LIN2_CAEEL
ID LIN2_CAEEL Reviewed; 961 AA.
AC P54936;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Protein lin-2;
DE AltName: Full=Abnormal cell lineage protein 2;
GN Name=lin-2; ORFNames=F17E5.1;
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 [MRNA] (ISOFORMS LIN-2A AND LIN-2B).
RC STRAIN=Bristol N2;
RX PubMed=8565857; DOI=10.1242/dev.122.1.97;
RA Hoskins R., Hajnal A.F., Harp S.A., Kim S.K.;
RT "The C. elegans vulval induction gene lin-2 encodes a member of the MAGUK
RT family of cell junction proteins.";
RL Development 122:97-111(1996).
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).
CC -!- FUNCTION: May play a structural role in the induction of the vulva. May
CC be required for the localization of signal transduction molecules (such
CC as let-23 receptor) to either the basal membrane domain or the cell
CC junctions.
CC -!- INTERACTION:
CC P54936; Q18624: gmeb-3; NbExp=3; IntAct=EBI-315019, EBI-319798;
CC P54936; O17583: lin-10; NbExp=5; IntAct=EBI-315019, EBI-313389;
CC P54936; Q9U245: lin-7; NbExp=4; IntAct=EBI-315019, EBI-319872;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Lin-2a;
CC IsoId=P54936-1; Sequence=Displayed;
CC Name=Lin-2b;
CC IsoId=P54936-2; Sequence=VSP_003154, VSP_003155;
CC -!- SIMILARITY: Belongs to the MAGUK family. {ECO:0000305}.
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DR EMBL; X92564; CAA63314.1; -; mRNA.
DR EMBL; X92565; CAA63315.1; -; mRNA.
DR EMBL; Z50873; CAA90759.2; -; Genomic_DNA.
DR EMBL; Z50873; CAA90760.2; -; Genomic_DNA.
DR PIR; T21072; T21072.
DR PIR; T21073; T21073.
DR RefSeq; NP_001024587.1; NM_001029416.2. [P54936-1]
DR RefSeq; NP_001024588.1; NM_001029417.2. [P54936-2]
DR AlphaFoldDB; P54936; -.
DR SMR; P54936; -.
DR BioGRID; 46305; 51.
DR IntAct; P54936; 58.
DR MINT; P54936; -.
DR STRING; 6239.F17E5.1a; -.
DR EPD; P54936; -.
DR PaxDb; P54936; -.
DR PeptideAtlas; P54936; -.
DR EnsemblMetazoa; F17E5.1a.1; F17E5.1a.1; WBGene00002991. [P54936-1]
DR EnsemblMetazoa; F17E5.1b.1; F17E5.1b.1; WBGene00002991. [P54936-2]
DR GeneID; 181400; -.
DR KEGG; cel:CELE_F17E5.1; -.
DR UCSC; F17E5.1b; c. elegans. [P54936-1]
DR CTD; 181400; -.
DR WormBase; F17E5.1a; CE27131; WBGene00002991; lin-2. [P54936-1]
DR WormBase; F17E5.1b; CE27132; WBGene00002991; lin-2. [P54936-2]
DR eggNOG; KOG0033; Eukaryota.
DR eggNOG; KOG0609; Eukaryota.
DR GeneTree; ENSGT00940000169045; -.
DR HOGENOM; CLU_001715_5_3_1; -.
DR InParanoid; P54936; -.
DR OMA; VAVHEVY; -.
DR OrthoDB; 95102at2759; -.
DR PhylomeDB; P54936; -.
DR Reactome; R-CEL-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-6794361; Neurexins and neuroligins.
DR SignaLink; P54936; -.
DR PRO; PR:P54936; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00002991; Expressed in larva and 3 other tissues.
DR GO; GO:0030054; C:cell junction; IDA:WormBase.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:WormBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0040026; P:positive regulation of vulval development; IMP:WormBase.
DR GO; GO:0009791; P:post-embryonic development; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:1903361; P:protein localization to basolateral plasma membrane; IMP:WormBase.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central.
DR DisProt; DP01436; -.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR014775; L27_C.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF02828; L27; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00569; L27; 2.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS51022; L27; 2.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..961
FT /note="Protein lin-2"
FT /id="PRO_0000094572"
FT DOMAIN 17..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 365..422
FT /note="L27 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 428..479
FT /note="L27 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 545..620
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 633..717
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 774..946
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 310..320
FT /note="Calmodulin-binding"
FT REGION 318..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..341
FT /note="Missing (in isoform Lin-2b)"
FT /evidence="ECO:0000303|PubMed:8565857"
FT /id="VSP_003154"
FT VAR_SEQ 342..409
FT /note="PGGDCCHRGESSSNDAAEPPADKDLSGAYKVLGSLDAINSLLDPNSYKPGST
FT TFQKIHDDGSVRNLLR -> MSSAATPPPMEHTSSEDSTTAPLQTPSSSSCLDVTVAVG
FT TSVSYLKASPLVSSPTSLVVDITESSSTL (in isoform Lin-2b)"
FT /evidence="ECO:0000303|PubMed:8565857"
FT /id="VSP_003155"
SQ SEQUENCE 961 AA; 108812 MW; 097D4B237AA0E788 CRC64;
MRELDPDESN LLLDEQLSIR DVIEQGPFSN VYRILHGPSN RKFLLRSINL NLFRQHTGLG
FEEIDEEIRI CQNLQHPYIC RLEKTINSVH YRHIIFENME GNDICFEIVQ RASNGFVFSE
YVVSHYTRQL LDALDYCHTR KIVHRDVRPH NLVLASKDTS APLKLCGFGV AKDLSEIGGS
MACGRVGVPQ FMAPEIVRKD RVSCSSDIWS SGVVLFLLLA GRLPFSGSTS DIYERIMQTD
VDVDGYMPNI SESARNLVRR MLNADPSKRI SAKEALNHEW IRDKEHMASR KHMNDVIDQM
RRYNESRKLK SNVLSAVNSG RFDETTPRQD TPQTAFVDGS SPGGDCCHRG ESSSNDAAEP
PADKDLSGAY KVLGSLDAIN SLLDPNSYKP GSTTFQKIHD DGSVRNLLRL YDKIKALPCE
PVVTEVDTST LRKETLNQID GLLGPSPEAL ELRQLLNSPH LASCVQALDV VVCEIRDPKN
EASGSGDKEG NCVSSDPAPA YLNGGVLPLG AQRAGTSFEH FNQSAVHTSY DEEEEELYDC
MSRLRLVQFQ KDTQEPMGIT LKVNEDGRCF VARIMHGGMI HRQATLHVGD EIREINGMSV
ANRSVESLQE MLRDARGQVT FKIIPSYRSA PPACEIFVRA QFDYEPSQDD LIPCPQAGIP
FKTGDILQVI SKDDHNWWQA RFVSSFPSIG NSSNAQRSNQ QQVAGLIPSP ELQEWRTACL
AMERSKNTCN THCMWFNKKK KYYTTKYLQK HSALFDQLDL VTYEEVMRLS QYRRKTLVLL
GAHGVGRRHI KNTLIHRHPN RFAYPIPHTT RPPRKDEVDG KHYYFVTNEQ MMADIQNNEY
LEYGTHEESM YGTKLETIRN IHKSGKIAIL DVEPQALKVL RTAEYSPFVV FIAAPNLQGM
QDPDGSLEKL LNESDVLRQA FGHLFDFIIT NSDIDDTIAQ LERLVEKLPA YPQWLPVTWV
Y
