ID   LIN13_CAEEL             Reviewed;        2248 AA.
AC   Q11107; Q9NBV2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Zinc finger protein lin-13;
DE   AltName: Full=Abnormal cell lineage protein 13;
GN   Name=lin-13; ORFNames=C03B8.4;
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], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP   524-SER--ASP-2248 AND 857-ARG--ASP-2248.
RX   PubMed=10880475; DOI=10.1093/genetics/155.3.1127;
RA   Melendez A., Greenwald I.;
RT   "Caenorhabditis elegans lin-13, a member of the LIN-35 Rb class of genes
RT   involved in vulval development, encodes a protein with zinc fingers and an
RT   LXCXE motif.";
RL   Genetics 155:1127-1137(2000).
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, INTERACTION WITH HPL-2, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF VAL-442 AND VAL-444.
RX   PubMed=16890929; DOI=10.1016/j.ydbio.2006.04.474;
RA   Coustham V., Bedet C., Monier K., Schott S., Karali M., Palladino F.;
RT   "The C. elegans HP1 homologue HPL-2 and the LIN-13 zinc finger protein form
RT   a complex implicated in vulval development.";
RL   Dev. Biol. 297:308-322(2006).
RN   [4]
RP   FUNCTION, AND MUTAGENESIS OF 857-ARG--ASP-2248.
RX   PubMed=24715729; DOI=10.1073/pnas.1321698111;
RA   Kozlowski L., Garvis S., Bedet C., Palladino F.;
RT   "The Caenorhabditis elegans HP1 family protein HPL-2 maintains ER
RT   homeostasis through the UPR and hormesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:5956-5961(2014).
CC   -!- FUNCTION: Involved in repression of vulval fate, possibly by a tumor
CC       suppressor protein Rb-mediated mechanism (PubMed:10880475,
CC       PubMed:16890929). May act in a common pathway with retinoblastoma-like
CC       protein homolog lin-35 and hpl-2 to influence the ER stress response in
CC       the intestine (PubMed:24715729). Plays a role in recruiting chromobox
CC       protein homolog hpl-2 to specific chromatin sites (PubMed:16890929).
CC       {ECO:0000269|PubMed:10880475, ECO:0000269|PubMed:16890929,
CC       ECO:0000269|PubMed:24715729}.
CC   -!- SUBUNIT: Interacts (via PLVPV motif) with chromobox protein homolog
CC       hpl-2 (via chromo (shadow subtype) domain); the interaction is direct
CC       and influences localization of hpl-2 to nuclear foci.
CC       {ECO:0000269|PubMed:16890929}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10880475,
CC       ECO:0000269|PubMed:16890929}. Note=Localization to nuclear foci
CC       overlaps partially with chromobox protein homolog hpl-2.
CC       {ECO:0000269|PubMed:16890929}.
CC   -!- TISSUE SPECIFICITY: In the L3 stage, expressed in syncytial hypodermal
CC       cell 7, body wall muscles, intestinal cells, distal tip cells and many
CC       neurons. {ECO:0000269|PubMed:10880475}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       {ECO:0000269|PubMed:10880475}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes various defects,
CC       including sterility, multiple vulvae, protruding vulva and arrested
CC       larvae (PubMed:10880475). Abolishes many hpl-2 nuclear foci
CC       (PubMed:16890929). Causes ectopic up-regulation of transcription of
CC       specific genes, such as lin-39 and lag-2 (PubMed:16890929).
CC       {ECO:0000269|PubMed:10880475, ECO:0000269|PubMed:16890929}.
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DR   EMBL; AF245435; AAF87497.1; -; mRNA.
DR   EMBL; FO080307; CCD62760.1; -; Genomic_DNA.
DR   PIR; T15390; T15390.
DR   RefSeq; NP_498678.3; NM_066277.4.
DR   AlphaFoldDB; Q11107; -.
DR   BioGRID; 41291; 9.
DR   STRING; 6239.C03B8.4; -.
DR   iPTMnet; Q11107; -.
DR   EPD; Q11107; -.
DR   PaxDb; Q11107; -.
DR   PeptideAtlas; Q11107; -.
DR   EnsemblMetazoa; C03B8.4.1; C03B8.4.1; WBGene00003002.
DR   GeneID; 176083; -.
DR   KEGG; cel:CELE_C03B8.4; -.
DR   UCSC; C03B8.4; c. elegans.
DR   CTD; 176083; -.
DR   WormBase; C03B8.4; CE30419; WBGene00003002; lin-13.
DR   eggNOG; KOG1721; Eukaryota.
DR   HOGENOM; CLU_001170_0_0_1; -.
DR   InParanoid; Q11107; -.
DR   OMA; FCDHFDS; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q11107; -.
DR   PRO; PR:Q11107; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003002; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0040027; P:negative regulation of vulval development; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0000003; P:reproduction; IGI:WormBase.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 22.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..2248
FT                   /note="Zinc finger protein lin-13"
FT                   /id="PRO_0000046888"
FT   ZN_FING         503..525
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         812..837
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         959..982
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1140..1162
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1556..1578
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1601..1623
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1657..1680
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1859..1900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           440..444
FT                   /note="Required for interaction with hpl-2 isoform a"
FT                   /evidence="ECO:0000269|PubMed:16890929"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        606..636
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..652
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1859..1895
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         442..444
FT                   /note="VPV->DPE: Abolishes interaction with hpl-2."
FT                   /evidence="ECO:0000269|PubMed:16890929"
FT   MUTAGEN         524..2248
FT                   /note="Missing: In n387; defects in vulval developmental.
FT                   Multiple vulvae in different genetic backgrounds, either
FT                   with lin-8, or lin-15, or lin-38 mutants, when grown at 15
FT                   degrees Celsius."
FT                   /evidence="ECO:0000269|PubMed:10880475"
FT   MUTAGEN         857..2248
FT                   /note="Missing: In n388; defects in vulval developmental.
FT                   Increased resistance to ER stress."
FT                   /evidence="ECO:0000269|PubMed:10880475,
FT                   ECO:0000269|PubMed:24715729"
SQ   SEQUENCE   2248 AA;  253418 MW;  26D95E6A96442321 CRC64;
     MDEFELFQQL NQTAPLVKTE EPEVPDEFQQ ANNNQSAPLR TGLSDLSHEI AAAKQREEEE
     AQRLADFMQK DMKEPAVKRK RGSEEYKKDP LESKAPLSTF GHSSRPRRSV NYASIERGDE
     AQAQSLVTDF GSRGNRKKPK RTRDELDENY MEENEGNSGR KKKPNAKGAS RQFQVPGLPT
     YASQYSRPPK QEDVFKTIVP LAEDARAEGE RVIGFRLDSQ PAVRRASGGF RRFCAWLSDN
     QIFSIMQTVD KLCIVGANNE DHDEILLKSI RHVYNAMPPT FRRDWEYAAR KDVFDSRLFV
     QNMPMPLSEI SVTDPRHPPS PIARGTTVRP NCCENQPLFL NMCETIEHYL GHHDVVHLFG
     CDICYRVYPS RYELTKHDCK EFAEYLRQLT FKQQTLHLEA AYMYLCCSQC GLWLSVKPSG
     EGKKGWTYFA TALMNHSCQP LVPVVAYFPK PLKDEGKGIR IQFQVMSELN IGLPLSCSEC
     NIEEFHSVVE IEEHFKEKHE ANHTCIKCGK TFGTEFMLKH HAQSHTTQTA QFANYLQMSA
     TYQPPPSSGR LPYVGFGSSI PAIGGLTSGE VQALEASENK KSEFVEPDEY TIRKKLLRWK
     HAKTKKENRN ITDSNEKEFS YEPGESSGEE DFQKSLLEQD NQSSSSSDSD SDSDDFTSSK
     QKKKRNIKIR GDLGYEHINR NKFFERPESE KEARKRIEKV YKKHVLLSRE RLLDPEEALR
     ILEESRMVHL NSIQSTLADD IAMSCIRTIS LPASNCIDPL KDLLLVNKIF YFCTKCNYIF
     SKDPVVHCLS CEVTEDDLIE VYHAASGPHA GVRCIDPECK AHLCSVISLK THLSDVHSKQ
     ATLELVSGEL DNFSENRFDR SLMLMAKHFT QLQFDERTYL ARFTDIECFM PFSGLLEAKD
     QPRPMPIRQQ PQQIKPAYSL VRPDIIAPNE LMRPYTLTPA IRPGQRIKPY KVPRTSRWYS
     CSWCDREYES LNQFVDHLTR FHTHPCPSCG KAFSSQNTRR THVCSRLFAE IKGRGATLCG
     QCPSCPEIHQ VERIFVHMLN RHFSTIEYVL ATGELLPPAR DVGIRYNHGE NGGYGRSYES
     LRAIEQSVVD PRSPDYRLKQ VKISALPIHG VELNRLPARD PPMGSFTVCP PKDKNIDPRL
     MCYMCELTFD SYDELTHHMD DHPEKWANCP FCAANTPTHF DLQKHLIQEH VVQISGQACC
     AFCQEHHRFM SSHILFRCKR VSRCTICGVK SNDPLANRVH IQRSHALTLR RFQCAYCIKV
     FVSVGEYYEH ECASGGGRVY SCTCSPNKFF NSPIEFCDHF DSVHILRNKC QLCSYDAPSQ
     DGMVKHRKTH MRSGCPKEQT KKLFILMKCL FPKHNSGYMR FIEGGPVPAS YQDVDRSQMN
     YLMCNMGTVS PSCHKSYAQA PRTLLEALEG VASDSRSGGL QKVVNVTTRM NEPSSSDVIM
     LSDDEDDDCV VFEKAVPNGV AQGSSTSTPN PESSINCEVR VETSQAGYGG AQQPGYVDED
     DTDLEVAQGG KSPYGEPVVK EVVDENGDDE LAVVAEVENS TGTLPSSISA GREKKFKCQK
     CSLAFYTNGS LESHMRDHRQ DAGAQLCTET YGIPVVTKAS WLCRNCCVVF ENQPKYQKHM
     AIHGDTCLTC IHCSGIAFNH TAIQNHMKSH EEKKVRYSCG TCLCTFASDL ALFDHLSVAH
     GVSLYYFCKV CGFGSTSADS VFQHISIHNG HNYSLVQRFG ACPAQLLNYD PTDELEFRSQ
     ILNKTIQLVS PSDCSHRSML LQCETVVSCK TCHCTQAWFN YMAFNNHSEE TGFPQFKNVD
     LANDYRRDFP LSRHLNERNA LSMSQFGNAK HGSANHSHGQ AQPNKRTFRH EVPYRTAAPR
     SSLQTNGSSM GSVTTNGGRV VRPSPPNSMN VTLRRAPPQQ APPRRIVIAN SAPNNTNVLR
     NHVAVTTKCQ FKDCDKVLHS EFDRQLHSMH SSNSSWFCRQ CGHSPKSEID LFLHYIQVHL
     KPAYDKHQSN SFKSNVFHLK CPIRSCTSPE FQSPKAFEKH MRTAHAAELP FEASCCDARF
     ASKALCVKHD QEHASFLDSN GTDASCCPIC GSLSMWSLPK DPHTDCLQSH IIRHGLDYRS
     SCRQCLKQFP ADVNQDQVIA HILDTHGMSM HGNTFHCNLC TTGTKTVEEF AEHCRKAHVF
     HILVKSSHST RGELVVTTGQ EYENYVGLKS VTRASLNSIS SQRASNAGET AQPSVLCAGS
     GNAALLTIAA AIGEPETSNN TAEVLTLD