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Database: UniProt
Entry: Q06441
LinkDB: Q06441
Original site: Q06441 
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   29-OCT-2014, entry version 106.
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: Adhesive glycoprotein that mediates cell-to-cell and
CC       cell-to-matrix interactions and may be involved in various
CC       processes including cellular proliferation, migration, adhesion
CC       and attachment. May play a role in ER stress response (By
CC       similarity). May participate in the genesis and function of
CC       cardiac and skeletal muscle. {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC       Sarcoplasmic reticulum {ECO:0000250}. Secreted {ECO:0000250}.
CC       Secreted, extracellular space {ECO:0000250}. Secreted,
CC       extracellular space, extracellular matrix {ECO:0000250}.
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. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 4 EGF-like domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00076}.
CC   -!- SIMILARITY: Contains 1 laminin G-like domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 TSP C-terminal (TSPC) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00635}.
CC   -!- SIMILARITY: Contains 8 TSP type-3 repeats. {ECO:0000255|PROSITE-
CC       ProRule:PRU00634}.
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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:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-KW.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISS:UniProtKB.
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   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.155.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 4.10.1080.10; -; 2.
DR   InterPro; IPR013320; ConA-like_dom.
DR   InterPro; IPR000742; EG-like_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR023413; GFP_like.
DR   InterPro; IPR009030; Growth_fac_rcpt_N_dom.
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; 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; 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;
KW   Growth factor; Mitogen; Repeat; Sarcoplasmic reticulum; Secreted;
KW   Signal; Unfolded protein response.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    955       Thrombospondin-4.
FT                                /FTId=PRO_0000035856.
FT   DOMAIN       25    192       Laminin G-like.
FT   DOMAIN      281    320       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      321    358       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      374    415       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      418    459       EGF-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00635}.
FT   CARBOHYD    609    609       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    938    938       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID    256    256       Interchain. {ECO:0000305}.
FT   DISULFID    259    259       Interchain. {ECO:0000305}.
FT   DISULFID    285    296       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    290    305       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    308    319       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    325    336       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    330    345       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    348    372       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    378    392       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    386    401       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    404    416       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    422    435       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    429    445       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    447    458       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    474    479       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    484    504       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    520    540       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    543    563       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    579    599       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    602    622       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    640    660       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    680    700       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    716    937       {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
//
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