ELAP2_XENLA
ID ELAP2_XENLA Reviewed; 995 AA.
AC Q6DDW2; A0A1L8GZB8; E3WE02;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Endosome/lysosome-associated apoptosis and autophagy regulator family member 2 {ECO:0000305};
DE AltName: Full=Estrogen-induced gene 121-like protein {ECO:0000303|PubMed:17475571};
DE Short=xEIG121L {ECO:0000303|PubMed:17475571};
DE Flags: Precursor;
GN Name=elapor2;
GN Synonyms=eig121l {ECO:0000303|PubMed:17475571},
GN kiaa1324l {ECO:0000250|UniProtKB:A8MWY0};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=21177533; DOI=10.1074/jbc.m110.177907;
RA Araki T., Kusakabe M., Nishida E.;
RT "A transmembrane protein EIG121L is required for epidermal differentiation
RT during early embryonic development.";
RL J. Biol. Chem. 286:6760-6768(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J;
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
RN [3] {ECO:0000312|EMBL:AAH77391.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAH77391.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=17475571; DOI=10.1016/j.modgep.2007.03.004;
RA Araki T., Kusakabe M., Nishida E.;
RT "Expression of estrogen induced gene 121-like (EIG121L) during early
RT Xenopus development.";
RL Gene Expr. Patterns 7:666-671(2007).
CC -!- FUNCTION: Functions as a regulator of the BMP signaling pathway and is
CC involved in epidermal differentiation. {ECO:0000269|PubMed:21177533}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21177533};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6DDW2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6DDW2-2; Sequence=VSP_060576;
CC -!- TISSUE SPECIFICITY: Expressed in the animal half of the embryo during
CC gastrulation, becoming restricted to the ventral ectoderm at stage
CC 12.5. At the neurula stage, expressed in the anterior ectoderm
CC surrounding the neural plate, and weakly in the epidermis. Expression
CC is especially high in the presumptive hatching gland and cement gland
CC regions. Surprisingly, by the tailbud stage (stage 22), expression is
CC limited to the hatching gland and is not seen in the cement gland.
CC Conversely, in tadpoles expressed broadly in the head, heart and fin.
CC Expression in the head is seen in the primary mouth and in the brain,
CC eyes, otic vesicles and olfactory pits. {ECO:0000269|PubMed:17475571}.
CC -!- DEVELOPMENTAL STAGE: First expressed at stage 9, after the mid-blastula
CC transition (MBT). Expression is highest at stage 10.5 and remains
CC constant until the tadpole stage (PubMed:17475571). First detected at
CC stage 10.5, expression increases gradually until the tadpole stage (at
CC protein level) (PubMed:21177533). Highly expressed in the epidermal
CC ectoderm at the neurula stage (PubMed:21177533).
CC {ECO:0000269|PubMed:17475571, ECO:0000269|PubMed:21177533}.
CC -!- INDUCTION: Expression is down-regulated by ras.
CC {ECO:0000269|PubMed:17475571}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown induces severe developmental
CC defects including dorsal open phenotype and the reduction of head and
CC tail structures at the tailbud stage. {ECO:0000269|PubMed:21177533}.
CC -!- SIMILARITY: Belongs to the ELAPOR family. {ECO:0000255}.
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DR EMBL; AB566126; BAJ41187.1; -; mRNA.
DR EMBL; CM004470; OCT89193.1; -; Genomic_DNA.
DR EMBL; BC077391; AAH77391.1; -; mRNA.
DR RefSeq; NP_001086747.1; NM_001093278.1.
DR AlphaFoldDB; Q6DDW2; -.
DR DNASU; 446582; -.
DR GeneID; 446582; -.
DR KEGG; xla:446582; -.
DR CTD; 446582; -.
DR Xenbase; XB-GENE-5954610; elapor2.L.
DR OMA; WNEPKQC; -.
DR OrthoDB; 192139at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 446582; Expressed in stomach and 9 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0070700; F:BMP receptor binding; IDA:UniProtKB.
DR GO; GO:0051961; P:negative regulation of nervous system development; IMP:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:UniProtKB.
DR GO; GO:0045684; P:positive regulation of epidermis development; IMP:UniProtKB.
DR InterPro; IPR039181; EIG121-like.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR InterPro; IPR044865; MRH_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR22727; PTHR22727; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR SUPFAM; SSF50911; SSF50911; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS51914; MRH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..995
FT /note="Endosome/lysosome-associated apoptosis and autophagy
FT regulator family member 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000353196"
FT TOPO_DOM 22..895
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 896..916
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 917..995
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 639..843
FT /note="MRH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 683
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 883
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 641..687
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 697..725
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 793..829
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT DISULFID 805..841
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT VAR_SEQ 820..995
FT /note="Missing (in isoform 2)"
FT /id="VSP_060576"
FT CONFLICT 35
FT /note="Y -> F (in Ref. 3; AAH77391 and 1; BAJ41187)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="V -> E (in Ref. 3; AAH77391 and 1; BAJ41187)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="N -> K (in Ref. 3; AAH77391 and 1; BAJ41187)"
FT /evidence="ECO:0000305"
FT CONFLICT 883
FT /note="N -> K (in Ref. 1; BAJ41187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 995 AA; 109731 MW; DC517D5B03D993AE CRC64;
MGVFCWSGCL VISLQLLLGA ALDNLSTCKE EDYHYEYTEC DSTGSRWRVA VPNPGKACAG
LPDPVKGKEC TFSCAAGEFL EISSQLCSKC EPGTYSLGTG IKFDEWDKMP QGFSNVATYM
ENTAEFSDNK PDSCVNSSWI PRGNYIESNS DDCTVSLIYA VHLKKAGSVS FEYQYLDNNI
FFEFFIQNDQ CQEMSSSSDK WVKLSDNSDW MNHMVSLKSG TNILYWRTTG ILMGTKVAKP
VLIKNITIEG VAYTSECFPC KPGTYSDEAG SSSCKICPRN TYSDRQAKEC IKCFEEKEYS
EEGASKCEER PPCTKKDLFQ IHTPCDSERK TQVIYKWIEP KICREELPAS IKLPASGNKE
DCPPCNPGYF SNGTSACSPC PVGTYSNGLS ECKTCPAGTE PVLGFEYKWW NILPGNMKTS
CFNVGNSKCD GMNGWEVAGD HIQSGIGGTD NDYLILNLHI SGFKPPTSVT GATGAELGRV
TFVFENICVS DCVLYFMVDI NRKSTSLVES FAGRKVYQSY THVIHKNATY MFTWAFQRTN
LAQDSRRFVN DIAKIYSIMV TNAIDGVSSS CRACALGPQQ LGSSCVPCPA GHYIDKESNM
CKECPPNTYL TPHQVYGKEA CVPCGPGSKS NKDHSACYSE CLVTYTNENQ TLSYNFNNLG
KVATLLNGPS FTSKGTKYYH LFNMSLCGHG GEKMAVCTDN ITDVTGKDIE ADSDDYSNVV
KTFVCQSTII PSDSKGFRTA LSSQSVNLAD SFLGVTNNSS LRGITISPDI FPSHLKIPDV
NFFFKSLATT SSCEQGRATV ISMRCNPAKL GQGDISVPRN CPAATCDGCN FYFLWETAEA
CPLCMESDYQ KIEGACKHGQ QETHYVWNEM KLCTNGVSLP EKNVSACESI DFWLKVGAGV
GAFTAVLLIA LTCYFWKKNQ KLEYKYSKLV ITANSKECEL PAPDSCAIME GEDNEDDVIY
SNKQSLLEKL KSLATKEKEH NFESVQLKSS RAQNI
