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Protein

Thrombospondin-1

Gene

thbs1

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Can bind to fibrinogen, fibronectin, laminin, type V collagen and integrins alpha-V/beta-1, alpha-V/beta-3 and alpha-IIb/beta-3 (By similarity). May play a role in ER stress response (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Unfolded protein response

Keywords - Ligandi

Calcium, Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Thrombospondin-1
Gene namesi
Name:thbs1
Synonyms:tsp1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-865586. thbs1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000003584419 – 1173Thrombospondin-1Add BLAST1155

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi155N-linked (GlcNAc...)Sequence analysis1
Glycosylationi158N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi174 ↔ 235By similarity
Glycosylationi250N-linked (GlcNAc...)Sequence analysis1
Glycosylationi363N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi394 ↔ 426By similarity
Disulfide bondi398 ↔ 431By similarity
Disulfide bondi409 ↔ 416By similarity
Disulfide bondi450 ↔ 487By similarity
Disulfide bondi454 ↔ 492By similarity
Disulfide bondi465 ↔ 477By similarity
Disulfide bondi507 ↔ 544By similarity
Disulfide bondi511 ↔ 549By similarity
Disulfide bondi522 ↔ 534By similarity
Disulfide bondi554 ↔ 565By similarity
Disulfide bondi559 ↔ 575By similarity
Disulfide bondi578 ↔ 589By similarity
Disulfide bondi595 ↔ 611By similarity
Disulfide bondi602 ↔ 620By similarity
Disulfide bondi623 ↔ 647By similarity
Disulfide bondi653 ↔ 666By similarity
Disulfide bondi660 ↔ 679By similarity
Disulfide bondi681 ↔ 692By similarity
Glycosylationi705N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi708 ↔ 716By similarity
Glycosylationi711N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi721 ↔ 741By similarity
Disulfide bondi757 ↔ 777By similarity
Disulfide bondi780 ↔ 800By similarity
Disulfide bondi816 ↔ 836By similarity
Disulfide bondi839 ↔ 859By similarity
Disulfide bondi877 ↔ 897By similarity
Disulfide bondi913 ↔ 933By similarity
Disulfide bondi949 ↔ 1170By similarity
Glycosylationi1070N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Homotrimer; disulfide-linked.

Structurei

3D structure databases

ProteinModelPortaliP35448.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 224Laminin G-likeAdd BLAST203
Domaini319 – 376VWFCPROSITE-ProRule annotationAdd BLAST58
Domaini382 – 432TSP type-1 1PROSITE-ProRule annotationAdd BLAST51
Domaini438 – 493TSP type-1 2PROSITE-ProRule annotationAdd BLAST56
Domaini495 – 550TSP type-1 3PROSITE-ProRule annotationAdd BLAST56
Domaini550 – 590EGF-like 1PROSITE-ProRule annotationAdd BLAST41
Domaini649 – 693EGF-like 2PROSITE-ProRule annotationAdd BLAST45
Repeati694 – 729TSP type-3 1Add BLAST36
Repeati730 – 765TSP type-3 2Add BLAST36
Repeati766 – 788TSP type-3 3Add BLAST23
Repeati789 – 824TSP type-3 4Add BLAST36
Repeati825 – 847TSP type-3 5Add BLAST23
Repeati848 – 885TSP type-3 6Add BLAST38
Repeati886 – 921TSP type-3 7Add BLAST36
Repeati922 – 957TSP type-3 8Add BLAST36
Domaini961 – 1173TSP C-terminalPROSITE-ProRule annotationAdd BLAST213

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni50 – 98Heparin-bindingBy similarityAdd BLAST49

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi929 – 931Cell attachment siteSequence analysis3

Sequence similaritiesi

Belongs to the thrombospondin family.Curated
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.Curated
Contains 1 TSP C-terminal (TSPC) domain.PROSITE-ProRule annotation
Contains 3 TSP type-1 domains.PROSITE-ProRule annotation
Contains 8 TSP type-3 repeats.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG018006.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR024731. EGF_dom.
IPR001791. Laminin_G.
IPR028499. Thrombospondin-1.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR000884. TSP1_rpt.
IPR028974. TSP_type-3_rpt.
IPR001007. VWF_dom.
[Graphical view]
PANTHERiPTHR10199:SF78. PTHR10199:SF78. 1 hit.
PfamiPF12947. EGF_3. 1 hit.
PF00090. TSP_1. 3 hits.
PF02412. TSP_3. 7 hits.
PF05735. TSP_C. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 2 hits.
SSF82895. SSF82895. 3 hits.
PROSITEiPS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS50092. TSP1. 3 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35448-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGIFLLLML VMPQTHQAAE SGNDDNSVFD LFELTGYNRK AGSRKPQGLH
60 70 80 90 100
LVKGPDPSSP AYRIEDADLI PPLPEDKFQD LLDAIRADRG FILLATLRQA
110 120 130 140 150
KKSRGALLSV ERKDGGGHIF SLISNGRART LDLSLSGERK QQVVSVEDAV
160 170 180 190 200
LATGNWTNIT LFVQEDRAQL YVGCNKMENA ELDVPIQKIF TENLASTAHL
210 220 230 240 250
RVAKGGVKDN FQGVLQNVRF VFGTTLEAIL RNKGCLSMTN SVITLDNPVN
260 270 280 290 300
GSSPAIRTNY IGHKTKDLQA VCGFSCDDLS KLFAEMKGLR TLVTTLKDQV
310 320 330 340 350
TKETEKNELI AQIVTRTPGV CLHNGVLHKN RDEWTVDSCT ECTCQNSATI
360 370 380 390 400
CRKVSCPLMP CTNATIPDGE CCPRCWPSDS ADDDWSPWSD WTPCSVTCGH
410 420 430 440 450
GIQQRGRSCD SLNNPCEGSS VQTRSCQIQD CDKRFKQDGG WSHWSPWSSC
460 470 480 490 500
SVTCGSGQIT RIRLCNSPVP QLNGKQCEGE GRENKPCQKD PCPINGQWGP
510 520 530 540 550
WSLWDTCTVT CGGGMQKRER LCNNPKPQYE GKDCIGEPTD SQICNKQDCP
560 570 580 590 600
IDGCLSNPCF AGVKCTSFID GSWKCGSCPP GYRGNGITCK DIDECKEVPD
610 620 630 640 650
ACFTLNGVHR CENTEPGYNC LPCPPRFTGT QPFGKGIEEA KANKQVCKPR
660 670 680 690 700
NPCADGTHDC HKNARCIYLG HYSDPMFRCE CRPGYAGNGI ICGEDTDLDG
710 720 730 740 750
WPNENLTCVD NATYHCLKDN CPNLPNSGQE DYDKDGMGDA CDKDDDNDGI
760 770 780 790 800
LDDRDNCQFV YNPAQYDYDR DDVGDRCDNC PYNHNPDQAD TDRNGEGDAC
810 820 830 840 850
SVDIDGDGIL NERDNCAYVY NVDQKDTDKD GVGDQCDNCP LEHNPEQTDS
860 870 880 890 900
DSDLIGDKCD NNQDIDEDGH QNNLDNCPYI PNANQADHDK DGKGDACDHD
910 920 930 940 950
DDNDGVPDDK DNCRLVPNPD QTDTNGDGRG DACQYDFDDD SIPDAEDVCP
960 970 980 990 1000
ENVEISTTDF RKFQMVPLDP KGTSQIDPNW VVRHQGKELV QTVNCDPGIA
1010 1020 1030 1040 1050
VGFDEFSAVD FSGTFFINTE RDDDYAGFVF GYQSSSRFYV VMWKQITQTY
1060 1070 1080 1090 1100
WDTTPTVAQG YSGLSIKVVN STSGPGEHLR NALWHTGNTP GQVRTLWHDP
1110 1120 1130 1140 1150
HQKGWKDFTA YRWHLTHRPK TGFIRVVMYE GKRVMADSGP IYDKTYAGGR
1160 1170
LGLFVFSQEM VFFSDLKYEC RDS
Length:1,173
Mass (Da):130,020
Last modified:June 1, 1994 - v1
Checksum:iA9F036D6516C0F24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04278 mRNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04278 mRNA. No translation available.

3D structure databases

ProteinModelPortaliP35448.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

XenbaseiXB-GENE-865586. thbs1.

Phylogenomic databases

HOVERGENiHBG018006.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR024731. EGF_dom.
IPR001791. Laminin_G.
IPR028499. Thrombospondin-1.
IPR003367. Thrombospondin_3-like_rpt.
IPR017897. Thrombospondin_3_rpt.
IPR008859. Thrombospondin_C.
IPR000884. TSP1_rpt.
IPR028974. TSP_type-3_rpt.
IPR001007. VWF_dom.
[Graphical view]
PANTHERiPTHR10199:SF78. PTHR10199:SF78. 1 hit.
PfamiPF12947. EGF_3. 1 hit.
PF00090. TSP_1. 3 hits.
PF02412. TSP_3. 7 hits.
PF05735. TSP_C. 1 hit.
PF00093. VWC. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 2 hits.
SM00209. TSP1. 3 hits.
SM00210. TSPN. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 3 hits.
SSF49899. SSF49899. 2 hits.
SSF82895. SSF82895. 3 hits.
PROSITEiPS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS50092. TSP1. 3 hits.
PS51234. TSP3. 8 hits.
PS51236. TSP_CTER. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTSP1_XENLA
AccessioniPrimary (citable) accession number: P35448
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 5, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.