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P14585

- LIN12_CAEEL

UniProt

P14585 - LIN12_CAEEL

Protein

Protein lin-12

Gene

lin-12

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    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. cell-cell signaling involved in cell fate commitment Source: WormBase
    2. cell fate specification Source: WormBase
    3. dauer exit Source: WormBase
    4. nematode larval development Source: WormBase
    5. Notch signaling pathway Source: WormBase
    6. oviposition Source: WormBase
    7. vulval development Source: WormBase

    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

    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

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

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

    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

    1
    1429
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14585.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini16 – 908893ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini932 – 1429498CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei909 – 93123HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

    Contains 5 ANK repeats.PROSITE-ProRule annotation
    Contains 13 EGF-like domains.PROSITE-ProRule annotation
    Contains 3 LNR (Lin/Notch) repeats.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 151 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