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P14585 (LIN12_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein lin-12
Alternative name(s):
Abnormal cell lineage protein 12
Gene names
Name:lin-12
ORF Names:R107.8
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length1429 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4

Subunit structure

Interacts with sel-10. Ref.5

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Contains 5 ANK repeats.

Contains 13 EGF-like domains.

Contains 3 LNR (Lin/Notch) repeats.

Ontologies

Keywords
   Biological processDifferentiation
   Cellular componentMembrane
   DomainANK repeat
EGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNotch signaling pathway

Inferred from sequence or structural similarity Ref.1. Source: WormBase

cell fate specification

Inferred from mutant phenotype PubMed 6616618. Source: WormBase

cell-cell signaling involved in cell fate commitment

Inferred from mutant phenotype PubMed 2736627. Source: WormBase

dauer exit

Inferred from genetic interaction PubMed 18599512. Source: WormBase

nematode larval development

Inferred from genetic interaction PubMed 1769331. Source: WormBase

oviposition

Inferred from mutant phenotype PubMed 8293978. Source: WormBase

vulval development

Inferred from mutant phenotype PubMed 11861555. Source: WormBase

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 16236769PubMed 9671583. Source: WormBase

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay PubMed 22901814PubMed 24512688. Source: WormBase

plasma membrane

Inferred from direct assay PubMed 24512688PubMed 9671583. Source: WormBase

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

transmembrane signaling receptor activity

Inferred from sequence or structural similarity Ref.1. Source: WormBase

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

sel-10Q937943EBI-326049,EBI-323098

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – 14291414Protein lin-12
PRO_0000007634

Regions

Topological domain16 – 908893Extracellular Potential
Transmembrane909 – 93123Helical; Potential
Topological domain932 – 1429498Cytoplasmic Potential
Domain20 – 6142EGF-like 1
Domain114 – 15037EGF-like 2
Domain152 – 19039EGF-like 3; calcium-binding Potential
Domain201 – 24646EGF-like 4
Domain250 – 28536EGF-like 5
Domain287 – 32337EGF-like 6
Domain323 – 36341EGF-like 7
Domain365 – 40238EGF-like 8; calcium-binding Potential
Domain404 – 44138EGF-like 9
Domain449 – 49244EGF-like 10
Domain503 – 54139EGF-like 11
Domain543 – 57937EGF-like 12
Domain582 – 61938EGF-like 13
Repeat638 – 67437LNR 1
Repeat678 – 70932LNR 2
Repeat716 – 75439LNR 3
Repeat1093 – 112230ANK 1
Repeat1126 – 115833ANK 2
Repeat1162 – 119433ANK 3
Repeat1206 – 123631ANK 4
Repeat1240 – 126930ANK 5

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Glycosylation6231N-linked (GlcNAc...) Potential
Glycosylation7511N-linked (GlcNAc...) Potential
Glycosylation7541N-linked (GlcNAc...) Potential
Glycosylation9001N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 35 By similarity
Disulfide bond29 ↔ 49 By similarity
Disulfide bond51 ↔ 60 By similarity
Disulfide bond118 ↔ 129 By similarity
Disulfide bond123 ↔ 138 By similarity
Disulfide bond140 ↔ 149 By similarity
Disulfide bond156 ↔ 169 By similarity
Disulfide bond163 ↔ 178 By similarity
Disulfide bond180 ↔ 189 By similarity
Disulfide bond205 ↔ 227 By similarity
Disulfide bond221 ↔ 234 By similarity
Disulfide bond236 ↔ 245 By similarity
Disulfide bond254 ↔ 264 By similarity
Disulfide bond259 ↔ 273 By similarity
Disulfide bond275 ↔ 284 By similarity
Disulfide bond291 ↔ 302 By similarity
Disulfide bond296 ↔ 311 By similarity
Disulfide bond313 ↔ 322 By similarity
Disulfide bond327 ↔ 339 By similarity
Disulfide bond334 ↔ 351 By similarity
Disulfide bond353 ↔ 362 By similarity
Disulfide bond369 ↔ 381 By similarity
Disulfide bond375 ↔ 390 By similarity
Disulfide bond392 ↔ 401 By similarity
Disulfide bond408 ↔ 419 By similarity
Disulfide bond413 ↔ 429 By similarity
Disulfide bond431 ↔ 440 By similarity
Disulfide bond462 ↔ 475 By similarity
Disulfide bond469 ↔ 480 By similarity
Disulfide bond482 ↔ 491 By similarity
Disulfide bond507 ↔ 518 By similarity
Disulfide bond512 ↔ 529 By similarity
Disulfide bond531 ↔ 540 By similarity
Disulfide bond547 ↔ 558 By similarity
Disulfide bond552 ↔ 567 By similarity
Disulfide bond569 ↔ 578 By similarity
Disulfide bond586 ↔ 597 By similarity
Disulfide bond591 ↔ 607 By similarity
Disulfide bond609 ↔ 618 By similarity
Disulfide bond638 ↔ 661 By similarity
Disulfide bond643 ↔ 656 By similarity
Disulfide bond652 ↔ 668 By similarity
Disulfide bond678 ↔ 702 By similarity
Disulfide bond684 ↔ 697 By similarity
Disulfide bond693 ↔ 709 By similarity
Disulfide bond716 ↔ 742 By similarity
Disulfide bond724 ↔ 737 By similarity
Disulfide bond733 ↔ 749 By similarity

Secondary structure

............................................ 1429
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14585 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 255EDD7A62C025DB

FASTA1,429157,116
        10         20         30         40         50         60 
MRIPTICFLF LLISLSKSLH IGSCLGLICG RNGHCHAGPV NGTQTSYWCR CDEGFGGEYC 

        70         80         90        100        110        120 
EQQCDVSKCG ADEKCVFDKD YRMETCVCKD CDINGNSLLK PSCPSGYGGD DCKTQGWCYP 

       130        140        150        160        170        180 
SVCMNGGQCI GAGNRAKCAC PDGFKGERCE LDVNECEENK NACGNRSTCM NTLGTYICVC 

       190        200        210        220        230        240 
PQGFLPPDCL KPGNTSTVEF KQPVCFLEIS ADHPDGRSMY CQNGGFCDKA SSKCQCPPGY 

       250        260        270        280        290        300 
HGSTCELLEK EDSCASNPCS HGVCISFSGG FQCICDDGYS GSYCQEGKDN CVNNKCEAGS 

       310        320        330        340        350        360 
KCINGVNSYF CDCPPERTGP YCEKMDCSAI PDICNHGTCI DSPLSEKAFE CQCEPGYEGI 

       370        380        390        400        410        420 
LCEQDKNECL SENMCLNNGT CVNLPGSFRC DCARGFGGKW CDEPLNMCQD FHCENDGTCM 

       430        440        450        460        470        480 
HTSDHSPVCQ CKNGFIGKRC EKECPIGFGG VRCDLRLEIG ICSRQGGKCF NGGKCLSGFC 

       490        500        510        520        530        540 
VCPPDFTGNQ CEVNRKNGKS SLSENLCLSD PCMNNATCID VDAHIGYACI CKQGFEGDIC 

       550        560        570        580        590        600 
ERHKDLCLEN PCSNGGVCHQ HRESFSCDCP PGFYGNGCEQ EKMFRCLKST CQNGGVCINE 

       610        620        630        640        650        660 
EEKGRKCECS YGFSGARCEE KINLTGFTEK DSLLRSVCEK RKCSERANDG NCDADCNYAA 

       670        680        690        700        710        720 
CKFDGGDCSG KREPFSKCRY GNMCADFFAN GVCNQACNNE ECLYDGMDCL PAVVRCPVKI 

       730        740        750        760        770        780 
REHCASRFAN GICDPECNTN GCGFDGGDCD NETNATIITN IRITVQMDPK EFQVTGGQSL 

       790        800        810        820        830        840 
MEISSALRVT VRIQRDEEGP LVFQWNGESE MDRVKMNERQ LTEQHVLSTS ISRKIKRSAT 

       850        860        870        880        890        900 
NIGVVVYLEV QENCDTGKCL YKDAQSVVDS ISARLAKKGI DSFGIPISEA LVAEPRKSGN 

       910        920        930        940        950        960 
NTGFLSWNAL LLIGAGCLIV MVVLMLGALP GNRTRKRRMI NASVWMPPME NEEKNRKNHQ 

       970        980        990       1000       1010       1020 
SITSSQHSLL EASYDGYIKR QRNELQHYSL YPNPQGYGNG NDFLGDFNHT NLQIPTEPEP 

      1030       1040       1050       1060       1070       1080 
ESPIKLHTEA AGSYAITEPI TRESVNIIDP RHNRTVLHWI ASNSSAEKSE DLIVHEAKEC 

      1090       1100       1110       1120       1130       1140 
IAAGADVNAM DCDENTPLML AVLARRRRLV AYLMKAGADP TIYNKSERSA LHQAAANRDF 

      1150       1160       1170       1180       1190       1200 
GMMVYMLNST KLKGDIEELD RNGMTALMIV AHNEGRDQVA SAKLLVEKGA KVDYDGAARK 

      1210       1220       1230       1240       1250       1260 
DSEKYKGRTA LHYAAQVSNM PIVKYLVGEK GSNKDKQDED GKTPIMLAAQ EGRIEVVMYL 

      1270       1280       1290       1300       1310       1320 
IQQGASVEAV DATDHTARQL AQANNHHNIV DIFDRCRPER EYSMDLHIQH THQPQPSRKV 

      1330       1340       1350       1360       1370       1380 
TRAPKKQTSR SKKESASNSR DSTHLTPPPS DGSTSTPSPQ HFMNTTHTTP TSLNYLSPEY 

      1390       1400       1410       1420 
QTEAGSSEAF QPQCGAFGNG EMWYTRASTS YTQMQNEPMT RYSEPAHYF 

« Hide

References

« Hide 'large scale' references
[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]"2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans."
Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J., Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M., Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L. expand/collapse author list , Gardner A., Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M., Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C., Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A., Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M., Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K., Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L., Wilkinson-Sproat J., Wohldman P.
Nature 368:32-38(1994) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M12069 Genomic DNA. Translation: AAA70191.1.
Z14092 Genomic DNA. Translation: CAA78474.1.
PIRS06434.
RefSeqNP_499007.1. NM_066606.3.
UniGeneCel.10278.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FO1X-ray3.12E931-1301[»]
3BRDX-ray2.21D930-957[»]
3BRFX-ray2.47D938-950[»]
ProteinModelPortalP14585.
SMRP14585. Positions 120-891, 1015-1351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid41481. 19 interactions.
DIPDIP-25208N.
IntActP14585. 2 interactions.
MINTMINT-117245.
STRING6239.R107.8.

Proteomic databases

PaxDbP14585.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaR107.8; R107.8; R107.8.
GeneID176282.
KEGGcel:CELE_R107.8.
UCSCR107.8. c. elegans.

Organism-specific databases

CTD176282.
WormBaseR107.8; CE00274; WBGene00003001; lin-12.

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000112741.
InParanoidP14585.
OMAFNGGKCL.
OrthoDBEOG7992RD.
PhylomeDBP14585.

Enzyme and pathway databases

SignaLinkP14585.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. 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]
PfamPF00023. 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]
PRINTSPR01452. LNOTCHREPEAT.
SMARTSM00248. ANK. 6 hits.
SM00181. EGF. 11 hits.
SM00179. EGF_CA. 2 hits.
SM00004. NL. 3 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 1 hit.
SSF90193. SSF90193. 3 hits.
PROSITEPS50297. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP14585.
NextBio891914.
PROP14585.

Entry information

Entry nameLIN12_CAEEL
AccessionPrimary (citable) accession number: P14585
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Caenorhabditis elegans

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