Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P98167

- SSPO_BOVIN

UniProt

P98167 - SSPO_BOVIN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

SCO-spondin

Gene

SSPO

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Involved in the modulation of neuronal aggregation. May be involved in developmental events during the formation of the central nervous system.

GO - Molecular functioni

  1. peptidase inhibitor activity Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium

Protein family/group databases

MEROPSiI08.954.

Names & Taxonomyi

Protein namesi
Recommended name:
SCO-spondin
Gene namesi
Name:SSPO
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 51465129SCO-spondinPRO_0000186461Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi? ↔ 5138By similarity
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi814 – 8141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi906 – 9061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1349 – 13491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1373 ↔ 1386By similarity
Disulfide bondi1380 ↔ 1399By similarity
Disulfide bondi1393 ↔ 1408By similarity
Disulfide bondi1413 ↔ 1425By similarity
Disulfide bondi1420 ↔ 1438By similarity
Disulfide bondi1432 ↔ 1447By similarity
Disulfide bondi1449 ↔ 1461By similarity
Disulfide bondi1456 ↔ 1474By similarity
Disulfide bondi1468 ↔ 1483By similarity
Disulfide bondi1489 ↔ 1501By similarity
Disulfide bondi1496 ↔ 1514By similarity
Disulfide bondi1508 ↔ 1525By similarity
Disulfide bondi1562 ↔ 1574By similarity
Disulfide bondi1569 ↔ 1587By similarity
Disulfide bondi1581 ↔ 1596By similarity
Disulfide bondi1600 ↔ 1613By similarity
Disulfide bondi1607 ↔ 1626By similarity
Disulfide bondi1620 ↔ 1637By similarity
Glycosylationi1647 – 16471N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1653 ↔ 1663By similarity
Disulfide bondi1658 ↔ 1676By similarity
Disulfide bondi1670 ↔ 1691By similarity
Disulfide bondi1703 ↔ 1739By similarity
Disulfide bondi1707 ↔ 1744By similarity
Disulfide bondi1718 ↔ 1729By similarity
Glycosylationi1806 – 18061N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1825 ↔ 1840By similarity
Disulfide bondi1834 ↔ 1845By similarity
Disulfide bondi1847 ↔ 1859By similarity
Disulfide bondi1865 ↔ 1884By similarity
Disulfide bondi1867 ↔ 1887By similarity
Disulfide bondi1889 ↔ 1897By similarity
Disulfide bondi1907 ↔ 1946By similarity
Disulfide bondi1918 ↔ 1922By similarity
Disulfide bondi1956 ↔ 1961By similarity
Glycosylationi2027 – 20271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2062 ↔ 2220By similarity
Glycosylationi2127 – 21271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2226 ↔ 2238By similarity
Disulfide bondi2233 ↔ 2251By similarity
Disulfide bondi2245 ↔ 2260By similarity
Disulfide bondi2383 ↔ 2395By similarity
Disulfide bondi2390 ↔ 2408By similarity
Disulfide bondi2402 ↔ 2417By similarity
Disulfide bondi2443 ↔ 2455By similarity
Disulfide bondi2450 ↔ 2468By similarity
Disulfide bondi2462 ↔ 2477By similarity
Disulfide bondi2480 ↔ 2516By similarity
Disulfide bondi2491 ↔ 2495By similarity
Disulfide bondi2526 ↔ 2531By similarity
Disulfide bondi2546 ↔ 2583By similarity
Disulfide bondi2550 ↔ 2588By similarity
Disulfide bondi2561 ↔ 2573By similarity
Glycosylationi2624 – 26241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2673 – 26731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2695 ↔ 2733By similarity
Disulfide bondi2706 ↔ 2710By similarity
Disulfide bondi2743 ↔ 2747By similarity
Disulfide bondi2763 ↔ 2801By similarity
Disulfide bondi2767 ↔ 2806By similarity
Disulfide bondi2783 ↔ 2791By similarity
Disulfide bondi2821 ↔ 2856By similarity
Disulfide bondi2825 ↔ 2861By similarity
Disulfide bondi2836 ↔ 2846By similarity
Glycosylationi2915 – 29151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2946 – 29461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2965 ↔ 3003By similarity
Disulfide bondi2976 ↔ 2980By similarity
Disulfide bondi3013 ↔ 3018By similarity
Glycosylationi3041 – 30411N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3143 – 31431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3153 – 31531N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3175 ↔ 3224By similarity
Disulfide bondi3179 ↔ 3229By similarity
Disulfide bondi3190 ↔ 3214By similarity
Disulfide bondi3244 ↔ 3281By similarity
Disulfide bondi3248 ↔ 3286By similarity
Disulfide bondi3259 ↔ 3271By similarity
Glycosylationi3290 – 32901N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3400 ↔ 3443By similarity
Disulfide bondi3404 ↔ 3449By similarity
Disulfide bondi3415 ↔ 3427By similarity
Disulfide bondi3464 ↔ 3499By similarity
Disulfide bondi3467 ↔ 3506By similarity
Disulfide bondi3477 ↔ 3489By similarity
Glycosylationi3502 – 35021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3580 – 35801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3607 – 36071N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3638 ↔ 3668By similarity
Disulfide bondi3642 ↔ 3673By similarity
Disulfide bondi3653 ↔ 3658By similarity
Glycosylationi3783 – 37831N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3814 ↔ 3852By similarity
Disulfide bondi3818 ↔ 3857By similarity
Disulfide bondi3830 ↔ 3842By similarity
Glycosylationi3906 – 39061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3938 – 39381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3939 ↔ 3975By similarity
Disulfide bondi3950 ↔ 3954By similarity
Disulfide bondi3988 ↔ 3993By similarity
Disulfide bondi4008 ↔ 4045By similarity
Disulfide bondi4012 ↔ 4050By similarity
Disulfide bondi4023 ↔ 4035By similarity
Glycosylationi4131 – 41311N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4152 ↔ 4188By similarity
Disulfide bondi4163 ↔ 4167By similarity
Disulfide bondi4198 ↔ 4203By similarity
Disulfide bondi4257 ↔ 4294By similarity
Disulfide bondi4261 ↔ 4299By similarity
Disulfide bondi4272 ↔ 4284By similarity
Glycosylationi4341 – 43411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4361 ↔ 4398By similarity
Disulfide bondi4372 ↔ 4374By similarity
Disulfide bondi4408 ↔ 4413By similarity
Glycosylationi4412 – 44121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4611 ↔ 4645By similarity
Disulfide bondi4622 ↔ 4626By similarity
Disulfide bondi4655 ↔ 4660By similarity
Glycosylationi4729 – 47291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4746 – 47461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4751 – 47511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4772 – 47721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4773 ↔ 4808By similarity
Disulfide bondi4777 ↔ 4813By similarity
Disulfide bondi4788 ↔ 4797By similarity
Glycosylationi4861 – 48611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4901 – 49011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4947 – 49471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4954 – 49541N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi5052 ↔ 5100By similarity
Glycosylationi5060 – 50601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi5066 ↔ 5117By similarity
Disulfide bondi5076 ↔ 5133By similarity
Disulfide bondi5080 ↔ 5135By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP98167.

Expressioni

Tissue specificityi

Subcommissural organ. Located at the boundary of the diencephalon and mesencephalon beneath the posterior commissure at the point where the axons cross the midline.1 Publication

Developmental stagei

Embryo.

Structurei

3D structure databases

ProteinModelPortaliP98167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 9477EMIAdd
BLAST
Domaini186 – 392207VWFD 1PROSITE-ProRule annotationAdd
BLAST
Domaini464 – 51956TIL 1Add
BLAST
Domaini558 – 768211VWFD 2PROSITE-ProRule annotationAdd
BLAST
Domaini822 – 87554TIL 2Add
BLAST
Domaini1009 – 1215207VWFD 3PROSITE-ProRule annotationAdd
BLAST
Domaini1271 – 132757TIL 3Add
BLAST
Domaini1372 – 140938LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini1412 – 144736LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini1448 – 148437LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini1488 – 152639LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini1561 – 159737LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini1599 – 163840LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini1652 – 169039LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini1691 – 174555TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini1747 – 180559TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini1821 – 186040EGF-like 1Add
BLAST
Domaini1861 – 189838EGF-like 2Add
BLAST
Domaini1906 – 196257TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini1962 – 202261VWFC 1PROSITE-ProRule annotationAdd
BLAST
Domaini2062 – 2220159F5/8 type CPROSITE-ProRule annotationAdd
BLAST
Domaini2225 – 226137LDL-receptor class A 8PROSITE-ProRule annotationAdd
BLAST
Domaini2382 – 241837LDL-receptor class A 9PROSITE-ProRule annotationAdd
BLAST
Domaini2442 – 247837LDL-receptor class A 10PROSITE-ProRule annotationAdd
BLAST
Domaini2479 – 253254TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini2534 – 258956TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini2612 – 265443TIL 4Add
BLAST
Domaini2694 – 274855TSP type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini2751 – 280757TSP type-1 7PROSITE-ProRule annotationAdd
BLAST
Domaini2809 – 286254TSP type-1 8PROSITE-ProRule annotationAdd
BLAST
Domaini2964 – 301956TSP type-1 9PROSITE-ProRule annotationAdd
BLAST
Domaini3020 – 307152TSP type-1 10PROSITE-ProRule annotationAdd
BLAST
Domaini3163 – 323068TSP type-1 11PROSITE-ProRule annotationAdd
BLAST
Domaini3232 – 328756TSP type-1 12PROSITE-ProRule annotationAdd
BLAST
Domaini3291 – 334555TIL 5Add
BLAST
Domaini3388 – 345063TSP type-1 13PROSITE-ProRule annotationAdd
BLAST
Domaini3452 – 350756TSP type-1 14PROSITE-ProRule annotationAdd
BLAST
Domaini3626 – 367449TSP type-1 15PROSITE-ProRule annotationAdd
BLAST
Domaini3802 – 385857TSP type-1 16PROSITE-ProRule annotationAdd
BLAST
Domaini3872 – 392453TSP type-1 17PROSITE-ProRule annotationAdd
BLAST
Domaini3938 – 399457TSP type-1 18PROSITE-ProRule annotationAdd
BLAST
Domaini3996 – 405156TSP type-1 19PROSITE-ProRule annotationAdd
BLAST
Domaini4101 – 416868VWFC 2PROSITE-ProRule annotationAdd
BLAST
Domaini4151 – 420454TSP type-1 20PROSITE-ProRule annotationAdd
BLAST
Domaini4245 – 430056TSP type-1 21PROSITE-ProRule annotationAdd
BLAST
Domaini4302 – 435857TSP type-1 22PROSITE-ProRule annotationAdd
BLAST
Domaini4360 – 441455TSP type-1 23PROSITE-ProRule annotationAdd
BLAST
Domaini4610 – 466152TSP type-1 24PROSITE-ProRule annotationAdd
BLAST
Domaini4761 – 481454TSP type-1 25PROSITE-ProRule annotationAdd
BLAST
Domaini4816 – 487055TIL 6Add
BLAST
Domaini4983 – 504159VWFC 3PROSITE-ProRule annotationAdd
BLAST
Domaini5052 – 513988CTCKPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi523 – 5275Poly-Arg

Sequence similaritiesi

Belongs to the thrombospondin family.Curated
Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation
Contains 2 EGF-like domains.Curated
Contains 1 EMI domain.Curated
Contains 1 F5/8 type C domain.PROSITE-ProRule annotation
Contains 10 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 25 TSP type-1 domains.PROSITE-ProRule annotation
Contains 3 VWFC domains.PROSITE-ProRule annotation
Contains 3 VWFD domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000154433.
HOVERGENiHBG080794.
InParanoidiP98167.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
4.10.400.10. 8 hits.
InterProiIPR000421. 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]
PfamiPF08742. 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]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00832. 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]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF57283. SSF57283. 1 hit.
SSF57424. SSF57424. 9 hits.
SSF57567. SSF57567. 14 hits.
SSF82895. SSF82895. 24 hits.
PROSITEiPS01225. CTCK_2. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

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

P98167-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLPALLFGA AWALANGRWC EQTETVLVEE EVTPHQEDLV PCASLQHYQR
60 70 80 90 100
RGWRLDLTWS GRAGLCAIYK PPETRPAAWN RTVRACCPGW GGTHCTLALA
110 120 130 140 150
EASPEGHCFA TWLCNLGAGS VNASAGSLEE CCAQPWGHSW RDGRSQTCHS
160 170 180 190 200
CSNHSRLGST PSPAILQPLA GAVAQLWSQR QRPSATCATW SGFHYRTFDG
210 220 230 240 250
RHFHFLGRCT YLLAGAADAT WAVHLQPMGH CPQPGHCQLA RVMMGPEEVL
260 270 280 290 300
IRGENVTVNG RLVPEGASQL LPGLSLQWQG DWLVLSGGLG VVVRLDRSSS
310 320 330 340 350
VSISVDQELQ GQTQGLCGVY NGQPEDDFLE PGRGLAALAA TFGNSWRLPD
360 370 380 390 400
SELGCLDAVE AAQGCEDPLR GTETGTEAGQ LRAEAQDVCH QLLEGPFREC
410 420 430 440 450
HTQVPPAEYH EACLFAYCAG APAGSGRAER LEAVCATLAS YAQDCAARRI
460 470 480 490 500
AVRWRKPGFC ERLCPGGQLY SDCASACPPS CSAVGEGSEW SCGEECVSGC
510 520 530 540 550
ECPPGLFWDG ALCVPAARCP CYRRRRRYEP GDTVRQLCNP CECRDGRWLC
560 570 580 590 600
AQAPCAAECA VGGDGHYVTF DGRSFSFRGR AGCRFILVQD FAKRQLLIVL
610 620 630 640 650
EHGDCDAGSC LHAISVSLGD TLVQLRDSGV VLVDGQDVAL PWSAAGGLSV
660 670 680 690 700
SRASSSFLLL RWPGARILWG VSDPAAYITL DPHHAHQVQG LCGTFTRNQQ
710 720 730 740 750
DDFLTPAGDV ETSITAFASK FQVAGGGTCS LEACTPLSPC STHTERQVFA
760 770 780 790 800
EVACAILHGP TFQECHGLVD REAFHLRCLA AVCGCTPGRD CLCPVLAAYA
810 820 830 840 850
RRCAQEGALP SWRNQTFCPV LCPGGQEYQE CAPACDRNCG EPEDCGELDN
860 870 880 890 900
CVAGCNCPLG LLWDPEGQCV PPNLCPCQLG AHRYAPGSAT MKDCNHCVCQ
910 920 930 940 950
ERGLWNCTAH HCAPPRTFCP RELVYVPGAC LLTCDSLDAD RTCPPGSPGG
960 970 980 990 1000
CVCPPGTVLL EERCVPPELC PCRHGGQWYL PNAAIQEDCN LCVCQGQQWH
1010 1020 1030 1040 1050
CTGQRCDGRC RASGAPHYVT FDGLALTFPG ACEYLLVREA SGQFMVSAQN
1060 1070 1080 1090 1100
LPCGASGLTC TKALTVRLQG TVVHMLRGRA VMVNGVSVTP PKVYSGPGLS
1110 1120 1130 1140 1150
LHTAGLFLLL STRLGLTLLW DGGTRVPVQL SPQLRGRVAG LCGDFDGDAS
1160 1170 1180 1190 1200
NDLRSRQGVL EPTAELAAHS WRLGPLCPEP GDLPHPCAVN AHRAGWARAR
1210 1220 1230 1240 1250
CGVVLQPLFA RCHVEVPPQQ HYEQCVYDAC GCDSGGDCEC LCSAIATYAD
1260 1270 1280 1290 1300
ECARHGIHVR WRSQELCPLQ CERGQVYEAC GPTCPATCHD HRPEPGWPCR
1310 1320 1330 1340 1350
AVACVEGCFC PEGTLLHGGV CLEPAACPCE WGGSFFPPGT VLQKDCGNNC
1360 1370 1380 1390 1400
TCRESQWLCG DDGGRCVEPG PGCAEGETPC RESGHCVPHG WLCDNQDDCG
1410 1420 1430 1440 1450
DGSDEEGCAT RVCGEGQVSC CSGRCLPLVL LCDGQDDCGD GMDEQGCPCP
1460 1470 1480 1490 1500
QDSLTCADGH CLPPARLCDG HPDCPDGADE ESCLGQVDCA PGEVSCVDGT
1510 1520 1530 1540 1550
CLGAIQLCDG VWDCLDGGDE GPGHCPLPSL PTPPAGTLPG PSAVSWKLHL
1560 1570 1580 1590 1600
PPWPVSALRL PCGPLDFACG SGECAPRGWR CDGEEDCADG SDESGCDRPC
1610 1620 1630 1640 1650
APHHAPCARG SHCVAAEQLC DGVPHCPDGS DEDPGACERL QAPGGPNRTG
1660 1670 1680 1690 1700
LPCPEYSCPD GLCIGFQQVC DGQPDCELAG TAGPSPEEQG CGAWGPWSPW
1710 1720 1730 1740 1750
ELCSRTCGPG VQGWSRRCSP PSLPVLWHCP GPERQTRACF AAACPEDGVW
1760 1770 1780 1790 1800
TSWSRWSPCS EPCGGVTARH RECHPPQNGG RTCATLPGGP PSTRETRPCP
1810 1820 1830 1840 1850
QDGCPNVTCS GELVFHACVP CPLTCDDISG QATCPPDRPC GGPGCWCPAG
1860 1870 1880 1890 1900
QVLGAQGRCV WPRQCPCLVD GSRYWPGQRV KTDCQLCVCQ DGRPRRCQPS
1910 1920 1930 1940 1950
LDCAVNCGWS AWSPWAECLG PCGSRSVQWS FRSPNNPRPA GRGHQCRGLH
1960 1970 1980 1990 2000
RKARRCQTEP CEGCEQDGRV HRVGERWRAG PCRVCQCLHD GSARCSPYCP
2010 2020 2030 2040 2050
LGSCPQDWVL VEGVGESCCH CVPPGENQTV HPMATPVPAP TPSPQIGAPL
2060 2070 2080 2090 2100
ITYLLPPPGD PCYSPLGLAR LPEGSLPASS QQLEHPAWAA ILRPAPGAPG
2110 2120 2130 2140 2150
WSPVEHADTQ GHTPPPYLQL DLLQPRNLTG IIVQGAGSSD WLQVSSDGLH
2160 2170 2180 2190 2200
WHSYRDIQHG TQPAPQLFPK NWNGPSTVWM FARMVQARHV RVWPSDGHHQ
2210 2220 2230 2240 2250
AAPSSDANLD GPLRVELLGC EPAPLCLGVG HRCVSGECAP RGAPCDGVED
2260 2270 2280 2290 2300
CKDGSDEEGC VTPPAGAGRI ESTAWSSAPS SAQPGQLPPQ PSEGLAEAEA
2310 2320 2330 2340 2350
DHWHPGRGSP VPPTGKGPAS LGSEPHPSPG GSVQTVTPTS QPEAQALRPE
2360 2370 2380 2390 2400
MAAVTVLPPH PMVTPEVPAG RSTTPGPFPH VQCSPGQVPC EVLGCVELEQ
2410 2420 2430 2440 2450
LCDGREDCLD GSDERPCAWA AGTVPFTVPT TTLPGLPASR DLCSPSQLTC
2460 2470 2480 2490 2500
GSGECLPVER RCDLQLDCQD GSDENGCVDC GLAPWSGWSS CSRSCGLGLA
2510 2520 2530 2540 2550
FQRRELLRPP LPGGSCPPDR LRSQPCFVQA CPVAGAWAEW EAWGPCSVSC
2560 2570 2580 2590 2600
GGGHRSRRRS CMDPPPKNGG APCPGPPQER APCGLQPCAG GTDCGQGRVH
2610 2620 2630 2640 2650
VSAELCRKGL VPPCPPSCLD PEANRSCSGL CLEGCRCPPG LLLQDAGCLP
2660 2670 2680 2690 2700
LSECPCLVGE ELQQPGVPFL LDNCSRCVCE KGALLCEPGG CPVPCGWSAW
2710 2720 2730 2740 2750
SSWGPCDRSC GSGLRARFRS PSNPPAASGG APCEGQRQEL QACYSACGAE
2760 2770 2780 2790 2800
VPGWTPWAPW SACSQSCLVP GGGPALRSRS RLCPGPGDTS CIGEATEEEP
2810 2820 2830 2840 2850
CSPPVCLGLG VWGQWAAWSA CSAPCNGGVQ TRGRRCSASA PGDPGCQGPH
2860 2870 2880 2890 2900
SQTRDCNTQP CTAQCPGDMV FRSAEQCRWE GGPCPGLCLA RGPGVECTGV
2910 2920 2930 2940 2950
CTAGCACPTG LFLHNSSCLP PSQCPCQLRG QLYAPGAVAR LDSCSNCTCI
2960 2970 2980 2990 3000
SGEMVCASEP CPVACGWSPW TPWSLCSRSC NVGVRRRFRA GTAPPAAFGG
3010 3020 3030 3040 3050
AACQGPNMEA EFCSLRPCGG PAGEWGPWSP CSVPCGGGYR NRTRGSSGPS
3060 3070 3080 3090 3100
PVDFSTCGLQ PCAGPAPGVC PPGKRWLDCA QGPASCAELS APRGADQPCH
3110 3120 3130 3140 3150
PGCYCPSGML LLNNACVPTQ DCPCTHGGRL HPPGSAVLRP CENCSCVSGL
3160 3170 3180 3190 3200
ITNCTSWPCK EGQPTWSPWT PWSECSASCG PARRHKHRFC TRPPGGAPSS
3210 3220 3230 3240 3250
MAPPLLLSSV PPLCPGPEAE EEPCLLPECD RAGGWGPWGP WSSCSRSCGG
3260 3270 3280 3290 3300
GLRSRSRACD QPPPQGLGDY CEGPRAQGAA CQALPCPVTN CTAIEGAEYS
3310 3320 3330 3340 3350
ACGPPCPRSC DDLVHCVWHC QPGCYCPPGQ VLSADGTVHV QPGHCSCLDL
3360 3370 3380 3390 3400
LTGERHRPGA QLAKPDGCNY CTCSEGQLTC TDLPCPVPGA WCPWSEWTAC
3410 3420 3430 3440 3450
SQPCQGQTRT RSRACSCPAP QHGGAPCPGE AGEAGAQHQR ETCASTPECP
3460 3470 3480 3490 3500
VDGAWSPWGP WSPCEVCLGR SHRSRECSWP PTSEGGRPCP GGHRQSRPCQ
3510 3520 3530 3540 3550
GNSTQCTDCA GGQDLLPCGQ PCPRSCEDLS PGVECQPDSM GCQQPRCGCP
3560 3570 3580 3590 3600
PGQLSQDGLC VTPSQCRCQY QPGAMGIPEN QSRSAGSGLS SWESLEPGEV
3610 3620 3630 3640 3650
VTGPCDNCTC VAGILQCQEV PACSGLGLWG SWGPWEDCSV SCGGGEQLRF
3660 3670 3680 3690 3700
RRCPRPPCPG PARQSRTCRT QVCREAGCPA GRLYRECQPS EGCPFSCAHV
3710 3720 3730 3740 3750
TGQVGCFSAG CEEGCHCPEG TFLHRSACVQ ECPCVLTALW LQGLGAAGAD
3760 3770 3780 3790 3800
PGAHLSVLGE NGQPLGPGDE LGSGQSLRTG CHNCSCAHGK LSCSVEACSK
3810 3820 3830 3840 3850
AAGGFSPWGP WGPCSRSCGG LGTRTRSRQC VRPMPAPGGQ GCHGPHWDLE
3860 3870 3880 3890 3900
YCPSPECPGA AGSTAEPATG LPGGWGLWSP WSPCSGTCTD PAHPAWRSRS
3910 3920 3930 3940 3950
RLCLANCTGG AASQERPCNL PSCTELPLCP GPGCEAGNCS WTAWAPWEPC
3960 3970 3980 3990 4000
SRSCGVGQQR RLRAYHPPGP GGHWCPDVLT AYQERRFCNL RACPVPGGWS
4010 4020 4030 4040 4050
RWSPWSWCDR SCGGGRSLRS RSCSSPPPKN GGAPCVGERH HARLCNPTPC
4060 4070 4080 4090 4100
EEGCPAGMEV VSCANRCPRR CSDLQEGIVC QEDQACQQGC RCPEGSLEQD
4110 4120 4130 4140 4150
GGCVPLGHCE CTDAQGHSWA PGSQHQEACN NCTCRAGQLS CTAQPCPPPA
4160 4170 4180 4190 4200
HCAWSRWSAW SPCSRSCGPA GQQSRFRSST SGSWAPECRE EQSQSQPCPQ
4210 4220 4230 4240 4250
SPCPPLCLQG TRPRSLGDSW LQDGCQQCSC TPEGIICEDA ECAGLGAWTP
4260 4270 4280 4290 4300
WSPWSDCPVS CGGGNQVRTR VCVASAPPRG GSPCLGPDVQ SQRCGLWPCP
4310 4320 4330 4340 4350
ALPDTCSWGP WGPCSRSCGP GLASRSASCP CLLAEAEPAC NSTSPRLDTQ
4360 4370 4380 4390 4400
ACYAGPCLEE CVWSSWSSWT RCSCEVLVQQ RYRHQRPAPG GAGAGPPCTR
4410 4420 4430 4440 4450
LDGHFRPCLT GNCSEDSCAP PFEFQACGSP CTGLCATYLS PWLCQDLPPC
4460 4470 4480 4490 4500
QPGCYCPEGL LEQAGGCVPP EQCNCQHVSG EGAGVTLAPG DRLQLGCKEC
4510 4520 4530 4540 4550
ECQRGELQCT SQGCQGLLPL SGWSEWSPCG PCLPLGLLAP ASRAALEERW
4560 4570 4580 4590 4600
PQDTAGLSPT SAPTLASEQH RHRLCLDPET GRPWAGDPDL CTVPLSQQRL
4610 4620 4630 4640 4650
CPDPGACQDL CQWGPWGAWS PCQVPCSGGF RLRWREAGIP PGGGCRGPWA
4660 4670 4680 4690 4700
QTESCNMGPC PGESCEAQDT VPTPDCANQC PRSCVDLWDR VECLQGPCRP
4710 4720 4730 4740 4750
GCRCPPGQLV QDGHCVPVSS CRCGLPSPNA SWALAPAEVV RLDCRNCTCV
4760 4770 4780 4790 4800
NGSLACSSHE CPTLGPWSAW SNCSAPCGGG TTKRHRSCKE GPGVTPCQAQ
4810 4820 4830 4840 4850
DMEQQQDCNL QPCPECPPGQ VLSACAVSCP RLCSHLQPGT PCMQEPCQLG
4860 4870 4880 4890 4900
CDCPRGQLLH NGTCVPPAEC PCTQLSLPWG LTLTLEEQHR ELPPGTLLTQ
4910 4920 4930 4940 4950
NCTHCICQGG AFSCSLTDCQ ECPPGETWQQ VAPGELGPCE QTCREPNATE
4960 4970 4980 4990 5000
TQGNCSGRQA PGCVCQRGHF RSQEGPCVPV DLCECWHHGR PHPPGSEWQK
5010 5020 5030 5040 5050
ACESCRCVSG ESICTQHCPP LTCAQGETAV QEPGGCCPTC RQEAPEEQPV
5060 5070 5080 5090 5100
SCRHLTELRN LTKGACYLEQ VEVNYCSGHC PSSTNVLPEE PYLQSQCDCC
5110 5120 5130 5140
SYRLDPENPV RILNLRCPGG RTELVVLPVI HSCQCSACQG GDFSER
Length:5,146
Mass (Da):543,593
Last modified:July 11, 2006 - v2
Checksum:i724C5FB8727E13DA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ416457 mRNA. Translation: CAC94914.1.
X93922 mRNA. Translation: CAA63815.1.
RefSeqiNP_777131.1. NM_174706.2.
UniGeneiBt.4812.

Genome annotation databases

GeneIDi282659.
KEGGibta:282659.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ416457 mRNA. Translation: CAC94914.1 .
X93922 mRNA. Translation: CAA63815.1 .
RefSeqi NP_777131.1. NM_174706.2.
UniGenei Bt.4812.

3D structure databases

ProteinModelPortali P98167.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi I08.954.

Proteomic databases

PRIDEi P98167.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 282659.
KEGGi bta:282659.

Organism-specific databases

CTDi 23145.

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000154433.
HOVERGENi HBG080794.
InParanoidi P98167.

Miscellaneous databases

NextBioi 20806337.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
4.10.400.10. 8 hits.
InterProi 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 ]
Pfami 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 ]
PRINTSi PR00261. LDLRECEPTOR.
SMARTi 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 ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF57283. SSF57283. 1 hit.
SSF57424. SSF57424. 9 hits.
SSF57567. SSF57567. 14 hits.
SSF82895. SSF82895. 24 hits.
PROSITEi PS01225. CTCK_2. 1 hit.
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 ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiSSPO_BOVIN
AccessioniPrimary (citable) accession number: P98167
Secondary accession number(s): Q8SPM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 11, 2006
Last modified: October 29, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3