CRE2A_XENLA
ID CRE2A_XENLA Reviewed; 361 AA.
AC Q5XH36;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Cysteine-rich with EGF-like domain protein 2-A;
DE Flags: Precursor;
GN Name=creld2-a;
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 [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Possible role in neuronal acetylcholine receptor transport.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Endoplasmic reticulum {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CRELD family. {ECO:0000305}.
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DR EMBL; BC084239; AAH84239.1; -; mRNA.
DR RefSeq; NP_001088243.1; NM_001094774.1.
DR AlphaFoldDB; Q5XH36; -.
DR DNASU; 495074; -.
DR GeneID; 495074; -.
DR KEGG; xla:495074; -.
DR CTD; 495074; -.
DR Xenbase; XB-GENE-999017; creld2.S.
DR OrthoDB; 883628at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 495074; Expressed in liver and 18 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00064; FU; 2.
DR InterPro; IPR021852; DUF3456.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF11938; DUF3456; 2.
DR Pfam; PF07645; EGF_CA; 2.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00261; FU; 2.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 2.
PE 2: Evidence at transcript level;
KW Calcium; Disulfide bond; EGF-like domain; Endoplasmic reticulum;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..361
FT /note="Cysteine-rich with EGF-like domain protein 2-A"
FT /id="PRO_0000256249"
FT DOMAIN 134..176
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 191..238
FT /note="FU 1"
FT REPEAT 251..298
FT /note="FU 2"
FT DOMAIN 288..329
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 341..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 138..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 146..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 166..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 292..306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 299..315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 317..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 361 AA; 39745 MW; D370C9AE4F00E08D CRC64;
MNGSRALHLS AWLLLCLLCS AAVARDDSCE TCRKLVDRFH KGLENTAKKN FGGGNTAWEE
KTLSKYESSE IRLVEIIENL CDSSDFECNH MVEEHEEQIE KWWFKMKKKY PDLLKWFCIE
TIKVCCPPGT YGPDCLACLG GSERPCHGNG FCNGDGTRSG DGLCRCEAEY TGPFCLECAD
EYFSSERNDT YSLCTACNQA CKTCDGPSNE DCKECKNGWI KDDGKCVDLN ECASEESPCK
DSQYCLNTEG SFLCKECDGS CLGCSGEGPE NCKDCATGYV LLAEKCTDVD ECDASEQVCS
RENETCLNTA GSYKCTCSEG FEDKEGNCVK IMEAENTEVT DGEMGTSASD INISNTAHED
L