ID   ELAP2_BOVIN             Reviewed;         960 AA.
AC   A7E2Z9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Endosome/lysosome-associated apoptosis and autophagy regulator family member 2 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=ELAPOR2 {ECO:0000250|UniProtKB:A8MWY0};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as a regulator of the BMP signaling pathway and may
CC       be involved in epidermal differentiation.
CC       {ECO:0000250|UniProtKB:Q3UZV7}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6DDW2};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ELAPOR family. {ECO:0000305}.
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DR   EMBL; BC151637; AAI51638.1; -; mRNA.
DR   RefSeq; NP_001039703.2; NM_001046238.3.
DR   AlphaFoldDB; A7E2Z9; -.
DR   STRING; 9913.ENSBTAP00000005255; -.
DR   PaxDb; A7E2Z9; -.
DR   PRIDE; A7E2Z9; -.
DR   GeneID; 518313; -.
DR   KEGG; bta:518313; -.
DR   CTD; 222223; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   HOGENOM; CLU_005066_0_0_1; -.
DR   InParanoid; A7E2Z9; -.
DR   TreeFam; TF315906; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0070700; F:BMP receptor binding; ISS:UniProtKB.
DR   GO; GO:0051961; P:negative regulation of nervous system development; ISS:UniProtKB.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045684; P:positive regulation of epidermis development; ISS:UniProtKB.
DR   InterPro; IPR039181; EIG121-like.
DR   InterPro; IPR009011; Man6P_isomerase_rcpt-bd_dom_sf.
DR   InterPro; IPR044865; MRH_dom.
DR   PANTHER; PTHR22727; PTHR22727; 2.
DR   SUPFAM; SSF50911; SSF50911; 1.
DR   PROSITE; PS51914; MRH; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..960
FT                   /note="Endosome/lysosome-associated apoptosis and autophagy
FT                   regulator family member 2"
FT                   /id="PRO_0000333797"
FT   TOPO_DOM        45..860
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        861..881
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        882..960
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          597..808
FT                   /note="MRH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         949
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A8MWY0"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        407
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        622
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        295..312
FT                   /evidence="ECO:0000250"
FT   DISULFID        325..348
FT                   /evidence="ECO:0000250"
FT   DISULFID        328..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        599..651
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        661..689
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        758..794
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
FT   DISULFID        770..806
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01262"
SQ   SEQUENCE   960 AA;  105850 MW;  BBE29B5A66F0DD92 CRC64;
     MLFLRPGPAR GRGRGRPARA PHSGLSPPWS PAWICCWALA GCQAAWAGAG DLPSTSGRPL
     PPCLEKDYHF EYTECDSSGS RWRVAIPNSA VDCSGLPDPV RGKECTFSCA SGEYLEMKNQ
     VCSKCGEGTY SLGSGIKFDE WDELPAGFSN VATFMDTVVG PSDSRPEGCN NSSWVPRGNY
     IESNRDDCTV SLIYAVHLKK SGYVFFEYQY VDNNIFFEFF IQNDQCQEMD TTADKWVKLT
     DNGEWGSHSV MLKSGTNILY WRTTGILMGS KAVKPVLVKN ITIEGVAYTS ECFPCKPGTF
     SDKPGSFICQ VCPRNTYSEK GAKECIRCDE DSQFSEEGSS ECMERPPCTS KDYFQIHTPC
     DEEGKTQIMY KWIEPKICRE DLTDAIRLPP SGEKKDCPPC NPGFYNNGSS SCHPCPPGTF
     SDGTKECRSC PAGTEPALGF EYKWWNVLPG NMKTSCFNVG NSKCDGMNGW EVAGDHIQSG
     AGGSDNDYLI LNLHIPGFKP PTSMTGAMGS ELGRITFVFE TLCSADCVLY FMVDINRKST
     NVVESWGGTK EKQAYTHVIF KNATFTFTWA FQRTNQGQDA TTLRKKPTSA WSVHLIPTCP
     YIRSMARRLV FHVGLGVEAL SNLSSVGSLM NGPSFTSKGT KYFHFFNISL CGHEGKKLAV
     CTNNITDFTV KEMVAGSDDY TNLVGAFVCQ STIIPSESKG FRAALSSQSI ILADTFLGVT
     VETTLQNINI KEDMFPVSPS QIPDVHFFYK SSTTTTSCVN GRSTAVKMRC NPAKPGAGAI
     SVPSKCPAGT CDGCTFYFLW ESVEACPLCT EHDFHEIEGA CKRGFQETLY VWNEPKWCIK
     GISLPEKKLS TCETVDFWLK VGAGVGAFTA VLLVALTCYF WKKNQKLEYK YSKLVMTTNS
     KECELPAADS CAIMEGEDNE EEVVYSNKQS LLGKLKSLAT KEKEDHFESV QLKSSRSPNI