P98167 (SSPO_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 99.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: SCO-spondin | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 5146 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Involved in the modulation of neuronal aggregation. May be involved in developmental events during the formation of the central nervous system. |
| Subcellular location | |
| Tissue specificity | Subcommissural organ. Located at the boundary of the diencephalon and mesencephalon beneath the posterior commissure at the point where the axons cross the midline. Ref.1 |
| Developmental stage | Embryo. |
| Sequence similarities | Belongs to the thrombospondin family. Contains 1 CTCK (C-terminal cystine knot-like) domain. Contains 2 EGF-like domains. Contains 1 EMI domain. Contains 1 F5/8 type C domain. Contains 10 LDL-receptor class A domains. Contains 6 TIL (trypsin inhibitory-like) domains. Contains 25 TSP type-1 domains. Contains 3 VWFC domains. Contains 3 VWFD domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell adhesion |
| Cellular component | Secreted |
| Domain | EGF-like domain Repeat Signal |
| Ligand | Calcium |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of peptidase activityInferred from electronic annotation. Source: GOC |
| Cellular_component | extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | peptidase inhibitor activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | Potential | ||||||||
| Chain | 18 – 5146 | 5129 | SCO-spondin | PRO_0000186461 | |||||||
Regions | |||||||||||
| Domain | 18 – 94 | 77 | EMI | ||||||||
| Domain | 186 – 392 | 207 | VWFD 1 | ||||||||
| Domain | 464 – 519 | 56 | TIL 1 | ||||||||
| Domain | 558 – 768 | 211 | VWFD 2 | ||||||||
| Domain | 822 – 875 | 54 | TIL 2 | ||||||||
| Domain | 1009 – 1215 | 207 | VWFD 3 | ||||||||
| Domain | 1271 – 1327 | 57 | TIL 3 | ||||||||
| Domain | 1372 – 1409 | 38 | LDL-receptor class A 1 | ||||||||
| Domain | 1412 – 1447 | 36 | LDL-receptor class A 2 | ||||||||
| Domain | 1448 – 1484 | 37 | LDL-receptor class A 3 | ||||||||
| Domain | 1488 – 1526 | 39 | LDL-receptor class A 4 | ||||||||
| Domain | 1561 – 1597 | 37 | LDL-receptor class A 5 | ||||||||
| Domain | 1599 – 1638 | 40 | LDL-receptor class A 6 | ||||||||
| Domain | 1652 – 1690 | 39 | LDL-receptor class A 7 | ||||||||
| Domain | 1691 – 1745 | 55 | TSP type-1 1 | ||||||||
| Domain | 1747 – 1805 | 59 | TSP type-1 2 | ||||||||
| Domain | 1821 – 1860 | 40 | EGF-like 1 | ||||||||
| Domain | 1861 – 1898 | 38 | EGF-like 2 | ||||||||
| Domain | 1906 – 1962 | 57 | TSP type-1 3 | ||||||||
| Domain | 1962 – 2022 | 61 | VWFC 1 | ||||||||
| Domain | 2062 – 2220 | 159 | F5/8 type C | ||||||||
| Domain | 2225 – 2261 | 37 | LDL-receptor class A 8 | ||||||||
| Domain | 2382 – 2418 | 37 | LDL-receptor class A 9 | ||||||||
| Domain | 2442 – 2478 | 37 | LDL-receptor class A 10 | ||||||||
| Domain | 2479 – 2532 | 54 | TSP type-1 4 | ||||||||
| Domain | 2534 – 2589 | 56 | TSP type-1 5 | ||||||||
| Domain | 2612 – 2654 | 43 | TIL 4 | ||||||||
| Domain | 2694 – 2748 | 55 | TSP type-1 6 | ||||||||
| Domain | 2751 – 2807 | 57 | TSP type-1 7 | ||||||||
| Domain | 2809 – 2862 | 54 | TSP type-1 8 | ||||||||
| Domain | 2964 – 3019 | 56 | TSP type-1 9 | ||||||||
| Domain | 3020 – 3071 | 52 | TSP type-1 10 | ||||||||
| Domain | 3163 – 3230 | 68 | TSP type-1 11 | ||||||||
| Domain | 3232 – 3287 | 56 | TSP type-1 12 | ||||||||
| Domain | 3291 – 3345 | 55 | TIL 5 | ||||||||
| Domain | 3388 – 3450 | 63 | TSP type-1 13 | ||||||||
| Domain | 3452 – 3507 | 56 | TSP type-1 14 | ||||||||
| Domain | 3626 – 3674 | 49 | TSP type-1 15 | ||||||||
| Domain | 3802 – 3858 | 57 | TSP type-1 16 | ||||||||
| Domain | 3872 – 3924 | 53 | TSP type-1 17 | ||||||||
| Domain | 3938 – 3994 | 57 | TSP type-1 18 | ||||||||
| Domain | 3996 – 4051 | 56 | TSP type-1 19 | ||||||||
| Domain | 4101 – 4168 | 68 | VWFC 2 | ||||||||
| Domain | 4151 – 4204 | 54 | TSP type-1 20 | ||||||||
| Domain | 4245 – 4300 | 56 | TSP type-1 21 | ||||||||
| Domain | 4302 – 4358 | 57 | TSP type-1 22 | ||||||||
| Domain | 4360 – 4414 | 55 | TSP type-1 23 | ||||||||
| Domain | 4610 – 4661 | 52 | TSP type-1 24 | ||||||||
| Domain | 4761 – 4814 | 54 | TSP type-1 25 | ||||||||
| Domain | 4816 – 4870 | 55 | TIL 6 | ||||||||
| Domain | 4983 – 5041 | 59 | VWFC 3 | ||||||||
| Domain | 5052 – 5139 | 88 | CTCK | ||||||||
| Compositional bias | 523 – 527 | 5 | Poly-Arg | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 80 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 122 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 153 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 255 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 814 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 906 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1349 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1647 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1806 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2027 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2127 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2624 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2673 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2915 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2946 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3041 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3143 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3153 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3290 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3502 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3580 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3607 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3783 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3906 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 3938 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4131 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4341 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4412 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4729 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4746 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4751 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4772 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4861 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4901 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4947 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 4954 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 5060 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 1373 ↔ 1386 | By similarity | |||||||||
| Disulfide bond | 1380 ↔ 1399 | By similarity | |||||||||
| Disulfide bond | 1393 ↔ 1408 | By similarity | |||||||||
| Disulfide bond | 1413 ↔ 1425 | By similarity | |||||||||
| Disulfide bond | 1420 ↔ 1438 | By similarity | |||||||||
| Disulfide bond | 1432 ↔ 1447 | By similarity | |||||||||
| Disulfide bond | 1449 ↔ 1461 | By similarity | |||||||||
| Disulfide bond | 1456 ↔ 1474 | By similarity | |||||||||
| Disulfide bond | 1468 ↔ 1483 | By similarity | |||||||||
| Disulfide bond | 1489 ↔ 1501 | By similarity | |||||||||
| Disulfide bond | 1496 ↔ 1514 | By similarity | |||||||||
| Disulfide bond | 1508 ↔ 1525 | By similarity | |||||||||
| Disulfide bond | 1562 ↔ 1574 | By similarity | |||||||||
| Disulfide bond | 1569 ↔ 1587 | By similarity | |||||||||
| Disulfide bond | 1581 ↔ 1596 | By similarity | |||||||||
| Disulfide bond | 1600 ↔ 1613 | By similarity | |||||||||
| Disulfide bond | 1607 ↔ 1626 | By similarity | |||||||||
| Disulfide bond | 1620 ↔ 1637 | By similarity | |||||||||
| Disulfide bond | 1653 ↔ 1663 | By similarity | |||||||||
| Disulfide bond | 1658 ↔ 1676 | By similarity | |||||||||
| Disulfide bond | 1670 ↔ 1691 | By similarity | |||||||||
| Disulfide bond | 1703 ↔ 1739 | By similarity | |||||||||
| Disulfide bond | 1707 ↔ 1744 | By similarity | |||||||||
| Disulfide bond | 1718 ↔ 1729 | By similarity | |||||||||
| Disulfide bond | 1825 ↔ 1840 | By similarity | |||||||||
| Disulfide bond | 1834 ↔ 1845 | By similarity | |||||||||
| Disulfide bond | 1847 ↔ 1859 | By similarity | |||||||||
| Disulfide bond | 1865 ↔ 1884 | By similarity | |||||||||
| Disulfide bond | 1867 ↔ 1887 | By similarity | |||||||||
| Disulfide bond | 1889 ↔ 1897 | By similarity | |||||||||
| Disulfide bond | 1907 ↔ 1946 | By similarity | |||||||||
| Disulfide bond | 1918 ↔ 1922 | By similarity | |||||||||
| Disulfide bond | 1956 ↔ 1961 | By similarity | |||||||||
| Disulfide bond | 2062 ↔ 2220 | By similarity | |||||||||
| Disulfide bond | 2226 ↔ 2238 | By similarity | |||||||||
| Disulfide bond | 2233 ↔ 2251 | By similarity | |||||||||
| Disulfide bond | 2245 ↔ 2260 | By similarity | |||||||||
| Disulfide bond | 2383 ↔ 2395 | By similarity | |||||||||
| Disulfide bond | 2390 ↔ 2408 | By similarity | |||||||||
| Disulfide bond | 2402 ↔ 2417 | By similarity | |||||||||
| Disulfide bond | 2443 ↔ 2455 | By similarity | |||||||||
| Disulfide bond | 2450 ↔ 2468 | By similarity | |||||||||
| Disulfide bond | 2462 ↔ 2477 | By similarity | |||||||||
| Disulfide bond | 2480 ↔ 2516 | By similarity | |||||||||
| Disulfide bond | 2491 ↔ 2495 | By similarity | |||||||||
| Disulfide bond | 2526 ↔ 2531 | By similarity | |||||||||
| Disulfide bond | 2546 ↔ 2583 | By similarity | |||||||||
| Disulfide bond | 2550 ↔ 2588 | By similarity | |||||||||
| Disulfide bond | 2561 ↔ 2573 | By similarity | |||||||||
| Disulfide bond | 2695 ↔ 2733 | By similarity | |||||||||
| Disulfide bond | 2706 ↔ 2710 | By similarity | |||||||||
| Disulfide bond | 2743 ↔ 2747 | By similarity | |||||||||
| Disulfide bond | 2763 ↔ 2801 | By similarity | |||||||||
| Disulfide bond | 2767 ↔ 2806 | By similarity | |||||||||
| Disulfide bond | 2783 ↔ 2791 | By similarity | |||||||||
| Disulfide bond | 2821 ↔ 2856 | By similarity | |||||||||
| Disulfide bond | 2825 ↔ 2861 | By similarity | |||||||||
| Disulfide bond | 2836 ↔ 2846 | By similarity | |||||||||
| Disulfide bond | 2965 ↔ 3003 | By similarity | |||||||||
| Disulfide bond | 2976 ↔ 2980 | By similarity | |||||||||
| Disulfide bond | 3013 ↔ 3018 | By similarity | |||||||||
| Disulfide bond | 3175 ↔ 3224 | By similarity | |||||||||
| Disulfide bond | 3179 ↔ 3229 | By similarity | |||||||||
| Disulfide bond | 3190 ↔ 3214 | By similarity | |||||||||
| Disulfide bond | 3244 ↔ 3281 | By similarity | |||||||||
| Disulfide bond | 3248 ↔ 3286 | By similarity | |||||||||
| Disulfide bond | 3259 ↔ 3271 | By similarity | |||||||||
| Disulfide bond | 3400 ↔ 3443 | By similarity | |||||||||
| Disulfide bond | 3404 ↔ 3449 | By similarity | |||||||||
| Disulfide bond | 3415 ↔ 3427 | By similarity | |||||||||
| Disulfide bond | 3464 ↔ 3499 | By similarity | |||||||||
| Disulfide bond | 3467 ↔ 3506 | By similarity | |||||||||
| Disulfide bond | 3477 ↔ 3489 | By similarity | |||||||||
| Disulfide bond | 3638 ↔ 3668 | By similarity | |||||||||
| Disulfide bond | 3642 ↔ 3673 | By similarity | |||||||||
| Disulfide bond | 3653 ↔ 3658 | By similarity | |||||||||
| Disulfide bond | 3814 ↔ 3852 | By similarity | |||||||||
| Disulfide bond | 3818 ↔ 3857 | By similarity | |||||||||
| Disulfide bond | 3830 ↔ 3842 | By similarity | |||||||||
| Disulfide bond | 3939 ↔ 3975 | By similarity | |||||||||
| Disulfide bond | 3950 ↔ 3954 | By similarity | |||||||||
| Disulfide bond | 3988 ↔ 3993 | By similarity | |||||||||
| Disulfide bond | 4008 ↔ 4045 | By similarity | |||||||||
| Disulfide bond | 4012 ↔ 4050 | By similarity | |||||||||
| Disulfide bond | 4023 ↔ 4035 | By similarity | |||||||||
| Disulfide bond | 4152 ↔ 4188 | By similarity | |||||||||
| Disulfide bond | 4163 ↔ 4167 | By similarity | |||||||||
| Disulfide bond | 4198 ↔ 4203 | By similarity | |||||||||
| Disulfide bond | 4257 ↔ 4294 | By similarity | |||||||||
| Disulfide bond | 4261 ↔ 4299 | By similarity | |||||||||
| Disulfide bond | 4272 ↔ 4284 | By similarity | |||||||||
| Disulfide bond | 4361 ↔ 4398 | By similarity | |||||||||
| Disulfide bond | 4372 ↔ 4374 | By similarity | |||||||||
| Disulfide bond | 4408 ↔ 4413 | By similarity | |||||||||
| Disulfide bond | 4611 ↔ 4645 | By similarity | |||||||||
| Disulfide bond | 4622 ↔ 4626 | By similarity | |||||||||
| Disulfide bond | 4655 ↔ 4660 | By similarity | |||||||||
| Disulfide bond | 4773 ↔ 4808 | By similarity | |||||||||
| Disulfide bond | 4777 ↔ 4813 | By similarity | |||||||||
| Disulfide bond | 4788 ↔ 4797 | By similarity | |||||||||
| Disulfide bond | 5052 ↔ 5100 | By similarity | |||||||||
| Disulfide bond | 5066 ↔ 5117 | By similarity | |||||||||
| Disulfide bond | 5076 ↔ 5133 | By similarity | |||||||||
| Disulfide bond | 5080 ↔ 5135 | By similarity | |||||||||
| Disulfide bond | ? ↔ 5138 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Subcommissural organ/Reissner's fiber complex: characterization of SCO-spondin, a glycoprotein with potent activity on neurite outgrowth." Gobron S. Glia 32:177-191(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Subcommissural organ. |
| [2] | "SCO-spondin: a new member of the thrombospondin family secreted by the subcommissural organ is a candidate in the modulation of neuronal aggregation." Gobron S., Monnerie H., Meiniel R., Creveaux I., Lehmann W., Lamalle D., Dastugue B., Meiniel A. J. Cell Sci. 109:1053-1061(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1719-2585. Tissue: Ependymocyte. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ416457 mRNA. Translation: CAC94914.1. X93922 mRNA. Translation: CAA63815.1. |
| IPI | IPI00712771. |
| RefSeq | NP_777131.1. NM_174706.2. |
| UniGene | Bt.4812. |
3D structure databases | |
| ProteinModelPortal | P98167. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | P98167. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 282659. |
| KEGG | bta:282659. |
Organism-specific databases | |
| CTD | 23145. |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| HOGENOM | HOG000154433. |
| HOVERGEN | HBG080794. |
Family and domain databases | |
| Gene3D | 4.10.400.10. 8 hits. |
| InterPro | IPR000421. Coagulation_fac_5/8-C_type_dom. IPR006207. Cys_knot_C. IPR008979. Galactose-bd-like. IPR001545. Gonadotropin_bsu. IPR023415. LDLR_class-A_CS. IPR002172. LDrepeatLR_classA_rpt. IPR008037. Prot_inh_PMP. IPR000884. Thrombospondin_1_rpt. IPR002919. TIL_dom. IPR014853. Unchr_dom_Cys-rich. IPR006552. VWC_out. IPR001007. VWF_C. IPR001846. VWF_type-D. [Graphical view] |
| Pfam | PF08742. C8. 3 hits. PF00754. F5_F8_type_C. 1 hit. PF00057. Ldl_recept_a. 8 hits. PF01826. TIL. 13 hits. PF00090. TSP_1. 22 hits. PF00093. VWC. 1 hit. PF00094. VWD. 3 hits. [Graphical view] |
| SMART | SM00832. C8. 3 hits. SM00041. CT. 1 hit. SM00231. FA58C. 1 hit. SM00068. GHB. 1 hit. SM00192. LDLa. 10 hits. SM00209. TSP1. 25 hits. SM00214. VWC. 3 hits. SM00215. VWC_out. 1 hit. SM00216. VWD. 3 hits. [Graphical view] |
| SUPFAM | SSF57567. Cysrich_TIL. 16 hits. SSF49785. Gal_bind_like. 1 hit. SSF57424. LDL_rcpt_classA_cys-rich. 9 hits. SSF57283. PMP_SGCI. 1 hit. SSF82895. TSP1. 25 hits. |
| PROSITE | PS01185. CTCK_1. False negative. PS01225. CTCK_2. 1 hit. PS00022. EGF_1. False negative. PS01186. EGF_2. False negative. PS50026. EGF_3. False negative. PS51041. EMI. False negative. PS01285. FA58C_1. 1 hit. PS01286. FA58C_2. 1 hit. PS50022. FA58C_3. 1 hit. PS01209. LDLRA_1. 7 hits. PS50068. LDLRA_2. 9 hits. PS50092. TSP1. 25 hits. PS01208. VWFC_1. 1 hit. PS50184. VWFC_2. 2 hits. PS51233. VWFD. 3 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20806337. |
Entry information
| Entry name | SSPO_BOVIN | ||||||||
| Accession | Primary (citable) accession number: P98167 Secondary accession number(s): Q8SPM4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |