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P14585

- LIN12_CAEEL

UniProt

P14585 - LIN12_CAEEL

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Protein
Protein lin-12
Gene
lin-12, R107.8
Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in several cell fate decisions that require cell-cell interactions. It is possible that lin-12 encodes a membrane-bound receptor for a signal that enables expression of the ventral uterine precursor cell fate. Activity in cell fate decisions and tumorigenesis is negatively regulated by sel-10.2 Publications

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. protein binding Source: UniProtKB
  3. transmembrane signaling receptor activity Source: WormBase

GO - Biological processi

  1. Notch signaling pathway Source: WormBase
  2. cell fate specification Source: WormBase
  3. cell-cell signaling involved in cell fate commitment Source: WormBase
  4. dauer exit Source: WormBase
  5. nematode larval development Source: WormBase
  6. oviposition Source: WormBase
  7. vulval development Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation

Enzyme and pathway databases

SignaLinkiP14585.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein lin-12
Alternative name(s):
Abnormal cell lineage protein 12
Gene namesi
Name:lin-12
ORF Names:R107.8
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940: Chromosome III

Organism-specific databases

WormBaseiR107.8; CE00274; WBGene00003001; lin-12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini16 – 908893Extracellular Reviewed prediction
Add
BLAST
Transmembranei909 – 93123Helical; Reviewed prediction
Add
BLAST
Topological domaini932 – 1429498Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: WormBase
  2. integral component of membrane Source: UniProtKB-KW
  3. nucleus Source: WormBase
  4. plasma membrane Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515 Reviewed prediction
Add
BLAST
Chaini16 – 14291414Protein lin-12
PRO_0000007634Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 35 By similarity
Disulfide bondi29 ↔ 49 By similarity
Glycosylationi41 – 411N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi51 ↔ 60 By similarity
Disulfide bondi118 ↔ 129 By similarity
Disulfide bondi123 ↔ 138 By similarity
Disulfide bondi140 ↔ 149 By similarity
Disulfide bondi156 ↔ 169 By similarity
Disulfide bondi163 ↔ 178 By similarity
Glycosylationi165 – 1651N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi180 ↔ 189 By similarity
Glycosylationi194 – 1941N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi205 ↔ 227 By similarity
Disulfide bondi221 ↔ 234 By similarity
Disulfide bondi236 ↔ 245 By similarity
Disulfide bondi254 ↔ 264 By similarity
Disulfide bondi259 ↔ 273 By similarity
Disulfide bondi275 ↔ 284 By similarity
Disulfide bondi291 ↔ 302 By similarity
Disulfide bondi296 ↔ 311 By similarity
Disulfide bondi313 ↔ 322 By similarity
Disulfide bondi327 ↔ 339 By similarity
Disulfide bondi334 ↔ 351 By similarity
Disulfide bondi353 ↔ 362 By similarity
Disulfide bondi369 ↔ 381 By similarity
Disulfide bondi375 ↔ 390 By similarity
Glycosylationi378 – 3781N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi392 ↔ 401 By similarity
Disulfide bondi408 ↔ 419 By similarity
Disulfide bondi413 ↔ 429 By similarity
Disulfide bondi431 ↔ 440 By similarity
Disulfide bondi462 ↔ 475 By similarity
Disulfide bondi469 ↔ 480 By similarity
Disulfide bondi482 ↔ 491 By similarity
Disulfide bondi507 ↔ 518 By similarity
Disulfide bondi512 ↔ 529 By similarity
Glycosylationi515 – 5151N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi531 ↔ 540 By similarity
Disulfide bondi547 ↔ 558 By similarity
Disulfide bondi552 ↔ 567 By similarity
Disulfide bondi569 ↔ 578 By similarity
Disulfide bondi586 ↔ 597 By similarity
Disulfide bondi591 ↔ 607 By similarity
Disulfide bondi609 ↔ 618 By similarity
Glycosylationi623 – 6231N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi638 ↔ 661 By similarity
Disulfide bondi643 ↔ 656 By similarity
Disulfide bondi652 ↔ 668 By similarity
Disulfide bondi678 ↔ 702 By similarity
Disulfide bondi684 ↔ 697 By similarity
Disulfide bondi693 ↔ 709 By similarity
Disulfide bondi716 ↔ 742 By similarity
Disulfide bondi724 ↔ 737 By similarity
Disulfide bondi733 ↔ 749 By similarity
Glycosylationi751 – 7511N-linked (GlcNAc...) Reviewed prediction
Glycosylationi754 – 7541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi900 – 9001N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP14585.

Interactioni

Subunit structurei

Interacts with sel-10.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
sel-10Q937943EBI-326049,EBI-323098

Protein-protein interaction databases

BioGridi41481. 19 interactions.
DIPiDIP-25208N.
IntActiP14585. 2 interactions.
MINTiMINT-117245.
STRINGi6239.R107.8.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi938 – 9414
Helixi1025 – 10317
Beta strandi1032 – 10343
Turni1042 – 10476
Helixi1056 – 10616
Helixi1072 – 108211
Helixi1097 – 11048
Helixi1107 – 11159
Helixi1130 – 11367
Helixi1140 – 11467
Helixi1150 – 11545
Helixi1166 – 11727
Helixi1178 – 118811
Helixi1197 – 11993
Beta strandi1201 – 12044
Helixi1211 – 12155
Helixi1220 – 122910
Helixi1244 – 12518
Helixi1254 – 12629
Beta strandi1272 – 12743
Helixi1277 – 12837
Helixi1287 – 12948

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FO1X-ray3.12E931-1301[»]
3BRDX-ray2.21D930-957[»]
3BRFX-ray2.47D938-950[»]
ProteinModelPortaliP14585.
SMRiP14585. Positions 46-807, 1015-1351.

Miscellaneous databases

EvolutionaryTraceiP14585.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 6142EGF-like 1
Add
BLAST
Domaini114 – 15037EGF-like 2
Add
BLAST
Domaini152 – 19039EGF-like 3; calcium-binding Reviewed prediction
Add
BLAST
Domaini201 – 24646EGF-like 4
Add
BLAST
Domaini250 – 28536EGF-like 5
Add
BLAST
Domaini287 – 32337EGF-like 6
Add
BLAST
Domaini323 – 36341EGF-like 7
Add
BLAST
Domaini365 – 40238EGF-like 8; calcium-binding Reviewed prediction
Add
BLAST
Domaini404 – 44138EGF-like 9
Add
BLAST
Domaini449 – 49244EGF-like 10
Add
BLAST
Domaini503 – 54139EGF-like 11
Add
BLAST
Domaini543 – 57937EGF-like 12
Add
BLAST
Domaini582 – 61938EGF-like 13
Add
BLAST
Repeati638 – 67437LNR 1
Add
BLAST
Repeati678 – 70932LNR 2
Add
BLAST
Repeati716 – 75439LNR 3
Add
BLAST
Repeati1093 – 112230ANK 1
Add
BLAST
Repeati1126 – 115833ANK 2
Add
BLAST
Repeati1162 – 119433ANK 3
Add
BLAST
Repeati1206 – 123631ANK 4
Add
BLAST
Repeati1240 – 126930ANK 5
Add
BLAST

Sequence similaritiesi

Contains 5 ANK repeats.
Contains 13 EGF-like domains.

Keywords - Domaini

ANK repeat, EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00740000114998.
HOGENOMiHOG000112741.
InParanoidiP14585.
OMAiFNGGKCL.
OrthoDBiEOG7992RD.
PhylomeDBiP14585.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF00023. Ank. 3 hits.
PF00008. EGF. 5 hits.
PF07645. EGF_CA. 1 hit.
PF12661. hEGF. 2 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PRINTSiPR01452. LNOTCHREPEAT.
SMARTiSM00248. ANK. 6 hits.
SM00181. EGF. 11 hits.
SM00179. EGF_CA. 2 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 1 hit.
SSF90193. SSF90193. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
PS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 12 hits.
PS01186. EGF_2. 11 hits.
PS50026. EGF_3. 13 hits.
PS01187. EGF_CA. 2 hits.
PS50258. LNR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14585-1 [UniParc]FASTAAdd to Basket

« Hide

MRIPTICFLF LLISLSKSLH IGSCLGLICG RNGHCHAGPV NGTQTSYWCR     50
CDEGFGGEYC EQQCDVSKCG ADEKCVFDKD YRMETCVCKD CDINGNSLLK 100
PSCPSGYGGD DCKTQGWCYP SVCMNGGQCI GAGNRAKCAC PDGFKGERCE 150
LDVNECEENK NACGNRSTCM NTLGTYICVC PQGFLPPDCL KPGNTSTVEF 200
KQPVCFLEIS ADHPDGRSMY CQNGGFCDKA SSKCQCPPGY HGSTCELLEK 250
EDSCASNPCS HGVCISFSGG FQCICDDGYS GSYCQEGKDN CVNNKCEAGS 300
KCINGVNSYF CDCPPERTGP YCEKMDCSAI PDICNHGTCI DSPLSEKAFE 350
CQCEPGYEGI LCEQDKNECL SENMCLNNGT CVNLPGSFRC DCARGFGGKW 400
CDEPLNMCQD FHCENDGTCM HTSDHSPVCQ CKNGFIGKRC EKECPIGFGG 450
VRCDLRLEIG ICSRQGGKCF NGGKCLSGFC VCPPDFTGNQ CEVNRKNGKS 500
SLSENLCLSD PCMNNATCID VDAHIGYACI CKQGFEGDIC ERHKDLCLEN 550
PCSNGGVCHQ HRESFSCDCP PGFYGNGCEQ EKMFRCLKST CQNGGVCINE 600
EEKGRKCECS YGFSGARCEE KINLTGFTEK DSLLRSVCEK RKCSERANDG 650
NCDADCNYAA CKFDGGDCSG KREPFSKCRY GNMCADFFAN GVCNQACNNE 700
ECLYDGMDCL PAVVRCPVKI REHCASRFAN GICDPECNTN GCGFDGGDCD 750
NETNATIITN IRITVQMDPK EFQVTGGQSL MEISSALRVT VRIQRDEEGP 800
LVFQWNGESE MDRVKMNERQ LTEQHVLSTS ISRKIKRSAT NIGVVVYLEV 850
QENCDTGKCL YKDAQSVVDS ISARLAKKGI DSFGIPISEA LVAEPRKSGN 900
NTGFLSWNAL LLIGAGCLIV MVVLMLGALP GNRTRKRRMI NASVWMPPME 950
NEEKNRKNHQ SITSSQHSLL EASYDGYIKR QRNELQHYSL YPNPQGYGNG 1000
NDFLGDFNHT NLQIPTEPEP ESPIKLHTEA AGSYAITEPI TRESVNIIDP 1050
RHNRTVLHWI ASNSSAEKSE DLIVHEAKEC IAAGADVNAM DCDENTPLML 1100
AVLARRRRLV AYLMKAGADP TIYNKSERSA LHQAAANRDF GMMVYMLNST 1150
KLKGDIEELD RNGMTALMIV AHNEGRDQVA SAKLLVEKGA KVDYDGAARK 1200
DSEKYKGRTA LHYAAQVSNM PIVKYLVGEK GSNKDKQDED GKTPIMLAAQ 1250
EGRIEVVMYL IQQGASVEAV DATDHTARQL AQANNHHNIV DIFDRCRPER 1300
EYSMDLHIQH THQPQPSRKV TRAPKKQTSR SKKESASNSR DSTHLTPPPS 1350
DGSTSTPSPQ HFMNTTHTTP TSLNYLSPEY QTEAGSSEAF QPQCGAFGNG 1400
EMWYTRASTS YTQMQNEPMT RYSEPAHYF 1429
Length:1,429
Mass (Da):157,116
Last modified:January 1, 1990 - v1
Checksum:i255EDD7A62C025DB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12069 Genomic DNA. Translation: AAA70191.1.
Z14092 Genomic DNA. Translation: CAA78474.1.
PIRiS06434.
RefSeqiNP_499007.1. NM_066606.3.
UniGeneiCel.10278.

Genome annotation databases

EnsemblMetazoaiR107.8; R107.8; WBGene00003001.
GeneIDi176282.
KEGGicel:CELE_R107.8.
UCSCiR107.8. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M12069 Genomic DNA. Translation: AAA70191.1 .
Z14092 Genomic DNA. Translation: CAA78474.1 .
PIRi S06434.
RefSeqi NP_499007.1. NM_066606.3.
UniGenei Cel.10278.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FO1 X-ray 3.12 E 931-1301 [» ]
3BRD X-ray 2.21 D 930-957 [» ]
3BRF X-ray 2.47 D 938-950 [» ]
ProteinModelPortali P14585.
SMRi P14585. Positions 46-807, 1015-1351.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 41481. 19 interactions.
DIPi DIP-25208N.
IntActi P14585. 2 interactions.
MINTi MINT-117245.
STRINGi 6239.R107.8.

Proteomic databases

PaxDbi P14585.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai R107.8 ; R107.8 ; WBGene00003001 .
GeneIDi 176282.
KEGGi cel:CELE_R107.8.
UCSCi R107.8. c. elegans.

Organism-specific databases

CTDi 176282.
WormBasei R107.8 ; CE00274 ; WBGene00003001 ; lin-12.

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00740000114998.
HOGENOMi HOG000112741.
InParanoidi P14585.
OMAi FNGGKCL.
OrthoDBi EOG7992RD.
PhylomeDBi P14585.

Enzyme and pathway databases

SignaLinki P14585.

Miscellaneous databases

EvolutionaryTracei P14585.
NextBioi 891914.
PROi P14585.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view ]
Pfami PF00023. Ank. 3 hits.
PF00008. EGF. 5 hits.
PF07645. EGF_CA. 1 hit.
PF12661. hEGF. 2 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view ]
PRINTSi PR01452. LNOTCHREPEAT.
SMARTi SM00248. ANK. 6 hits.
SM00181. EGF. 11 hits.
SM00179. EGF_CA. 2 hits.
SM00004. NL. 3 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 1 hit.
SSF90193. SSF90193. 3 hits.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
PS00010. ASX_HYDROXYL. 3 hits.
PS00022. EGF_1. 12 hits.
PS01186. EGF_2. 11 hits.
PS50026. EGF_3. 13 hits.
PS01187. EGF_CA. 2 hits.
PS50258. LNR. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Caenorhabditis elegans lin-12 gene encodes a transmembrane protein with overall similarity to Drosophila Notch."
    Yochem J., Weston K., Greenwald I.
    Nature 335:547-550(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: Bristol N2.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  3. "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.
  4. "lin-12, a nematode homeotic gene, is homologous to a set of mammalian proteins that includes epidermal growth factor."
    Greenwald I.
    Cell 43:583-590(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-712, FUNCTION.
  5. "sel-10, a negative regulator of lin-12 activity in Caenorhabditis elegans, encodes a member of the CDC4 family of proteins."
    Hubbard E.J.A., Wu G., Kitajewski J., Greenwald I.
    Genes Dev. 11:3182-3193(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SEL-10.

Entry informationi

Entry nameiLIN12_CAEEL
AccessioniPrimary (citable) accession number: P14585
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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