletal muscle.
CC -!- SUBUNIT: Homotrimer; disulfide-linked.
CC -!- DEVELOPMENTAL STAGE: Initial expression during neurulation.
CC Increase during tailbud stages but decrease by the feeding tadpole
CC stage.
CC -!- SIMILARITY: Belongs to the thrombospondin family.
CC -!- SIMILARITY: Contains 4 EGF-like domains.
CC -!- SIMILARITY: Contains 1 laminin G-like domain.
CC -!- SIMILARITY: Contains 1 TSP C-terminal (TSPC) domain.
CC -!- SIMILARITY: Contains 8 TSP type-3 repeats.
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DR EMBL; Z19091; CAA79518.1; -; mRNA.
DR PIR; A45441; A45441.
DR RefSeq; NP_001081597.1; NM_001088128.1.
DR UniGene; Xl.12952; -.
DR ProteinModelPortal; Q06441; -.
DR SMR; Q06441; 598-939.
DR GeneID; 397943; -.
DR KEGG; xla:397943; -.
DR CTD; 7060; -.
DR HOVERGEN; HBG000636; -.
DR KO; K04659; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR Gene3D; 2.40.155.10; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR InterPro; IPR000742; EG-like_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR023413; GFP_like.
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 Pfam; PF11598; COMP; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF02412; TSP_3; 6.
DR Pfam; PF05735; TSP_C; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; ConA_like_lec_gl; 2.
DR PROSITE; PS00022; EGF_1; FALSE_NEG.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; FALSE_NEG.
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; Glycoprotein;
KW Growth factor; Mitogen; Repeat; Signal.
FT SIGNAL 1 24 Potential.
FT CHAIN 25 955 Thrombospondin-4.
FT /FTId=PRO_0000035856.
FT DOMAIN 25 192 Laminin G-like.
FT DOMAIN 281 320 EGF-like 1.
FT DOMAIN 321 358 EGF-like 2; calcium-binding (Potential).
FT DOMAIN 374 415 EGF-like 3; calcium-binding (Potential).
FT DOMAIN 418 459 EGF-like 4.
FT REPEAT 460 492 TSP type-3 1.
FT REPEAT 493 528 TSP type-3 2.
FT REPEAT 529 551 TSP type-3 3.
FT REPEAT 552 587 TSP type-3 4.
FT REPEAT 588 610 TSP type-3 5.
FT REPEAT 611 648 TSP type-3 6.
FT REPEAT 649 688 TSP type-3 7.
FT REPEAT 689 724 TSP type-3 8.
FT DOMAIN 728 942 TSP C-terminal.
FT CARBOHYD 609 609 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 938 938 N-linked (GlcNAc...) (Potential).
FT DISULFID 256 256 Interchain (Probable).
FT DISULFID 259 259 Interchain (Probable).
FT DISULFID 285 296 By similarity.
FT DISULFID 290 305 By similarity.
FT DISULFID 308 319 By similarity.
FT DISULFID 325 336 By similarity.
FT DISULFID 330 345 By similarity.
FT DISULFID 348 372 By similarity.
FT DISULFID 378 392 By similarity.
FT DISULFID 386 401 By similarity.
FT DISULFID 404 416 By similarity.
FT DISULFID 422 435 By similarity.
FT DISULFID 429 445 By similarity.
FT DISULFID 447 458 By similarity.
FT DISULFID 474 479 By similarity.
FT DISULFID 484 504 By similarity.
FT DISULFID 520 540 By similarity.
FT DISULFID 543 563 By similarity.
FT DISULFID 579 599 By similarity.
FT DISULFID 602 622 By similarity.
FT DISULFID 640 660 By similarity.
FT DISULFID 680 700 By similarity.
FT DISULFID 716 937 By similarity.
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
//
