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Protein

SCO-spondin

Gene

Sspo

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
SCO-spondin
Gene namesi
Name:Sspo
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:2674311. Sspo.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000024504318 – 4998SCO-spondinAdd BLAST4981

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi? ↔ 4990By similarity
Glycosylationi88N-linked (GlcNAc...)Sequence analysis1
Glycosylationi130N-linked (GlcNAc...)Sequence analysis1
Glycosylationi534N-linked (GlcNAc...)Sequence analysis1
Glycosylationi698N-linked (GlcNAc...)Sequence analysis1
Glycosylationi771N-linked (GlcNAc...)Sequence analysis1
Glycosylationi790N-linked (GlcNAc...)Sequence analysis1
Glycosylationi824N-linked (GlcNAc...)Sequence analysis1
Glycosylationi866N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1230N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1254 ↔ 1267By similarity
Disulfide bondi1261 ↔ 1280By similarity
Disulfide bondi1274 ↔ 1289By similarity
Disulfide bondi1294 ↔ 1306By similarity
Disulfide bondi1301 ↔ 1319By similarity
Disulfide bondi1313 ↔ 1328By similarity
Disulfide bondi1330 ↔ 1342By similarity
Disulfide bondi1337 ↔ 1355By similarity
Disulfide bondi1349 ↔ 1364By similarity
Disulfide bondi1370 ↔ 1382By similarity
Disulfide bondi1377 ↔ 1395By similarity
Disulfide bondi1389 ↔ 1406By similarity
Disulfide bondi1443 ↔ 1455By similarity
Disulfide bondi1450 ↔ 1468By similarity
Disulfide bondi1462 ↔ 1477By similarity
Disulfide bondi1481 ↔ 1494By similarity
Disulfide bondi1488 ↔ 1507By similarity
Disulfide bondi1501 ↔ 1518By similarity
Glycosylationi1528N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1534 ↔ 1544By similarity
Disulfide bondi1539 ↔ 1557By similarity
Disulfide bondi1551 ↔ 1572By similarity
Disulfide bondi1584 ↔ 1620By similarity
Disulfide bondi1588 ↔ 1625By similarity
Glycosylationi1598N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1599 ↔ 1610By similarity
Disulfide bondi1640 ↔ 1680By similarity
Disulfide bondi1644 ↔ 1685By similarity
Disulfide bondi1654 ↔ 1664By similarity
Glycosylationi1687N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1772 ↔ 1811By similarity
Disulfide bondi1783 ↔ 1787By similarity
Disulfide bondi1821 ↔ 1826By similarity
Glycosylationi1892N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1989N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2092 ↔ 2104By similarity
Disulfide bondi2099 ↔ 2117By similarity
Disulfide bondi2111 ↔ 2126By similarity
Disulfide bondi2243 ↔ 2255By similarity
Disulfide bondi2250 ↔ 2268By similarity
Disulfide bondi2262 ↔ 2277By similarity
Disulfide bondi2300 ↔ 2312By similarity
Disulfide bondi2307 ↔ 2325By similarity
Disulfide bondi2319 ↔ 2334By similarity
Disulfide bondi2337 ↔ 2373By similarity
Disulfide bondi2348 ↔ 2352By similarity
Disulfide bondi2383 ↔ 2388By similarity
Disulfide bondi2403 ↔ 2440By similarity
Disulfide bondi2407 ↔ 2445By similarity
Disulfide bondi2418 ↔ 2430By similarity
Glycosylationi2481N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2530N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2552 ↔ 2590By similarity
Disulfide bondi2563 ↔ 2567By similarity
Disulfide bondi2600 ↔ 2604By similarity
Disulfide bondi2620 ↔ 2658By similarity
Disulfide bondi2624 ↔ 2663By similarity
Disulfide bondi2640 ↔ 2648By similarity
Disulfide bondi2678 ↔ 2713By similarity
Disulfide bondi2682 ↔ 2718By similarity
Disulfide bondi2693 ↔ 2703By similarity
Glycosylationi2772N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2802N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2821 ↔ 2859By similarity
Disulfide bondi2832 ↔ 2836By similarity
Disulfide bondi2869 ↔ 2874By similarity
Glycosylationi2897N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2952N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2999N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3009N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3031 ↔ 3080By similarity
Disulfide bondi3035 ↔ 3085By similarity
Disulfide bondi3046 ↔ 3070By similarity
Disulfide bondi3100 ↔ 3137By similarity
Disulfide bondi3104 ↔ 3142By similarity
Disulfide bondi3115 ↔ 3127By similarity
Glycosylationi3146N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3235N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3256 ↔ 3299By similarity
Disulfide bondi3260 ↔ 3305By similarity
Disulfide bondi3271 ↔ 3283By similarity
Glycosylationi3301N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3320 ↔ 3355By similarity
Disulfide bondi3323 ↔ 3362By similarity
Disulfide bondi3333 ↔ 3345By similarity
Glycosylationi3357N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3435N-linked (GlcNAc...)Sequence analysis1
Glycosylationi3462N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3493 ↔ 3523By similarity
Disulfide bondi3497 ↔ 3528By similarity
Disulfide bondi3508 ↔ 3513By similarity
Glycosylationi3638N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3669 ↔ 3707By similarity
Disulfide bondi3673 ↔ 3712By similarity
Disulfide bondi3685 ↔ 3697By similarity
Glycosylationi3761N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3794 ↔ 3830By similarity
Disulfide bondi3805 ↔ 3809By similarity
Disulfide bondi3843 ↔ 3848By similarity
Disulfide bondi3863 ↔ 3900By similarity
Disulfide bondi3867 ↔ 3905By similarity
Disulfide bondi3878 ↔ 3890By similarity
Glycosylationi3986N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4007 ↔ 4043By similarity
Disulfide bondi4018 ↔ 4022By similarity
Disulfide bondi4053 ↔ 4058By similarity
Disulfide bondi4112 ↔ 4149By similarity
Disulfide bondi4116 ↔ 4154By similarity
Disulfide bondi4127 ↔ 4139By similarity
Disulfide bondi4169 ↔ 4207By similarity
Disulfide bondi4173 ↔ 4212By similarity
Disulfide bondi4184 ↔ 4195By similarity
Glycosylationi4196N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4216 ↔ 4253By similarity
Disulfide bondi4227 ↔ 4229By similarity
Disulfide bondi4263 ↔ 4268By similarity
Glycosylationi4267N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4408N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4463N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4466 ↔ 4500By similarity
Disulfide bondi4477 ↔ 4481By similarity
Disulfide bondi4510 ↔ 4515By similarity
Glycosylationi4584N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4601N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4606N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4628 ↔ 4663By similarity
Disulfide bondi4632 ↔ 4668By similarity
Disulfide bondi4643 ↔ 4652By similarity
Glycosylationi4716N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4756N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4799N-linked (GlcNAc...)Sequence analysis1
Glycosylationi4806N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4892 ↔ 4952By similarity
Glycosylationi4912N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi4918 ↔ 4969By similarity
Disulfide bondi4928 ↔ 4985By similarity
Disulfide bondi4932 ↔ 4987By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ8CG65.
PRIDEiQ8CG65.

PTM databases

iPTMnetiQ8CG65.
PhosphoSitePlusiQ8CG65.

Expressioni

Tissue specificityi

Subcommissural organ.1 Publication

Developmental stagei

Weakly expressed at E14 and E15 in the SCO anlage; increasing progressively until E17 dpc.1 Publication

Gene expression databases

BgeeiENSMUSG00000029797.
CleanExiMM_SSPO.
ExpressionAtlasiQ8CG65. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000131401.

Structurei

3D structure databases

ProteinModelPortaliQ8CG65.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 102EMIAdd BLAST85
Domaini163 – 288VWFD 1PROSITE-ProRule annotationAdd BLAST126
Domaini349 – 404TIL 1Add BLAST56
Domaini404 – 496VWFC 1PROSITE-ProRule annotationAdd BLAST93
Domaini443 – 652VWFD 2PROSITE-ProRule annotationAdd BLAST210
Domaini706 – 759TIL 2Add BLAST54
Domaini893 – 1097VWFD 3PROSITE-ProRule annotationAdd BLAST205
Domaini1153 – 1209TIL 3Add BLAST57
Domaini1253 – 1290LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST38
Domaini1293 – 1328LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST36
Domaini1329 – 1365LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST37
Domaini1369 – 1407LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST39
Domaini1442 – 1478LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST37
Domaini1480 – 1519LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST40
Domaini1533 – 1571LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST39
Domaini1572 – 1626TSP type-1 1PROSITE-ProRule annotationAdd BLAST55
Domaini1628 – 1686TSP type-1 2PROSITE-ProRule annotationAdd BLAST59
Domaini1702 – 1741EGF-like 1Add BLAST40
Domaini1742 – 1768EGF-like 2Add BLAST27
Domaini1771 – 1827TSP type-1 3PROSITE-ProRule annotationAdd BLAST57
Domaini1827 – 1887VWFC 2PROSITE-ProRule annotationAdd BLAST61
Domaini1929 – 2085F5/8 type CPROSITE-ProRule annotationAdd BLAST157
Domaini2091 – 2127LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST37
Domaini2242 – 2278LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST37
Domaini2299 – 2335LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST37
Domaini2336 – 2389TSP type-1 4PROSITE-ProRule annotationAdd BLAST54
Domaini2391 – 2446TSP type-1 5PROSITE-ProRule annotationAdd BLAST56
Domaini2469 – 2511TIL 4Add BLAST43
Domaini2551 – 2605TSP type-1 6PROSITE-ProRule annotationAdd BLAST55
Domaini2609 – 2664TSP type-1 7PROSITE-ProRule annotationAdd BLAST56
Domaini2666 – 2719TSP type-1 8PROSITE-ProRule annotationAdd BLAST54
Domaini2820 – 2875TSP type-1 9PROSITE-ProRule annotationAdd BLAST56
Domaini2876 – 2919TSP type-1 10PROSITE-ProRule annotationAdd BLAST44
Domaini2926 – 2978TIL 5Add BLAST53
Domaini3019 – 3086TSP type-1 11PROSITE-ProRule annotationAdd BLAST68
Domaini3088 – 3143TSP type-1 12PROSITE-ProRule annotationAdd BLAST56
Domaini3147 – 3201TIL 6Add BLAST55
Domaini3244 – 3306TSP type-1 13PROSITE-ProRule annotationAdd BLAST63
Domaini3308 – 3363TSP type-1 14PROSITE-ProRule annotationAdd BLAST56
Domaini3481 – 3529TSP type-1 15PROSITE-ProRule annotationAdd BLAST49
Domaini3657 – 3713TSP type-1 16PROSITE-ProRule annotationAdd BLAST57
Domaini3727 – 3779TSP type-1 17PROSITE-ProRule annotationAdd BLAST53
Domaini3793 – 3849TSP type-1 18PROSITE-ProRule annotationAdd BLAST57
Domaini3851 – 3906TSP type-1 19PROSITE-ProRule annotationAdd BLAST56
Domaini3909 – 3964TIL 7Add BLAST56
Domaini4006 – 4059TSP type-1 20PROSITE-ProRule annotationAdd BLAST54
Domaini4100 – 4155TSP type-1 21PROSITE-ProRule annotationAdd BLAST56
Domaini4157 – 4213TSP type-1 22PROSITE-ProRule annotationAdd BLAST57
Domaini4215 – 4269TSP type-1 23PROSITE-ProRule annotationAdd BLAST55
Domaini4465 – 4516TSP type-1 24PROSITE-ProRule annotationAdd BLAST52
Domaini4616 – 4669TSP type-1 25PROSITE-ProRule annotationAdd BLAST54
Domaini4835 – 4893VWFC 3PROSITE-ProRule annotationAdd BLAST59
Domaini4892 – 4991CTCKPROSITE-ProRule annotationAdd BLAST100

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

eggNOGiKOG1215. Eukaryota.
KOG1216. Eukaryota.
KOG3538. Eukaryota.
KOG3611. Eukaryota.
ENOG410XNSK. LUCA.
GeneTreeiENSGT00760000118896.
HOGENOMiHOG000154433.
HOVERGENiHBG080794.
InParanoidiQ8CG65.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
4.10.400.10. 9 hits.
InterProiIPR006207. Cys_knot_C.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR002919. TIL_dom.
IPR000884. TSP1_rpt.
IPR014853. Unchr_dom_Cys-rich.
IPR001007. VWF_dom.
IPR001846. VWF_type-D.
[Graphical view]
PfamiPF08742. C8. 3 hits.
PF00754. F5_F8_type_C. 1 hit.
PF00057. Ldl_recept_a. 7 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.
SM00192. LDLa. 10 hits.
SM00209. TSP1. 25 hits.
SM00214. VWC. 4 hits.
SM00215. VWC_out. 9 hits.
SM00216. VWD. 2 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF57424. SSF57424. 9 hits.
SSF57567. SSF57567. 14 hits.
SSF82895. SSF82895. 24 hits.
PROSITEiPS01225. CTCK_2. 1 hit.
PS01186. EGF_2. 2 hits.
PS50022. FA58C_3. 1 hit.
PS01209. LDLRA_1. 8 hits.
PS50068. LDLRA_2. 10 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.

Q8CG65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPLALLFGM LWTQANGHWC EQIETVHVEE EVTPRQEDLV PCTSLYHYSR
60 70 80 90 100
LGWQLDLSWS GRVGLTRPPA LGLCAIYKPP ETRPATWNRT VRACCPGWGG
110 120 130 140 150
AHCTDALAET SPKGHCFVTW HCQPLAGSAN SSAGSLEDPA DELGVWPLTL
160 170 180 190 200
NDPILFPGMS LQWQGDWLVL SGGLGVVVRL DRSSSISISV DHEFWGRTQG
210 220 230 240 250
LCGLYNGRPE DDFVEPGGGL ATLAATFGNS WKLPGSEPGC LDAVEVAWGC
260 270 280 290 300
ESLLGGTLTD LEAVKLQAQA QDMCHQLLEG PFWQCHGQVQ PDEYHETCLF
310 320 330 340 350
AYCVGATAGN GPEGQLEAVC ATFANYAQAC ARQHIYVHWR KPGFCERVCP
360 370 380 390 400
GGQLYSDCVS SCPPSCSAVA QGEEGSCGKE CVSGCECPTG LFWDGALCVP
410 420 430 440 450
AAHCPCYHRR QRYAPGDTVK QQCNPCVCQD GRWHCAQALC PAECAVGGDG
460 470 480 490 500
HYFTFDGRSF FFRGTPGCHY SLVQDSVKGQ LLVVLEHGAC DTGSCLHALS
510 520 530 540 550
VFLGNTHIQL RYSGAVLVDG EDVDLPWIGV EGFNISWASS TFLLLHWPGA
560 570 580 590 600
WVLWGVAEPA AYITLDPRHA YQVQGLCGTF TWKQQDDFLT PAGDIETSVT
610 620 630 640 650
AFASKFQVSG DGRCPLVDKS PLFCSSYSQH LTFTEAACAI LHGHAFQECH
660 670 680 690 700
GLVDREPFRL RCLEAVCGCA PGRDCLCPVL SAYTRHCAQE GVLLQWRNET
710 720 730 740 750
LCPVSCPGGQ VYQECAPVCG HHCGEPEDCK ELGICVAGCN CPPGLLWDLE
760 770 780 790 800
GQCVPPSMCH CQFGGHRYTI NTTTVRDCSH CICQERGLWN CTAHHCPRQW
810 820 830 840 850
ALCPRELIYV PGACLLTCDS PRANHSCWAG STDGCVCPPG TVLLDKHCVS
860 870 880 890 900
PDLCPCRHNG QWYPPNATIQ EDCNICVCQG QRWHCTGQRC SGWCQASGAP
910 920 930 940 950
HYVTFDGLVF TFPGACEYLL VREAGGRFSV SVQNLPCGAS GLTCTKALVV
960 970 980 990 1000
RLDSTVVHML RGQAVTVNGV SIRLPKVYTG PGLSLHHAGL FLLLTTRLGL
1010 1020 1030 1040 1050
TLLWDGGTRV LVQLSPHFHG RVAGLCGNFD SDASNDLRSR QGVLEPTAEL
1060 1070 1080 1090 1100
TAHSWRLNPL CPEPGDLPHP VNAHRANWAR ARCEVILQPI FAPCHTEVPP
1110 1120 1130 1140 1150
QQYYEWCVYD ACGCDTGGDC ECLCSAIATY ADECARHRHH VRWRSQELCP
1160 1170 1180 1190 1200
LQCEGGQVYE PCGSTCPPTC HDHHSELRWH CQVITCVEGC FCPEGTLLHG
1210 1220 1230 1240 1250
GACMKLAACP CEWQGSFFPP GTVLQKDCGN CTCQGSQWHC DRGGAPCEDM
1260 1270 1280 1290 1300
EPGCAEGETL CRENGHCVPL EWLCDNQDDC GDGSDEEGCA TSVCGEGQMS
1310 1320 1330 1340 1350
CQSGHCLPLS LICDGQDDCG DGTDEQGCLC PHGSLACADG RCLPPALLCN
1360 1370 1380 1390 1400
GHPDCLDAAD EESCLGPVSC ISGEVSCVDG TCVRTIQLCD GVWDCPDGAD
1410 1420 1430 1440 1450
EGPSHCSLPS LPTPPGGIGQ NPSTSSLDTA PSPVGSTSPA SPCSLLEFQC
1460 1470 1480 1490 1500
NSGECTPRGW RCDQEEDCTD GSDELDCGGP CMLYQVPCAH SPHCVSPGQL
1510 1520 1530 1540 1550
CDGVTQCPDG SDEDPDVCEE QSASGGANRT GAPCPEFSCP DGTCIDFLLV
1560 1570 1580 1590 1600
CDGNPDCELA DETEPSLDEQ GCGAWGSWGP WAPCSQTCGS GTRSRNRNCS
1610 1620 1630 1640 1650
TSSLQVLQNC PGLQHQSQAC FTEACPVDGE WSSWSPWSPC SEPCGGTTTR
1660 1670 1680 1690 1700
HRQCRPPQNG GQDCALLPGS THSTRQTSPC PQEGCLNATC FGELVFRTCA
1710 1720 1730 1740 1750
PCPLTCDDIS GQAACPPDRP CSSPGCWCPD GKVLNTEGQC VRPRQCPCLV
1760 1770 1780 1790 1800
DGAHYWPGQR IKMDCQLCFL DCGWSSWSPW AECLGPCSSQ SLQWSFRSPN
1810 1820 1830 1840 1850
NPRLSGHGRQ CRGIHRKARR CQTEACEGCE QWGLMYNVGE RWRGGPCMVC
1860 1870 1880 1890 1900
ECLHSSITHC SPYCPIGSCP QGWVLVEGMG ESCCHCALPE KNQTVIHMTT
1910 1920 1930 1940 1950
PAPAPASAPS PQIGAHLVTY VLPPTADACY SPLGLAGLPM WAPSQHWEHI
1960 1970 1980 1990 2000
TRADPVEAPM AGPGPREGAS AEWHTQPLYL QLDLRRPRNL TGIIVQRAGS
2010 2020 2030 2040 2050
SAAYVSTLSL QFSSDNLQWH NYVNSLSSTL SPPKPSPESS NHMAPEVWTF
2060 2070 2080 2090 2100
DQMVQARYIR VWPHSGHLRD NNQHDIFLWV ELLGLSPLAP LCPGSRHRCA
2110 2120 2130 2140 2150
SGECAPKGGP CDGAVDCDDG SDEEGCGSLH ASTTSRTPAL SPTQPGKFPR
2160 2170 2180 2190 2200
EVSEDLRQGA EAMTSHSPPS SGETAGLIPA SEGTLPVSGQ PMQTLSATST
2210 2220 2230 2240 2250
FPPGAKSLHP GMAAVTVHPP HSVTPGAPVG QTVSPRPFPP MPCGPGQVPC
2260 2270 2280 2290 2300
DVLGCVEQEQ LCDGREDCLD GSDEQHCASA EPFTVPTTAL PGLPASKALC
2310 2320 2330 2340 2350
SPSQLRCGSG ECLPFEHRCD LQVNCQDGSD EDNCVDCVLA PWSGWSDCSR
2360 2370 2380 2390 2400
SCGLGLIFQH RELLRLPLPG GSCLLDQFRS QSCFVQACPV AGAWAEWGPW
2410 2420 2430 2440 2450
TACSVSCGGG HQSRQRSCVD PPPKNGGAPC PGPSHEKAPC NLQLCPGDTD
2460 2470 2480 2490 2500
CEPGLVHVNA ELCQKGLVPP CPPSCLDPEA NRSCSGHCME GCRCPPGLLL
2510 2520 2530 2540 2550
QDSHCLPLSE CPCLVGQKLI QPRLAFLLDN CSQCICEKGT LLCKPGACSQ
2560 2570 2580 2590 2600
SCGWSAWSPW TACDRSCGSG VRARFRSPTN PPVAFGGSPC EGDRQELQAC
2610 2620 2630 2640 2650
YTDCGTEIPG WTPWTSWSSC SQSCLVPGGD PGWRQRSRLC PSSRDTFCPG
2660 2670 2680 2690 2700
EATQEEPCSP PVCPVPSAWG LWASWSTCSA SCNGGIQTRG RSCSGSAPGN
2710 2720 2730 2740 2750
PVCLGPHTQT RDCNMHPCTA QCPGNMVFRS AEQCLEEGGP CPQLCLAQDP
2760 2770 2780 2790 2800
GVECTGSCAP SCNCPPGLFL HNASCLPRSQ CPCQLHGQLY APGAVAHLDC
2810 2820 2830 2840 2850
NNCTCISGEM VCTSKRCPVA CGWSPWTPWS PCSQSCNVGI RRRFRAGTEP
2860 2870 2880 2890 2900
PAAFGGAECQ GPNLDAEFCS LRPCRGPGAA WSSWTPCSVP CGGGYRNRTQ
2910 2920 2930 2940 2950
GSGPHSPIEF STCSLQPCAG PVPGVCPEDQ QWLDCAQGPA SCAHLSIPGE
2960 2970 2980 2990 3000
ANQTCHPGCY CLSGMLLLNN VCVPVQDCPC AHRGRLYSPG SAVHLPCENC
3010 3020 3030 3040 3050
SCISGLITNC SSWPCEEGQP AWSSWTPWSV CSASCNPARR HRHRFCARPP
3060 3070 3080 3090 3100
HRAPFSLVLL TTVAAPTTLC PGPEAEEEPC LLPGCNQAGG WSPWSPWSGC
3110 3120 3130 3140 3150
SRSCGGGLRS RTRACDQPSP QGLGDFCEGP QAQGEACQAQ PCPVTNCSAM
3160 3170 3180 3190 3200
EGAEYSPCGP PCPRSCDDLV HCVWRCQPGC YCPLGKVLSA DGAICVKPSY
3210 3220 3230 3240 3250
CSCLDLLTGK RHHAGTQLMR PDGCNHCTCM EGRLNCTDLP CQVSGDWCPW
3260 3270 3280 3290 3300
SKWTACSQPC RGQTRTRSRA CVCPAPQHGG SPCPEESGGT GVQHQMEACP
3310 3320 3330 3340 3350
NATACPVDGA WSPWGPWSSC DACLGQSYRS RVCSHPPISD GGKPCLGGYQ
3360 3370 3380 3390 3400
QSRPCRNSST LCTDCGGGQD LLPCGQPCPH SCQDLSLGST CQPGSAGCQS
3410 3420 3430 3440 3450
GCGCPPGQLS QDGLCVFPVD CHCHFQPRAM GIPENRSRSV GSTLSSWESL
3460 3470 3480 3490 3500
EPGEVVTGPC DNCTCVAGIL QCHEVPSCPG PGIWSSWGPW EKCSVSCGGG
3510 3520 3530 3540 3550
EQLRSRQCAR PPCPGLAQQS RICHIHVCRE TGCPAGRLYR ECQPSDGCPF
3560 3570 3580 3590 3600
SCAHVTGQVA CFSERCKEGC HCPEGTFQHH VACVQECPCV LTVLLLQELG
3610 3620 3630 3640 3650
LASAALGSYP TLLGDEGKPL GPGVELLPGQ MLQTDCGNCS CVHGKLSCSM
3660 3670 3680 3690 3700
VECSRVHGSF GPWGMWSLCS RSCGGLGTRT RTRQCVLPTL APGGLSCRGP
3710 3720 3730 3740 3750
LQDLEYCFSP ECPGTAGSTV EPVTGLAGGW GPWSPWSPCS HSCTDPAHPA
3760 3770 3780 3790 3800
WRSRTRLCLA NCTVGDSSQE RPCNLPSCAA LLPCPGPGCG SGNCFWTSWA
3810 3820 3830 3840 3850
PWEPCSRSCG VGQQRRLRAY HPPGPGGHWC PDILTAYQER RFCNLRACPV
3860 3870 3880 3890 3900
PGGWSHWSPW SWCDRSCGGG RSLRSRSCSS PPPKNGGTSC VGERHHVRPC
3910 3920 3930 3940 3950
NPMPCEEGCP AGMEMVSCAN HCPYSCSDLQ EGGMCQEDQA CQLGCRCSEG
3960 3970 3980 3990 4000
FLEQDGGCVP VGHCECTDAQ GRSWAPGSQH QDACNNCSCQ AGQLSCTAQL
4010 4020 4030 4040 4050
CSPPAHCAWS HWSAWSSCSH SCGPQGQQSR FRSSTSGSWA LECQKEQSQS
4060 4070 4080 4090 4100
QPCPEVPCPP LCLHEAHLHE LGDNWLHGEC QQCSCTPEGA ICKDTDCAVP
4110 4120 4130 4140 4150
RGWTLWSSWS YCSVSCGGGS QVRTRSCTVS APPHGSLSCE GPDTQTRHCG
4160 4170 4180 4190 4200
QQLCLQKLER CSWGPWGPCS RSCGTGLASR SGSCPCLLTK EDSKCNDTFL
4210 4220 4230 4240 4250
GLDTQACYSG PCQDDCTWGD WSSWTRCSCK VLVQQRYRHQ VPAPGQAGEG
4260 4270 4280 4290 4300
TPCTRLDGHF RPCTIGNCSE DSCPPPFEFQ SCGSPCAGLC ATHLNHRLCQ
4310 4320 4330 4340 4350
DLPPCQPGCY CPKGLLEQAG SCILPEQCNC WHISGEGARV TLAPGDRLQL
4360 4370 4380 4390 4400
GCKECVCRRG ELQCSSQGCE GLLPLTGWSE WSPCGPCLPQ SALAPASRTA
4410 4420 4430 4440 4450
LEGHWPLNTS DLPPPSVTLL ASEQYRHRLC LDPETRRPWA GDPALCTVPL
4460 4470 4480 4490 4500
SQQRLCPDPG ACNDTCQWGP WGPWSPCQMP CSGGFKLRWR VARDTSAGEC
4510 4520 4530 4540 4550
PGPWAQTESC NMGSCPGESC ETRDTVFTLD CANQCPRSCA DLWDGVQCLQ
4560 4570 4580 4590 4600
GPCSPGCRCP PGQLVQDGHC VPISSCRCGL PSANASWELA PTQVVQLDCH
4610 4620 4630 4640 4650
NCTCINGTLM CPHLECPVLG PWSAWSECSA VCGKGTMVRH RSCEEHPDRE
4660 4670 4680 4690 4700
PCQALDLQQW QECNLQACPE CPPGQVLSTC ATMCPSLCSH LWPGTICVRE
4710 4720 4730 4740 4750
PCQLGCGCPG GQLLYNGTCI PPEACPCTQF SLPWGLTLPL EEQARELPSG
4760 4770 4780 4790 4800
TVLTRNCTHC TCQGGAFICS LTDCQECAPG EIWQHGKLGP CEKTCPEMNM
4810 4820 4830 4840 4850
TQAWSNCTEA QAPGCVCQLG YFRSQTGLCV PEDHCECWHH GSPHLPGSEW
4860 4870 4880 4890 4900
QEACESCRCL HGKSVCIRHC PELSCAQGEV IMQEPGSCCP ICQQDTLKEE
4910 4920 4930 4940 4950
PVSCRYLTEL RNLTKGPCHL DQIEVSYCSG HCRSSTNVMT EEPYLQSQCD
4960 4970 4980 4990
CCSYRLDPDS PVRILNLLCP DGHTEPVVLP VIHSCQCSAC QGGDFSKH
Length:4,998
Mass (Da):534,975
Last modified:July 27, 2011 - v2
Checksum:i52726F62E3639AEC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti192H → Q in CAD42654 (PubMed:12909363).Curated1
Sequence conflicti1043V → L in CAD42654 (PubMed:12909363).Curated1
Sequence conflicti1049E → Y in CAD42654 (PubMed:12909363).Curated1
Sequence conflicti1071V → W in CAD42654 (PubMed:12909363).Curated1
Sequence conflicti1080R → P in CAD42654 (PubMed:12909363).Curated1
Sequence conflicti1769F → G in CAD42654 (PubMed:12909363).Curated1
Sequence conflicti3379P → R in CAD42654 (PubMed:12909363).Curated1
Sequence conflicti3412D → H in CAD42654 (PubMed:12909363).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ491857 mRNA. Translation: CAD42654.1.
AC153815 Genomic DNA. No translation available.
UniGeneiMm.25039.

Genome annotation databases

EnsembliENSMUST00000043676; ENSMUSP00000047991; ENSMUSG00000029797.
UCSCiuc009bul.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ491857 mRNA. Translation: CAD42654.1.
AC153815 Genomic DNA. No translation available.
UniGeneiMm.25039.

3D structure databases

ProteinModelPortaliQ8CG65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000131401.

PTM databases

iPTMnetiQ8CG65.
PhosphoSitePlusiQ8CG65.

Proteomic databases

PaxDbiQ8CG65.
PRIDEiQ8CG65.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043676; ENSMUSP00000047991; ENSMUSG00000029797.
UCSCiuc009bul.1. mouse.

Organism-specific databases

MGIiMGI:2674311. Sspo.

Phylogenomic databases

eggNOGiKOG1215. Eukaryota.
KOG1216. Eukaryota.
KOG3538. Eukaryota.
KOG3611. Eukaryota.
ENOG410XNSK. LUCA.
GeneTreeiENSGT00760000118896.
HOGENOMiHOG000154433.
HOVERGENiHBG080794.
InParanoidiQ8CG65.

Miscellaneous databases

PROiQ8CG65.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029797.
CleanExiMM_SSPO.
ExpressionAtlasiQ8CG65. baseline and differential.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
4.10.400.10. 9 hits.
InterProiIPR006207. Cys_knot_C.
IPR000421. FA58C.
IPR008979. Galactose-bd-like.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR002919. TIL_dom.
IPR000884. TSP1_rpt.
IPR014853. Unchr_dom_Cys-rich.
IPR001007. VWF_dom.
IPR001846. VWF_type-D.
[Graphical view]
PfamiPF08742. C8. 3 hits.
PF00754. F5_F8_type_C. 1 hit.
PF00057. Ldl_recept_a. 7 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.
SM00192. LDLa. 10 hits.
SM00209. TSP1. 25 hits.
SM00214. VWC. 4 hits.
SM00215. VWC_out. 9 hits.
SM00216. VWD. 2 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF57424. SSF57424. 9 hits.
SSF57567. SSF57567. 14 hits.
SSF82895. SSF82895. 24 hits.
PROSITEiPS01225. CTCK_2. 1 hit.
PS01186. EGF_2. 2 hits.
PS50022. FA58C_3. 1 hit.
PS01209. LDLRA_1. 8 hits.
PS50068. LDLRA_2. 10 hits.
PS50092. TSP1. 25 hits.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 2 hits.
PS51233. VWFD. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSSPO_MOUSE
AccessioniPrimary (citable) accession number: Q8CG65
Secondary accession number(s): E9QMN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 99 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.