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Protein

Laminin-like protein epi-1

Gene

epi-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

During the formation of neuromuscular junctions at the larval stage, negatively regulates membrane protrusion from body wall muscles, probably downstream of the integrin complex formed by pat-2 and pat-3.1 Publication

GO - Biological processi

  • axonal defasciculation Source: WormBase
  • basement membrane organization Source: WormBase
  • cell adhesion Source: InterPro
  • cell migration Source: WormBase
  • neuron migration Source: WormBase
  • positive regulation of endopeptidase activity Source: WormBase
  • positive regulation of locomotion Source: WormBase
  • regulation of cell proliferation Source: WormBase
  • reproduction Source: WormBase
  • response to heat Source: WormBase
  • response to misfolded protein Source: WormBase
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin-like protein epi-1
Gene namesi
Name:epi-1
ORF Names:K08C7.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiK08C7.3b; CE06136; WBGene00001328; epi-1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: WormBase
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

RNAi-mediated knockdown in L4 larval stage, causes ectopic membrane extensions from body wall muscles.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2802 – 28021L → F in rh152; causes ectopic muscle membrane extensions. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Chaini28 – 36723645Laminin-like protein epi-1PRO_0000017100Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi121 – 1211N-linked (GlcNAc...)1 Publication
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence analysis
Glycosylationi249 – 2491N-linked (GlcNAc...)3 Publications
Disulfide bondi298 ↔ 307By similarity
Disulfide bondi300 ↔ 320By similarity
Disulfide bondi322 ↔ 331By similarity
Disulfide bondi334 ↔ 354By similarity
Glycosylationi351 – 3511N-linked (GlcNAc...)2 Publications
Disulfide bondi357 ↔ 366By similarity
Disulfide bondi359 ↔ 391By similarity
Disulfide bondi394 ↔ 403By similarity
Disulfide bondi406 ↔ 424By similarity
Disulfide bondi427 ↔ 438By similarity
Disulfide bondi429 ↔ 445By similarity
Disulfide bondi447 ↔ 456By similarity
Disulfide bondi459 ↔ 469By similarity
Disulfide bondi472 ↔ 484By similarity
Disulfide bondi474 ↔ 491By similarity
Glycosylationi477 – 4771N-linked (GlcNAc...)1 Publication
Disulfide bondi493 ↔ 502By similarity
Disulfide bondi505 ↔ 516By similarity
Glycosylationi511 – 5111N-linked (GlcNAc...)Sequence analysis
Disulfide bondi519 ↔ 531By similarity
Disulfide bondi521 ↔ 538By similarity
Glycosylationi530 – 5301N-linked (GlcNAc...)Sequence analysis
Disulfide bondi540 ↔ 549By similarity
Disulfide bondi552 ↔ 561By similarity
Disulfide bondi564 ↔ 576By similarity
Disulfide bondi566 ↔ 583By similarity
Disulfide bondi585 ↔ 594By similarity
Disulfide bondi597 ↔ 607By similarity
Disulfide bondi610 ↔ 622By similarity
Disulfide bondi612 ↔ 629By similarity
Disulfide bondi631 ↔ 640By similarity
Glycosylationi634 – 6341N-linked (GlcNAc...)1 Publication
Disulfide bondi643 ↔ 653By similarity
Disulfide bondi656 ↔ 668By similarity
Disulfide bondi658 ↔ 674By similarity
Disulfide bondi676 ↔ 685By similarity
Disulfide bondi688 ↔ 698By similarity
Disulfide bondi701 ↔ 715By similarity
Disulfide bondi703 ↔ 724By similarity
Disulfide bondi726 ↔ 735By similarity
Disulfide bondi738 ↔ 753By similarity
Disulfide bondi756 ↔ 770By similarity
Disulfide bondi758 ↔ 777By similarity
Glycosylationi761 – 7611N-linked (GlcNAc...)2 Publications
Disulfide bondi779 ↔ 788By similarity
Disulfide bondi791 ↔ 806By similarity
Disulfide bondi809 ↔ 821By similarity
Disulfide bondi811 ↔ 828By similarity
Disulfide bondi830 ↔ 839By similarity
Glycosylationi1014 – 10141N-linked (GlcNAc...)2 Publications
Glycosylationi1341 – 13411N-linked (GlcNAc...)2 Publications
Disulfide bondi1415 ↔ 1427By similarity
Disulfide bondi1417 ↔ 1434By similarity
Disulfide bondi1436 ↔ 1445By similarity
Disulfide bondi1448 ↔ 1458By similarity
Disulfide bondi1461 ↔ 1469By similarity
Disulfide bondi1463 ↔ 1476By similarity
Disulfide bondi1478 ↔ 1487By similarity
Disulfide bondi1490 ↔ 1503By similarity
Disulfide bondi1506 ↔ 1520By similarity
Disulfide bondi1508 ↔ 1527By similarity
Disulfide bondi1529 ↔ 1538By similarity
Disulfide bondi1541 ↔ 1551By similarity
Disulfide bondi1554 ↔ 1566By similarity
Disulfide bondi1556 ↔ 1573By similarity
Disulfide bondi1575 ↔ 1584By similarity
Disulfide bondi1587 ↔ 1602By similarity
Glycosylationi1705 – 17051N-linked (GlcNAc...)1 Publication
Glycosylationi1756 – 17561N-linked (GlcNAc...)2 Publications
Disulfide bondi1830 ↔ 1839By similarity
Disulfide bondi1832 ↔ 1846By similarity
Disulfide bondi1849 ↔ 1858By similarity
Disulfide bondi1861 ↔ 1877By similarity
Glycosylationi1868 – 18681N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1880 ↔ 1894By similarity
Disulfide bondi1882 ↔ 1905By similarity
Disulfide bondi1907 ↔ 1916By similarity
Disulfide bondi1919 ↔ 1934By similarity
Disulfide bondi1937 ↔ 1951By similarity
Disulfide bondi1939 ↔ 1958By similarity
Glycosylationi1944 – 19441N-linked (GlcNAc...)1 Publication
Disulfide bondi1961 ↔ 1970By similarity
Disulfide bondi1973 ↔ 1987By similarity
Glycosylationi1986 – 19861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1990 ↔ 2000By similarity
Disulfide bondi1992 ↔ 2007By similarity
Glycosylationi2002 – 20021N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2009 ↔ 2018By similarity
Disulfide bondi2021 ↔ 2034By similarity
Disulfide bondi2037 ↔ 2048By similarity
Disulfide bondi2039 ↔ 2055By similarity
Disulfide bondi2057 ↔ 2066By similarity
Disulfide bondi2069 ↔ 2081By similarity
Disulfide bondi2084 ↔ 2096By similarity
Disulfide bondi2086 ↔ 2103By similarity
Disulfide bondi2105 ↔ 2114By similarity
Disulfide bondi2117 ↔ 2129By similarity
Glycosylationi2159 – 21591N-linked (GlcNAc...)Sequence analysis
Glycosylationi2207 – 22071N-linked (GlcNAc...)1 Publication
Glycosylationi2231 – 22311N-linked (GlcNAc...)2 Publications
Glycosylationi2235 – 22351N-linked (GlcNAc...)2 Publications
Glycosylationi2401 – 24011N-linked (GlcNAc...)2 Publications
Glycosylationi2421 – 24211N-linked (GlcNAc...)Sequence analysis
Glycosylationi2487 – 24871N-linked (GlcNAc...)2 Publications
Glycosylationi2821 – 28211N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3040 ↔ 3066By similarity
Glycosylationi3087 – 30871N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3209 ↔ 3235By similarity
Glycosylationi3242 – 32421N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3460 ↔ 3482By similarity
Glycosylationi3541 – 35411N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3633 ↔ 3669By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ21313.
PaxDbiQ21313.
PRIDEiQ21313.

Expressioni

Gene expression databases

ExpressionAtlasiQ21313. baseline.

Interactioni

Protein-protein interaction databases

BioGridi43057. 8 interactions.
STRINGi6239.K08C7.3a.1.

Structurei

3D structure databases

ProteinModelPortaliQ21313.
SMRiQ21313. Positions 24-841, 1414-1585, 1796-2138, 2718-3671.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 297270Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini298 – 35659Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini357 – 42670Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini427 – 47145Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini472 – 51847Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini519 – 56345Laminin EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini564 – 60946Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini610 – 65546Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini656 – 70045Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini701 – 75555Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini756 – 80853Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini809 – 83931Laminin EGF-like 11; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini1415 – 146046Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1461 – 150545Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini1506 – 155348Laminin EGF-like 14PROSITE-ProRule annotationAdd
BLAST
Domaini1554 – 160451Laminin EGF-like 15PROSITE-ProRule annotationAdd
BLAST
Domaini1605 – 161410Laminin EGF-like 16; first partPROSITE-ProRule annotation
Domaini1615 – 1796182Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini1797 – 182933Laminin EGF-like 16; second partPROSITE-ProRule annotationAdd
BLAST
Domaini1830 – 187950Laminin EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini1880 – 193657Laminin EGF-like 18PROSITE-ProRule annotationAdd
BLAST
Domaini1937 – 198953Laminin EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini1990 – 203647Laminin EGF-like 20PROSITE-ProRule annotationAdd
BLAST
Domaini2037 – 208347Laminin EGF-like 21PROSITE-ProRule annotationAdd
BLAST
Domaini2084 – 213148Laminin EGF-like 22PROSITE-ProRule annotationAdd
BLAST
Domaini2693 – 2884192Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini2896 – 3066171Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini3072 – 3235164Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini3310 – 3482173Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini3488 – 3669182Laminin G-like 5PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 22 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 5 laminin G-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IP6A. Eukaryota.
ENOG410ZVNS. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000017472.
InParanoidiQ21313.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 21 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 3 hits.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 14 hits.
SM00180. EGF_Lam. 21 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 6 hits.
PROSITEiPS00022. EGF_1. 19 hits.
PS01186. EGF_2. 4 hits.
PS01248. EGF_LAM_1. 21 hits.
PS50027. EGF_LAM_2. 21 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q21313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPYDSSPWA TKALFLIVTL LAQFTYSQVL TPSQITISHR KPITATSTCG
60 70 80 90 100
EIQGQPVTEI YCSLTGSTQY TPLNSYSYQD DEQQKSWSQY ENPMVRGGHG
110 120 130 140 150
CGHCNAGNEN SHPAANMVDG NNSWWMSPPL SRGLQHNEVN ITIDLEQEFH
160 170 180 190 200
VAYVWIQMAN SPRPGSWVLE RSTDHGKTYQ PWFNFAENAA ECMRRFGMES
210 220 230 240 250
LSPISEDDSV TCRTDMASLQ PLENAEMVIR ILEHRPSSRQ FATSEALQNF
260 270 280 290 300
TRATNVRLRL LGTRTLQGHL MDMNEWRDPT VTRRYFYAIK EIMIGGRCVC
310 320 330 340 350
NGHAVTCDIL EPQRPKSLLC RCEHNTCGDM CERCCPGFVQ KQWQAATAHN
360 370 380 390 400
NFTCEACNCF GRSNECEYDA EVDLNKQSID SQGNYEGGGV CKNCRENTEG
410 420 430 440 450
VNCNKCSFGY FRPEGVTWNE PQPCKVCDCD PDKHTGACAE ETGKCECLPR
460 470 480 490 500
FVGEDCDQCA SGYYDAPKCK PCECNVNGTI GDVCLPEDGQ CPCKAGFGGT
510 520 530 540 550
FCETCADGYT NVTAGCVECV CDATGSEHGN CSASTGQCEC KPAYAGLSCD
560 570 580 590 600
KCQVGYFGDD CKFCNCDPMG TEGGVCDQTT GQCLCKEGFA GDKCDRCDIA
610 620 630 640 650
FYGYPNCKAC ACDGAGITSP ECDATSGQCP CNGNFTGRTC DKCAAGFYNY
660 670 680 690 700
PDCRGCECLL SGAKGQTCDS NGQCYCKGNF EGERCDRCKP NFYNFPICEE
710 720 730 740 750
CNCNPSGVTR DFQGCDKVSP GELCSCRKHV TGRICDQCKP TFWDLQYHHE
760 770 780 790 800
DGCRSCDCNV NGTISGLNTC DLKTGQCMCK KNADGRRCDQ CADGFYRLNS
810 820 830 840 850
YNQMGCESCH CDIGGALRAE CDITSGQCKC RPRVTGLRCD QPIENHYFPT
860 870 880 890 900
LWHNQYEAED AHTEDQKPVR FAVDPEQFAD FSWRGYAVFS PIQDKILIDV
910 920 930 940 950
DITKATVYRL LFRYRNPTSV PVTATVTINP RFTHTHDVEQ TGKATFAPGD
960 970 980 990 1000
LPAMKEITVD GKPFVLNPGK WSLAISTKQR LFLDYVVVLP AEYYEGTVLR
1010 1020 1030 1040 1050
QRAPQPCLSH STKNTTCVDL IYPPIPSVSR QFVDMDKVPF NYINEDGTTT
1060 1070 1080 1090 1100
ALEHVPVEIL LSEITGPAAF VRADENPRVV EAKLDVPETG EYVIVLEYHN
1110 1120 1130 1140 1150
REETDGNIGV GISQNDKEVL NGNAVIHHCP YATFCRELVS SEGTIPYIPL
1160 1170 1180 1190 1200
EKGEATVRLN IKPNHEFGLA GVQLIKKSDF SSEYLQQVPV CIKKDARCVQ
1210 1220 1230 1240 1250
QSYPPAADSV TTEAESGSNM DKSILGDKLP FPVSNSKEMR VVPLDDAQAT
1260 1270 1280 1290 1300
VEISGVVPTR GHYMFMVHYF NPDNTPINID VLIQNEHYFQ GDSCNSFACS
1310 1320 1330 1340 1350
SVPLAFCPSI SGCRALIRDK ERPEVIQFYM DDKYTATFYH NSSQKGPIYI
1360 1370 1380 1390 1400
DSITAVPYNS YKDKLMEPLA LDLSNEFLKE CSEDNLKNHP ESVSDFCKQK
1410 1420 1430 1440 1450
IFSLTTDFNA AALSCDCVAQ GSESFQCEQY GGQCKCKPGV IGRRCERCAP
1460 1470 1480 1490 1500
GYYNFPECIK CQCNAGQQCD ERTGQCFCPP HVEGQTCDRC VSNAFGYDPL
1510 1520 1530 1540 1550
IGCQKCGCHP QGSEGGNLVC DPESGQCLCR ESMGGRQCDR CLAGFYGFPH
1560 1570 1580 1590 1600
CYGCSCNRAG TTEEICDATN AQCKCKENVY GGRCEACKAG TFDLSAENPL
1610 1620 1630 1640 1650
GCVNCFCFGV TDSCRSSMYP VTIMSVDMSS FLTTDDNGMV DNKDDTVIYT
1660 1670 1680 1690 1700
SEETSPNSVY FNVPIEKKDY TTSYGLKLTF KLSTVPRGGR KSMNADADVR
1710 1720 1730 1740 1750
LTGANMTIEY WASEQPTNPE EQFTVKCKLV PENFLTAEGK TVTREELMKV
1760 1770 1780 1790 1800
LHSLQNITLK ASYFDHPKTS TLYEFGLEIS EPNGVDSVIK ASSVEQCQCP
1810 1820 1830 1840 1850
APYTGPSCQL CASGYHRVQS GSFLGACVPC ECNGHSATCD PDTGICTDCE
1860 1870 1880 1890 1900
HNTNGDHCEF CNEGHYGNAT NGSPYDCMAC ACPFAPTNNF AKSCDVSEEG
1910 1920 1930 1940 1950
QLLQCNCKPG YTGDRCDRCA SGFFGHPQIS GESCSPCQCN GNNNLTDSRS
1960 1970 1980 1990 2000
CHPNSGDCYL CEQNTDGRHC ESCAAWFYGD AVTAKNCSSC ECSQCGSQYC
2010 2020 2030 2040 2050
DNKSGGCECK INVEGDSCDR CKPDHWGFSK CQGCQGCHCG TAAFNTQCNV
2060 2070 2080 2090 2100
ENGQCTCRPG ATGMRCEHCE HGYWNYGEHG CDKCDCEADL SMGTVCDVRT
2110 2120 2130 2140 2150
GQCHCQEGAT GSRCDQCLPS YLRIPTYGCR RCDECVHHLI GDVDNLELEI
2160 2170 2180 2190 2200
DVLGTAIANI SSATIVGARL ARNKKEFNDI NEITKMLNDE ENSFGNVFGD
2210 2220 2230 2240 2250
AQDILTNSTQ IQNKLVRTKT HSQNSVSSAK NITLNGTEFL QEVMKRAQRA
2260 2270 2280 2290 2300
RQSVRSLAEI ALAIGSSSKA VNVDPRLLKE AEETLMTLEA ASADQYPEKA
2310 2320 2330 2340 2350
QTVPGKLEEI QKKIQEETEK LDKQKETFEA QKKRAEELAA YLNSAQQLLK
2360 2370 2380 2390 2400
ESKSKADKSN NIAKMLQLTK VENLVAAITD DLERVEAAKG EFQKLNVAIG
2410 2420 2430 2440 2450
NITENLKDKR EEMTHAVTTL NETRNDVAEA LEAAKKRVRR DEKSVDMQLV
2460 2470 2480 2490 2500
NAKAHELHLQ ATTLRQTFDN NKDNTDQAVE AANAFSNLTD TLKNAKAQID
2510 2520 2530 2540 2550
NAYEALSAEP AFAESVQNAR DKPFPDETKE KIDALSKTVS QDLKETEKLK
2560 2570 2580 2590 2600
KQLEQLTELS EKLRKRKEAV KAGIPKYSKN TLDSIDEKVQ EVEKLKAEID
2610 2620 2630 2640 2650
ANIEETRAKI SEIAGKAEEI TEKANSAMEG IRLARRNSVQ LNKLAPVIVS
2660 2670 2680 2690 2700
KFEELKKLSS ARSAKVDSVS DKVSQIKEMI AVARDAANRI KLGAHFEKGS
2710 2720 2730 2740 2750
SLDLNIPQRV TRSAAHADIS FYFRTEQEHG IPLFFGNEET AVGSRAVPTA
2760 2770 2780 2790 2800
DYVAAEIEYG RPKITVDLGD APAVVKLDTP VNDGLWRRLN IERIGKTVSV
2810 2820 2830 2840 2850
TLSKPNSVET AETKSSVAGG NKSVLNLNQQ ISRLFVGGVP TSARISKDLY
2860 2870 2880 2890 2900
NRDFVGDIES LKLHGEPIGL WNSREKGNTN VNGAQKKPKI TDNADELVVS
2910 2920 2930 2940 2950
LDGEGYTSYK PSHWNPRKAT KISLSFLTFS PHGLLFFVGK DKDFMALELS
2960 2970 2980 2990 3000
DGGVKLSVDL GSGVGQWITE SSNYNDGKWH TVSIVREEKH VKIMIDGETE
3010 3020 3030 3040 3050
VLEGDVPGKD SEMSVTEFLY IGGTPSGLSV RTTIVPLRGC IKSVKLGSDN
3060 3070 3080 3090 3100
VDLESSHASK GVRSGCPLHS VRTVSFLSDR TTASFNNATE FSEDVSVTFK
3110 3120 3130 3140 3150
FKTRSIRQPS SLFTVNDDED SVLSVSINED GILTVTSGED IATLELAASP
3160 3170 3180 3190 3200
DEKWHYVSIR KTKYIIRIDA DDSFSNEVAR KHADDSNPDA SFLSAFFGKS
3210 3220 3230 3240 3250
GETPSFVGCI GDVTLNGKLL DFANSEIKEI SLNGCSLSDD ENISTTTTAA
3260 3270 3280 3290 3300
PKPTDDSDVA VLPIDEEEES TTTTTTTTTE EPTEEPAEAR PDGHCSLPED
3310 3320 3330 3340 3350
PMVQFEDAEG FNFGSQQYSR IEYDILPEAI DKSGEFTFKI RPTSDNGIIF
3360 3370 3380 3390 3400
IATNKRTDHI AVMLEHGRVV FTYDTGSGQV IIKSDKSIID GRWHTIKVSR
3410 3420 3430 3440 3450
RGKSAHLIVD DNSYESEGAA NQNEDLIETQ PPFYVGGVPA DLAGFARNLV
3460 3470 3480 3490 3500
VGVRSQFSGC IKDFKLNGKS LDNGKEFGTE QCSQFSEPGM YFGKDGGYAI
3510 3520 3530 3540 3550
VQKDYEVGLT FGLEVEMRPR MKNGILFSVG VLEYITVEFV NGSIKTTVES
3560 3570 3580 3590 3600
GSGGEELWHH PDIENQYCDG QWQSFKISKK RNLLTVAVNG KAHLKILKKA
3610 3620 3630 3640 3650
KTDVLTKDPL YFGGLPEGVT NKGIKTNKPF VGCIRFVSFG LKKDRKIRRK
3660 3670
KQVDTERFDV FGDVHRNACP AI
Length:3,672
Mass (Da):404,230
Last modified:November 1, 1996 - v1
Checksum:i28E262DB5FF14BFA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z70286 Genomic DNA. Translation: CAA94293.1.
PIRiT23433.
RefSeqiNP_001023282.1. NM_001028111.3.
UniGeneiCel.18380.

Genome annotation databases

EnsemblMetazoaiK08C7.3b.1; K08C7.3b.1; WBGene00001328.
K08C7.3b.2; K08C7.3b.2; WBGene00001328.
GeneIDi177956.
UCSCiK08C7.3a. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z70286 Genomic DNA. Translation: CAA94293.1.
PIRiT23433.
RefSeqiNP_001023282.1. NM_001028111.3.
UniGeneiCel.18380.

3D structure databases

ProteinModelPortaliQ21313.
SMRiQ21313. Positions 24-841, 1414-1585, 1796-2138, 2718-3671.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi43057. 8 interactions.
STRINGi6239.K08C7.3a.1.

Proteomic databases

EPDiQ21313.
PaxDbiQ21313.
PRIDEiQ21313.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiK08C7.3b.1; K08C7.3b.1; WBGene00001328.
K08C7.3b.2; K08C7.3b.2; WBGene00001328.
GeneIDi177956.
UCSCiK08C7.3a. c. elegans.

Organism-specific databases

CTDi177956.
WormBaseiK08C7.3b; CE06136; WBGene00001328; epi-1.

Phylogenomic databases

eggNOGiENOG410IP6A. Eukaryota.
ENOG410ZVNS. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000017472.
InParanoidiQ21313.

Miscellaneous databases

PROiQ21313.

Gene expression databases

ExpressionAtlasiQ21313. baseline.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 21 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 3 hits.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 14 hits.
SM00180. EGF_Lam. 21 hits.
SM00281. LamB. 1 hit.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 6 hits.
PROSITEiPS00022. EGF_1. 19 hits.
PS01186. EGF_2. 4 hits.
PS01248. EGF_LAM_1. 21 hits.
PS50027. EGF_LAM_2. 21 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."
    Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.
    Nat. Biotechnol. 21:667-672(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.
  3. "Identification of the hydrophobic glycoproteins of Caenorhabditis elegans."
    Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.
    Glycobiology 15:952-964(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249; ASN-351; ASN-761; ASN-1014; ASN-1341; ASN-1756; ASN-2231; ASN-2235; ASN-2401 AND ASN-2487, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "FGF negatively regulates muscle membrane extension in Caenorhabditis elegans."
    Dixon S.J., Alexander M., Fernandes R., Ricker N., Roy P.J.
    Development 133:1263-1275(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LEU-2802.
  5. "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
    Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
    Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-121; ASN-249; ASN-351; ASN-477; ASN-634; ASN-761; ASN-1014; ASN-1341; ASN-1705; ASN-1756; ASN-1944; ASN-2207; ASN-2231; ASN-2235; ASN-2401 AND ASN-2487, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.

Entry informationi

Entry nameiEPI1_CAEEL
AccessioniPrimary (citable) accession number: Q21313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.