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Q2PC93

- SSPO_CHICK

UniProt

Q2PC93 - SSPO_CHICK

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Protein

SCO-spondin

Gene

SSPO

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 2 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

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

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
SCO-spondin
Gene namesi
Name:SSPO
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

Secretedextracellular space By similarity

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 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 52555237SCO-spondinPRO_0000245045Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi? ↔ 5247By similarity
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi801 – 8011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi931 – 9311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi972 – 9721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1340 – 13401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1363 ↔ 1376By similarity
Disulfide bondi1370 ↔ 1389By similarity
Disulfide bondi1383 ↔ 1397By similarity
Disulfide bondi1401 ↔ 1413By similarity
Disulfide bondi1408 ↔ 1426By similarity
Disulfide bondi1420 ↔ 1435By similarity
Disulfide bondi1440 ↔ 1452By similarity
Disulfide bondi1447 ↔ 1465By similarity
Disulfide bondi1459 ↔ 1476By similarity
Disulfide bondi1480 ↔ 1492By similarity
Disulfide bondi1487 ↔ 1505By similarity
Disulfide bondi1499 ↔ 1514By similarity
Disulfide bondi1516 ↔ 1528By similarity
Disulfide bondi1523 ↔ 1541By similarity
Disulfide bondi1535 ↔ 1550By similarity
Disulfide bondi1556 ↔ 1568By similarity
Disulfide bondi1563 ↔ 1581By similarity
Disulfide bondi1575 ↔ 1592By similarity
Glycosylationi1610 – 16101N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1617 ↔ 1629By similarity
Disulfide bondi1624 ↔ 1642By similarity
Disulfide bondi1636 ↔ 1651By similarity
Glycosylationi1652 – 16521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1655 ↔ 1668By similarity
Disulfide bondi1662 ↔ 1681By similarity
Disulfide bondi1675 ↔ 1692By similarity
Disulfide bondi1700 ↔ 1711By similarity
Disulfide bondi1706 ↔ 1724By similarity
Glycosylationi1713 – 17131N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1718 ↔ 1733By similarity
Glycosylationi1743 – 17431N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1749 ↔ 1759By similarity
Disulfide bondi1754 ↔ 1772By similarity
Disulfide bondi1766 ↔ 1789By similarity
Disulfide bondi1801 ↔ 1837By similarity
Disulfide bondi1805 ↔ 1842By similarity
Disulfide bondi1816 ↔ 1827By similarity
Glycosylationi1856 – 18561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1857 ↔ 1897By similarity
Disulfide bondi1861 ↔ 1902By similarity
Disulfide bondi1871 ↔ 1881By similarity
Disulfide bondi2003 ↔ 2042By similarity
Disulfide bondi2014 ↔ 2018By similarity
Disulfide bondi2052 ↔ 2057By similarity
Glycosylationi2125 – 21251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2162 ↔ 2310By similarity
Glycosylationi2230 – 22301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2328 ↔ 2339By similarity
Disulfide bondi2335 ↔ 2352By similarity
Disulfide bondi2346 ↔ 2361By similarity
Disulfide bondi2482 ↔ 2494By similarity
Disulfide bondi2489 ↔ 2507By similarity
Disulfide bondi2501 ↔ 2516By similarity
Disulfide bondi2539 ↔ 2551By similarity
Disulfide bondi2546 ↔ 2564By similarity
Disulfide bondi2558 ↔ 2573By similarity
Disulfide bondi2576 ↔ 2612By similarity
Disulfide bondi2587 ↔ 2591By similarity
Disulfide bondi2622 ↔ 2627By similarity
Disulfide bondi2642 ↔ 2679By similarity
Disulfide bondi2646 ↔ 2684By similarity
Disulfide bondi2657 ↔ 2669By similarity
Glycosylationi2746 – 27461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2791 ↔ 2829By similarity
Disulfide bondi2802 ↔ 2806By similarity
Disulfide bondi2839 ↔ 2843By similarity
Disulfide bondi2861 ↔ 2897By similarity
Disulfide bondi2865 ↔ 2902By similarity
Disulfide bondi2881 ↔ 2887By similarity
Disulfide bondi2917 ↔ 2952By similarity
Disulfide bondi2921 ↔ 2957By similarity
Disulfide bondi2932 ↔ 2942By similarity
Glycosylationi3011 – 30111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3042 – 30421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3061 ↔ 3099By similarity
Glycosylationi3065 – 30651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3072 ↔ 3076By similarity
Disulfide bondi3109 ↔ 3114By similarity
Glycosylationi3136 – 31361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3238 – 32381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3248 – 32481N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3270 ↔ 3303By similarity
Disulfide bondi3274 ↔ 3308By similarity
Disulfide bondi3285 ↔ 3293By similarity
Glycosylationi3350 – 33501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3366 – 33661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3392 – 33921N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3422 ↔ 3468By similarity
Disulfide bondi3426 ↔ 3474By similarity
Disulfide bondi3437 ↔ 3449By similarity
Disulfide bondi3489 ↔ 3524By similarity
Disulfide bondi3492 ↔ 3531By similarity
Disulfide bondi3502 ↔ 3514By similarity
Glycosylationi3598 – 35981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3625 – 36251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3656 ↔ 3693By similarity
Disulfide bondi3660 ↔ 3699By similarity
Disulfide bondi3671 ↔ 3683By similarity
Disulfide bondi3714 ↔ 3745By similarity
Disulfide bondi3718 ↔ 3750By similarity
Disulfide bondi3729 ↔ 3735By similarity
Glycosylationi3823 – 38231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3869 – 38691N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3890 ↔ 3928By similarity
Disulfide bondi3894 ↔ 3933By similarity
Disulfide bondi3906 ↔ 3918By similarity
Disulfide bondi3963 ↔ 3998By similarity
Disulfide bondi3967 ↔ 4003By similarity
Disulfide bondi3982 ↔ 3988By similarity
Glycosylationi4018 – 40181N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4019 ↔ 4055By similarity
Disulfide bondi4030 ↔ 4034By similarity
Disulfide bondi4068 ↔ 4073By similarity
Disulfide bondi4088 ↔ 4125By similarity
Disulfide bondi4092 ↔ 4130By similarity
Disulfide bondi4103 ↔ 4115By similarity
Glycosylationi4174 – 41741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4211 – 42111N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4231 ↔ 4266By similarity
Disulfide bondi4242 ↔ 4246By similarity
Disulfide bondi4276 ↔ 4281By similarity
Glycosylationi4362 – 43621N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4387 ↔ 4417By similarity
Disulfide bondi4398 ↔ 4400By similarity
Disulfide bondi4427 ↔ 4432By similarity
Glycosylationi4428 – 44281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4498 – 44981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4548 ↔ 4601By similarity
Disulfide bondi4551 ↔ 4607By similarity
Disulfide bondi4575 ↔ 4591By similarity
Disulfide bondi4611 ↔ 4646By similarity
Disulfide bondi4622 ↔ 4626By similarity
Disulfide bondi4656 ↔ 4661By similarity
Glycosylationi4730 – 47301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4747 – 47471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4752 – 47521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4774 ↔ 4809By similarity
Disulfide bondi4778 ↔ 4814By similarity
Disulfide bondi4789 ↔ 4798By similarity
Disulfide bondi4818 ↔ 4852By similarity
Disulfide bondi4829 ↔ 4833By similarity
Disulfide bondi4863 ↔ 4868By similarity
Glycosylationi4867 – 48671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4939 – 49391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi4970 – 49701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi4980 ↔ 5017By similarity
Disulfide bondi4991 ↔ 4995By similarity
Disulfide bondi5027 ↔ 5032By similarity
Glycosylationi5081 – 50811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi5122 – 51221N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi5161 ↔ 5209By similarity
Glycosylationi5169 – 51691N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi5175 ↔ 5226By similarity
Disulfide bondi5185 ↔ 5242By similarity
Disulfide bondi5189 ↔ 5244By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ2PC93.

Interactioni

Protein-protein interaction databases

STRINGi9031.ENSGALP00000038585.

Structurei

3D structure databases

ProteinModelPortaliQ2PC93.
SMRiQ2PC93. Positions 3059-3085.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 11193EMIAdd
BLAST
Domaini193 – 395203VWFD 1PROSITE-ProRule annotationAdd
BLAST
Domaini453 – 50856TIL 1Add
BLAST
Domaini508 – 60194VWFC 1PROSITE-ProRule annotationAdd
BLAST
Domaini547 – 755209VWFD 2PROSITE-ProRule annotationAdd
BLAST
Domaini809 – 86860TIL 2Add
BLAST
Domaini868 – 92659VWFC 2PROSITE-ProRule annotationAdd
BLAST
Domaini999 – 1207209VWFD 3PROSITE-ProRule annotationAdd
BLAST
Domaini1263 – 131957TIL 3Add
BLAST
Domaini1362 – 139837LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini1400 – 143637LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini1439 – 147739LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini1479 – 151537LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini1515 – 155137LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini1555 – 159339LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini1616 – 165237LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini1654 – 169340LDL-receptor class A 8PROSITE-ProRule annotationAdd
BLAST
Domaini1699 – 173436LDL-receptor class A 9PROSITE-ProRule annotationAdd
BLAST
Domaini1748 – 179043LDL-receptor class A 10PROSITE-ProRule annotationAdd
BLAST
Domaini1789 – 184355TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini1845 – 190359TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini1907 – 196155TIL 4Add
BLAST
Domaini1919 – 195638EGF-like 1Add
BLAST
Domaini1957 – 198327EGF-like 2Add
BLAST
Domaini1961 – 201959VWFC 3PROSITE-ProRule annotationAdd
BLAST
Domaini2002 – 205857TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini2058 – 212063VWFC 4PROSITE-ProRule annotationAdd
BLAST
Domaini2162 – 2310149F5/8 type CPROSITE-ProRule annotationAdd
BLAST
Domaini2327 – 236236LDL-receptor class A 11PROSITE-ProRule annotationAdd
BLAST
Domaini2481 – 251737LDL-receptor class A 12PROSITE-ProRule annotationAdd
BLAST
Domaini2538 – 257437LDL-receptor class A 13PROSITE-ProRule annotationAdd
BLAST
Domaini2575 – 262854TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini2630 – 268556TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini2708 – 275043TIL 5Add
BLAST
Domaini2790 – 284455TSP type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini2849 – 290355TSP type-1 7PROSITE-ProRule annotationAdd
BLAST
Domaini2905 – 295854TSP type-1 8PROSITE-ProRule annotationAdd
BLAST
Domaini3020 – 307758VWFC 5PROSITE-ProRule annotationAdd
BLAST
Domaini3060 – 311556TSP type-1 9PROSITE-ProRule annotationAdd
BLAST
Domaini3117 – 315842TSP type-1 10PROSITE-ProRule annotationAdd
BLAST
Domaini3165 – 321753TIL 6Add
BLAST
Domaini3217 – 327559VWFC 6PROSITE-ProRule annotationAdd
BLAST
Domaini3258 – 330952TSP type-1 11PROSITE-ProRule annotationAdd
BLAST
Domaini3410 – 347566TSP type-1 12PROSITE-ProRule annotationAdd
BLAST
Domaini3477 – 353256TSP type-1 13PROSITE-ProRule annotationAdd
BLAST
Domaini3644 – 370057TSP type-1 14PROSITE-ProRule annotationAdd
BLAST
Domaini3702 – 375150TSP type-1 15PROSITE-ProRule annotationAdd
BLAST
Domaini3878 – 393457TSP type-1 16PROSITE-ProRule annotationAdd
BLAST
Domaini3951 – 400454TSP type-1 17PROSITE-ProRule annotationAdd
BLAST
Domaini4018 – 407457TSP type-1 18PROSITE-ProRule annotationAdd
BLAST
Domaini4076 – 413156TSP type-1 19PROSITE-ProRule annotationAdd
BLAST
Domaini4230 – 428253TSP type-1 20PROSITE-ProRule annotationAdd
BLAST
Domaini4322 – 438463TSP type-1 21PROSITE-ProRule annotationAdd
BLAST
Domaini4386 – 443348TSP type-1 22PROSITE-ProRule annotationAdd
BLAST
Domaini4537 – 460872TSP type-1 23PROSITE-ProRule annotationAdd
BLAST
Domaini4610 – 466253TSP type-1 24PROSITE-ProRule annotationAdd
BLAST
Domaini4762 – 481554TSP type-1 25PROSITE-ProRule annotationAdd
BLAST
Domaini4817 – 486953TSP type-1 26PROSITE-ProRule annotationAdd
BLAST
Domaini4872 – 492655TIL 7Add
BLAST
Domaini4979 – 503355TSP type-1 27PROSITE-ProRule annotationAdd
BLAST
Domaini5092 – 515059VWFC 7PROSITE-ProRule annotationAdd
BLAST
Domaini5161 – 524888CTCKPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi737 – 7426Poly-Ala

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 13 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 27 TSP type-1 domains.PROSITE-ProRule annotation
Contains 7 VWFC domains.PROSITE-ProRule annotation
Contains 3 VWFD domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOVERGENiHBG080794.
InParanoidiQ2PC93.
PhylomeDBiQ2PC93.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
4.10.400.10. 13 hits.
InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
IPR006207. Cys_knot_C.
IPR008979. Galactose-bd-like.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR000884. Thrombospondin_1_rpt.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
IPR001007. VWF_C.
IPR001846. VWF_type-D.
[Graphical view]
PfamiPF08742. C8. 3 hits.
PF00754. F5_F8_type_C. 1 hit.
PF00057. Ldl_recept_a. 11 hits.
PF01826. TIL. 13 hits.
PF00090. TSP_1. 25 hits.
PF00093. VWC. 1 hit.
PF00094. VWD. 3 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00832. C8. 3 hits.
SM00231. FA58C. 1 hit.
SM00192. LDLa. 13 hits.
SM00209. TSP1. 27 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 3 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF57424. SSF57424. 12 hits.
SSF57567. SSF57567. 15 hits.
SSF82895. SSF82895. 25 hits.
PROSITEiPS01225. CTCK_2. 1 hit.
PS01285. FA58C_1. 1 hit.
PS01286. FA58C_2. 1 hit.
PS50022. FA58C_3. 1 hit.
PS01209. LDLRA_1. 11 hits.
PS50068. LDLRA_2. 13 hits.
PS50092. TSP1. 27 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.

Q2PC93-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MGIVATVLLW VVTEAARGRW CERTEQVTEE EVVMPRREDV VPCPSMYQYS
60 70 80 90 100
LAGWRIDLNR MRQVYGGERG VPPTSTHPGA AMCYIYRPPE TQLVVRNRTV
110 120 130 140 150
RACCAGWSGP HCTEVEGSLG QCHASWQCQD ALGAHNLSTV SMAECCRQPW
160 170 180 190 200
GHSWRNGSSA LCFACSRQPL TGDVPLPTAP RGPAARHRGP TASCTVWAGS
210 220 230 240 250
RYRSFDGRHF GFQGECAYSL AASTDSTWAV SITPGSPPVL HMTFGLDTVV
260 270 280 290 300
AQGHNISVNG VAVPEGRQHL HGGISVTWLG DFVAVESGLG VHLKLDGRGT
310 320 330 340 350
VYVTVSAELR GSTKGLCGPY NDDPIDDFLR VEGDVAPLAA SFGNSWRIPD
360 370 380 390 400
ANPELSCSDA VEPSPGCAMG STAQRAAEAM CGMLLTDPFR QCHEAVDPHG
410 420 430 440 450
FYEACLELHC REGGTGPSPP PAVCDTLATY VRDCAQRRAY IEWRRPGLCE
460 470 480 490 500
QQCGHGQRYS DCVSSCPASC MAAGTAEEGH CRDDCASGCE CTPGLLLDRG
510 520 530 540 550
ACIPQSACPC LHRGHIYAPG QSIRQRCNQC TCRGGRWLCT QDRCAAECAV
560 570 580 590 600
LGDLHYITFD RRRFSFPGAC EYTLVQDFVE GTLRITAEQE ACGGHQPLSC
610 620 630 640 650
LRALSITVPG ASARLHSTGE VVVDGRVVPL PFASAALTVR RASSSFLLLQ
660 670 680 690 700
TFGAHLLWGL ETPAAYITLQ PAFANKVRGL CGTYNWDQRD DFATPAGDVE
710 720 730 740 750
VGVTAFANKY RVSTDCPVLS PVPFEPCSTY APRRELAAAA CAILHGASFQ
760 770 780 790 800
PCHHLVDREP FHQLCLYDVC ACPAGKHCLC PALAAYAREC AQEGAALSWR
810 820 830 840 850
NESFCGTQCR GGQVYQECSS PCGRTCADLR LDGASSCPSL DNICVSGCNC
860 870 880 890 900
PEGPVLDDGG QCVPPGVCPC QHSSQLYPAG SKIRQGCNAC MCTAGTWSCT
910 920 930 940 950
DAPCPDAAFC PGDLVYVFGS CLRTCDSAEP NGTCTGIADG CVCPPGTVFL
960 970 980 990 1000
DERCVPPEEC PCQHNGRLYH PNDTIVRDCN TCVCRQQRWQ CSSEDCMGTC
1010 1020 1030 1040 1050
VATGDPHYIT FDGRAFSFLG DCEYVLVREA NGLFTVTAEN VPCGTSGVTC
1060 1070 1080 1090 1100
TKSVVVEMGN TVVHMLRGRD VTVNGVSVRP PKVYSGNGLT LQRAGIFLLL
1110 1120 1130 1140 1150
LSRLGLAVLW DGGTRVYIRL QPQHRGRVVG LCGNFDRDAE NDLASQQGVL
1160 1170 1180 1190 1200
EPTAELFGNS WRVSLLCPEV DGTTAQHPCT DNPHRATWAR KRCSILTQRL
1210 1220 1230 1240 1250
FAPCHDEVPC QHFYDWCIFD ACGCDSGGDC ECLCTAIATY AEECSQRGIH
1260 1270 1280 1290 1300
IRWRSQDLCP MQCDGGQEYS ACGPPCPQTC RNLGLELPEH CDTMSCLEGC
1310 1320 1330 1340 1350
FCPEGKVLHE GSCIDPAECP CFWQGIAFPD SAVVQQGCRN CSCTAGLWQC
1360 1370 1380 1390 1400
VPTAEPCPAQ PHCPDSEFPC RSGGRCVPGA WLCDNEDDCG DGSDEVCALH
1410 1420 1430 1440 1450
CAPHQHRCAD GQCVPWGARC DGLSDCGDGS DERGCPPPPC APPEFRCASG
1460 1470 1480 1490 1500
RCIPRAHVCN GELDCGFADD SDEAGCSPSC SVGEFQCAAG RCVPYPHRCN
1510 1520 1530 1540 1550
GHDDCGDFSD ERGCVCPAGH FQCPDAQCLP PAALCDGMQD CGDGTDEAFC
1560 1570 1580 1590 1600
PDRITCAPGQ LPCPDGSCVS QVKLCDGIWD CRDGWDESSV RCMVSWAPPA
1610 1620 1630 1640 1650
PTQLPTVPAN GTAAPVCGPY EFPCRSGQCV PRGWVCDSEA DCPDNSDELG
1660 1670 1680 1690 1700
CNRSCVLGHF PCALGAHCIH YDHLCDGIPH CPDHSDESDD NCGSTQIPPC
1710 1720 1730 1740 1750
PGHFVCNNRV CVNATRVCDG ALDCPQGEDE LACEGYVPTG ERNQTVGPCA
1760 1770 1780 1790 1800
EYSCRDGDCI TFKQVCNGLP DCRDGDMASG WLPSDEWDCG QWGPWAPWGI
1810 1820 1830 1840 1850
CSHSCGLGQQ LRARECSQRT PGVLHQCHGE ATQARPCFST ACPVDGAWSE
1860 1870 1880 1890 1900
WTMWSNCTQG CEGVVVRQRH CQPPRDGGRP CAALPATAHA TLEIGTCQQD
1910 1920 1930 1940 1950
GCPPASCPGG LQPRPCAPCP ASCADLASRA PCRREQCTPG CWCAEGLVLD
1960 1970 1980 1990 2000
GERGCVRPRE CRCEVDGLRY WPGQRMKLNC RLCTCLDGQP RRCRHNPACS
2010 2020 2030 2040 2050
VSCSWSAWSP WGECLGPCGV QSIQWSFRSP SHPGKHGTNR QCRGIYRKAR
2060 2070 2080 2090 2100
RCQTEPCQEC EHQGRSRAQG DRWRWGPCHV CQCLPGPEVR CSPYCARSAV
2110 2120 2130 2140 2150
GCPQGQVLVE GKGDSCCFCA QIGDNVTAIP TALTMEPPST MPGEPSDSPL
2160 2170 2180 2190 2200
PTFPLPSPGD PCYSPLGIAS LPDSSFTASA EQQQHPARAA RLHHVSPGLE
2210 2220 2230 2240 2250
LQGWAPPADT VPGLPSHLPF LQLDLLQTTN LTGVVVQGAG AGDAFITAFQ
2260 2270 2280 2290 2300
LQFSTDGNRW HNYQQLFQGN WDATTPVVQP LDHMVQARYI RILPQGFHNA
2310 2320 2330 2340 2350
IFLRAELLGC PTVPLDLAVT TAVTPAPCGT GEFWCGVSCV TASRRCDGAT
2360 2370 2380 2390 2400
DCPGGADEAG CEPPSSTTLP THPASLTTPG SAGILGLTAE PPVAPPAAVP
2410 2420 2430 2440 2450
EGTSAWLTVG STSPAVPSTT GLPGVPTATI TPRGPPSAGP PSPGMAAVTV
2460 2470 2480 2490 2500
SHPVMGPPAL PMPPTGVPTP TSAEPPLPRL LCPPDQFLCD ALGCVDAAMV
2510 2520 2530 2540 2550
CDGQQDCLDG SDEAHCGALP TSGSSPSPLA WPSSPPPTCS PKQFSCGTGE
2560 2570 2580 2590 2600
CLALEKRCDL SRDCADGSDE SSCADCILSP WGGWSQCSHS CGLGVTSRQR
2610 2620 2630 2640 2650
VLLRGALPGG TCHTPRLDTR ACFLRACPVP GAWAAWGVWS SCDAECGGGM
2660 2670 2680 2690 2700
RSRTRSCTDP PPKNGGQPCA GEALQSQPCN LQPCGDTREC GPGMVLVQEG
2710 2720 2730 2740 2750
DCVQGLVPPC PQVCGDLSAT SSCQSPCQEG CRCPPGLFLQ EGTCVNASQC
2760 2770 2780 2790 2800
HCHQGQQRWL PSQVFLRDGC SQCVCRDGVV TCEDTACPIA CAWSAWSLWT
2810 2820 2830 2840 2850
LCDRSCGVGM QERFRSPSNP AAANGGAPCD GDTREVRECH TPCATAEPSS
2860 2870 2880 2890 2900
GWSSWTPWSP CSRSCFHHVD QRGRRHRFRH CEGMGTCPGL GVQEEPCDTA
2910 2920 2930 2940 2950
PCPVAGVWMP WSAWSECSAP CDAGVQTRSR TCTPPAFGGA ECTGPHLQTR
2960 2970 2980 2990 3000
NCNTRPCGAQ CPDTMQYLTA EECRHSEGRC PWICQDLGAG VACTAQCQPG
3010 3020 3030 3040 3050
CHCPAGLLLQ NGTCVPPSHC LCHHRGHLYQ PGDINALDTC NNCTCVTGQM
3060 3070 3080 3090 3100
VCSTETCPVP CTWSNWTAWS TCSHSCDVGM RRRYRVPIVP PLAGGGPPCQ
3110 3120 3130 3140 3150
GPSMEVEFCS LQPCRAVAPW GPWSECSVSC GGGYRNRTRD GPPLHSLEFS
3160 3170 3180 3190 3200
TCNPAPCPGK EPGVCPPGKQ WQACAQGAAS CAELSAAPPA DGSCHPGCYC
3210 3220 3230 3240 3250
PPGALLLNNE CVAEAACPCA VDGVLYQPGD VVPQGCHNCS CIAGRVTNCS
3260 3270 3280 3290 3300
QEDCGDVDGP WTPWTPWSEC SASCGPGRQR RYRFCSAHPG VPCAEPQPQE
3310 3320 3330 3340 3350
RPCARQPCHS PDCAAVPGSV FSHCRPPCPR SCDDISHCVW HRQPGCYCTN
3360 3370 3380 3390 3400
GTLLDATGTA CVALENCTCL DAHSGQRHQP GQSVPRGDGC NNCTCTQGRL
3410 3420 3430 3440 3450
LCTGLPCPVP GAWCEWSPWT PCSRSCGDEA ATRHRVCSCP APQQGGAGCP
3460 3470 3480 3490 3500
GGLEGHGDTG MQLQHQECPS VPPCPEDGAW AAWGPWSGCG GCGGQAVRTR
3510 3520 3530 3540 3550
SCSSPPARFG GLPCAGEARQ SRACPWATSS CPECAGGLVA FTCGKPCPHS
3560 3570 3580 3590 3600
CEDLREDTAC MATPRCLPAC ACPHGQLLQD GDCVPPELCR CAWAPSKNGS
3610 3620 3630 3640 3650
IWEQDGAVPM QELQPGETVQ RHCQNCTCKS GTLQCHAEPG CRADGGWSPW
3660 3670 3680 3690 3700
GPWSPCSPGC QAGTQLASRQ CNNPTPQLGG RGCSGHSQRQ RPCPATEGCP
3710 3720 3730 3740 3750
EEEPWGEWSP WGPCSASCGG GEQLRHRDCP PPGGCPGLAL QSKTCNTHVC
3760 3770 3780 3790 3800
REAGCPPGRL YRECQQGEGC PYSCAHLAGR IACFPGGCQE GCHCPTGTLL
3810 3820 3830 3840 3850
HHGHCLQECP CVLTAEVLRK LRNSSADLQA APHLLGTRGP PLALDQELPP
3860 3870 3880 3890 3900
GSTIHSACTS CTCLHGRLNC SEPVCPRDGG FSPWGPWSSC SRSCGGLGVM
3910 3920 3930 3940 3950
TRRRGCTNPE PARGGRDCAG PRSDSKYCQS PECPAVPTTE PGPGVAGAEE
3960 3970 3980 3990 4000
EEGFGPWSPW SPCSKTCTHP ERPATKTRER PCVGTAVCSG DGFQEQPCNL
4010 4020 4030 4040 4050
PLCSDVPPCQ GEDCAGLNCS WAPWGPWTEC SRSCGVGRQQ RLRAYSPPGA
4060 4070 4080 4090 4100
SGRWCPGILS AFVQRRFCSL QACKVDGAWS AWSPWSRCDR TCGGGRAVRT
4110 4120 4130 4140 4150
RSCTRPPPKN GGQRCPGERH QLHLCNAQPC DDSCPPGMAL VTCANHCPRH
4160 4170 4180 4190 4200
CGDLQEGIVC REEEHCEPGC RCPNGTLEQD GGCVPLAHCE CTDAQGHGWV
4210 4220 4230 4240 4250
PGSTHHDGCN NCTCLEGRLR CTDRLCPPLR CPWSRWSRWS PCSVTCGDGQ
4260 4270 4280 4290 4300
QTRFRTPTAG SWDEECQGEQ MENRGCAAGP CPPLCPQGSW ERRLGDMWLQ
4310 4320 4330 4340 4350
GECQRCTCTP EGTVCEDTTC AGAEHCTWGT WSPCSRSCGT GLASREGSCP
4360 4370 4380 4390 4400
CPFPGPPGAV CNASTGDGAR PHREVQACYL RPCPAECSWS AWSSWGGCSC
4410 4420 4430 4440 4450
SSPLQHRYRH RHGTGLCVGL DVELHPCNTS GCSESSCEPP FEFQPCSPPC
4460 4470 4480 4490 4500
ARLCSTLQHP ELCPAQSHCL PGCFCPQGLL EQRSACVPPE QCDCLHTNES
4510 4520 4530 4540 4550
GDLVTLSPGD IILLGCKECV CQDGALQCSS EGCQGLLPLS PWSEWTPCST
4560 4570 4580 4590 4600
CLPLFPSHLG DATPHVSVQH RYRACLDPQS GQPWSGDTAV CSAELQQQRL
4610 4620 4630 4640 4650
CPDPDICQEL CLWSPWGPWG PCQQPCSGSF RLRHRHLQRL AGSGQCQGAQ
4660 4670 4680 4690 4700
TQSESCNTAV CPGEDCEKQG RVFATTCANS CPRACADLWQ HVECVQGGCK
4710 4720 4730 4740 4750
PGCRCPQGQL LQDGLCVPTA QCRCGLSGDN GTQELWPGQE ATIECHNCTC
4760 4770 4780 4790 4800
ENGTMVCPAL PCPSYGPWST WSPCSSSCGS GRTSRHRTCE PNPGGVPCMA
4810 4820 4830 4840 4850
SGMQETAECS PQPCPAGCQL SPWSPWSPCS SSCGGGRSER SRELLGGEEE
4860 4870 4880 4890 4900
PCPIPALRQH RVCNVHNCTQ ECPRSQVHRE CANACPHACA DLRPQTQCLP
4910 4920 4930 4940 4950
QPCQPGCACP PGQVLQDGAC VPPEECRCTL DSTMPGVLNL SREEQEQEHA
4960 4970 4980 4990 5000
PGSRLQHRCN TCICIRGTFN CSQEECNVDC LWSPWSPWSP CSVTCGMGER
5010 5020 5030 5040 5050
LSHRHPLRQR LYEGAECLGP PVRRAACHLP DCACPEGERW QGHEVPPGCE
5060 5070 5080 5090 5100
QSCRDILDET PANCTPSPSP GCTCEPGHYR NSSGHCVPST LCECLHQGQL
5110 5120 5130 5140 5150
HQPGSEWQEQ CARCRCVDGK ANCTDGCTPL SCPEGEVKVR EPGRCCPVCR
5160 5170 5180 5190 5200
MEWPEEPSSM CRRFTELRNI TKGPCSLPNV EVSFCSGRCP SRTAVTPEEP
5210 5220 5230 5240 5250
YLQTLCECCS YRLDPGSPVR ILSLPCAGGA AEPVVLPIIH SCECSSCQGG

DFSKR
Length:5,255
Mass (Da):560,556
Last modified:February 7, 2006 - v1
Checksum:iDBE892EA9AA0378B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ866919 mRNA. Translation: CAI29216.1.
RefSeqiNP_001006351.2. NM_001006351.2.
UniGeneiGga.33700.
Gga.52789.

Genome annotation databases

GeneIDi420367.
KEGGigga:420367.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ866919 mRNA. Translation: CAI29216.1 .
RefSeqi NP_001006351.2. NM_001006351.2.
UniGenei Gga.33700.
Gga.52789.

3D structure databases

ProteinModelPortali Q2PC93.
SMRi Q2PC93. Positions 3059-3085.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9031.ENSGALP00000038585.

Proteomic databases

PaxDbi Q2PC93.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 420367.
KEGGi gga:420367.

Organism-specific databases

CTDi 23145.

Phylogenomic databases

eggNOGi NOG12793.
HOVERGENi HBG080794.
InParanoidi Q2PC93.
PhylomeDBi Q2PC93.

Miscellaneous databases

NextBioi 20823284.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
4.10.400.10. 13 hits.
InterProi IPR000421. Coagulation_fac_5/8-C_type_dom.
IPR006207. Cys_knot_C.
IPR008979. Galactose-bd-like.
IPR023415. LDLR_class-A_CS.
IPR002172. LDrepeatLR_classA_rpt.
IPR000884. Thrombospondin_1_rpt.
IPR002919. TIL_dom.
IPR014853. Unchr_dom_Cys-rich.
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. 11 hits.
PF01826. TIL. 13 hits.
PF00090. TSP_1. 25 hits.
PF00093. VWC. 1 hit.
PF00094. VWD. 3 hits.
[Graphical view ]
PRINTSi PR00261. LDLRECEPTOR.
SMARTi SM00832. C8. 3 hits.
SM00231. FA58C. 1 hit.
SM00192. LDLa. 13 hits.
SM00209. TSP1. 27 hits.
SM00214. VWC. 5 hits.
SM00216. VWD. 3 hits.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF57424. SSF57424. 12 hits.
SSF57567. SSF57567. 15 hits.
SSF82895. SSF82895. 25 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. 11 hits.
PS50068. LDLRA_2. 13 hits.
PS50092. TSP1. 27 hits.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 2 hits.
PS51233. VWFD. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of SCO-spondin in chick embryos."
    Didier R.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: CNS.

Entry informationi

Entry nameiSSPO_CHICK
AccessioniPrimary (citable) accession number: Q2PC93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: February 7, 2006
Last modified: October 29, 2014
This is version 61 of the entry and version 1 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