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LNKN1_CAEEL
ID   LNKN1_CAEEL             Reviewed;         599 AA.
AC   P30639;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Protein linkin {ECO:0000303|PubMed:25437307};
DE   Flags: Precursor;
GN   Name=lnkn-1 {ECO:0000312|WormBase:ZK637.3};
GN   Synonyms=tag-256 {ECO:0000312|WormBase:ZK637.3};
GN   ORFNames=ZK637.3 {ECO:0000312|WormBase:ZK637.3};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=1538779; DOI=10.1038/356037a0;
RA   Sulston J., Du Z., Thomas K., Wilson R., Hillier L., Staden R.,
RA   Halloran N., Green P., Thierry-Mieg J., Qiu L., Dear S., Coulson A.,
RA   Craxton M., Durbin R., Berks M., Metzstein M., Hawkins T., Ainscough R.,
RA   Waterston R.;
RT   "The C. elegans genome sequencing project: a beginning.";
RL   Nature 356:37-41(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=25437307; DOI=10.7554/elife.04449;
RA   Kato M., Chou T.F., Yu C.Z., DeModena J., Sternberg P.W.;
RT   "LINKIN, a new transmembrane protein necessary for cell adhesion.";
RL   Elife 3:E04449-E04449(2014).
CC   -!- FUNCTION: Probable cell adhesion protein involved in gonadal cell
CC       migration. {ECO:0000269|PubMed:25437307}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:25437307}; Single-pass type I membrane protein
CC       {ECO:0000255}. Lateral cell membrane {ECO:0000269|PubMed:25437307};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in all somatic gonadal cells including
CC       distal tip cells, anchor cell, uterine precursor cells and spermatheca
CC       precursor cells of the hermaphrodite. Also expressed in the pharynx,
CC       pharyngeal-intestinal valve, intestine, excretory cell and canal, seam
CC       cells, a subset of hypodermal cells, vulval precursor cells of the
CC       hermaphrodite and hook precursor cells in the male.
CC       {ECO:0000269|PubMed:25437307}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the somatic gonad from the L3 stage
CC       of larval development to adulthood. {ECO:0000269|PubMed:25437307}.
CC   -!- DISRUPTION PHENOTYPE: Hermaphrodites are maternal effect lethal and
CC       have elongated and strained appearing distal tip cells with abnormal
CC       migration. Male animals have detached gonadal cells that do not migrate
CC       leading to a partially elongated gonad. RNAi-mediated knockdown results
CC       in a mild defective gonad phenotype with 11% of animals having detached
CC       gonads and 17% of animals having 'stringy' gonads.
CC   -!- SIMILARITY: Belongs to the TIP family. {ECO:0000305}.
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DR   EMBL; Z11115; CAA77450.1; -; Genomic_DNA.
DR   PIR; S15789; S15789.
DR   RefSeq; NP_498963.1; NM_066562.4.
DR   AlphaFoldDB; P30639; -.
DR   BioGRID; 41454; 1.
DR   STRING; 6239.ZK637.3; -.
DR   EPD; P30639; -.
DR   PaxDb; P30639; -.
DR   PeptideAtlas; P30639; -.
DR   PRIDE; P30639; -.
DR   EnsemblMetazoa; ZK637.3.1; ZK637.3.1; WBGene00014023.
DR   GeneID; 176253; -.
DR   UCSC; ZK637.3; c. elegans.
DR   CTD; 176253; -.
DR   WormBase; ZK637.3; CE00434; WBGene00014023; lnkn-1.
DR   eggNOG; KOG4550; Eukaryota.
DR   GeneTree; ENSGT00390000013367; -.
DR   HOGENOM; CLU_020272_2_0_1; -.
DR   InParanoid; P30639; -.
DR   OMA; PGDWIPW; -.
DR   OrthoDB; 790976at2759; -.
DR   PhylomeDB; P30639; -.
DR   PRO; PR:P30639; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00014023; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:WormBase.
DR   GO; GO:0005886; C:plasma membrane; HDA:WormBase.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR024881; Tip.
DR   PANTHER; PTHR13412; PTHR13412; 1.
DR   Pfam; PF13517; FG-GAP_3; 1.
DR   SUPFAM; SSF69318; SSF69318; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Glycoprotein; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..599
FT                   /note="Protein linkin"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000065529"
FT   TOPO_DOM        20..553
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        554..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        575..599
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        378
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   599 AA;  67593 MW;  38A3C5FD25A81972 CRC64;
     MKKILPIIWL INLVSGSLSL EKKAPDLLGK VCAFGDFNAD RNTDILVFAN GTLTINYQET
     KLLDVLEASK FTPGTSFAIS KPSLNADFVE CSVGDFNGDS RLDVLVSIRD KDTEIYNHTL
     WTSEIEDEKE IFRPFHVAML QQHAMAIDVS DDGWTDVLGF YPNGSMFCTG FNKEGKYNLL
     VNGCKHEFVA FPEKLNIYPG MPHLFVDLNS DLIADIVFMT KESDGSLFMS VWQKTKISWQ
     FRDWVPKLTP AQYPFVGAPV VMDVDSDGEL DILVPICRED ECSHITQMAS WSKTKLWGLV
     ACDMQDYTVI KEPFSRVIFR VGEFSLDSFP DMVVIAQATR ANTRPVIKVM DNAECTKCEK
     NGTRRFEIRA QENIQPKNMS LGVIKMGTFF DLLEDGSLDL LVEYEYGGQT RFGFIYCPDK
     GDTTFLKVQV FTGVCSDRCN PKSNEIGSSI SMTGACASFS MTDGWGGSTQ SVACQVPASS
     NRALYLPFLL YGLGRSPNFV DELNIAIPKY ADRKEDWKHS LKQIVPNSRI IVLPPSDQYP
     HWTSRLYVTP SALIVQSLAV IALVCCMLLM VVVFLHYREK KEDRYERQQQ SHRFHFDAM
 
 
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