CRE2B_XENLA
ID CRE2B_XENLA Reviewed; 361 AA.
AC Q4V7M2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cysteine-rich with EGF-like domain protein 2-B;
DE Flags: Precursor;
GN Name=creld2-b;
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=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2005) 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; BC097826; AAH97826.1; -; mRNA.
DR RefSeq; NP_001089538.1; NM_001096069.1.
DR AlphaFoldDB; Q4V7M2; -.
DR DNASU; 734593; -.
DR GeneID; 734593; -.
DR KEGG; xla:734593; -.
DR CTD; 734593; -.
DR Xenbase; XB-GENE-6255881; creld2.L.
DR OMA; PEANECK; -.
DR OrthoDB; 883628at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 734593; Expressed in egg cell and 19 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-B"
FT /id="PRO_0000256250"
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 339..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..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 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; 39515 MW; 8E342A145975774A CRC64;
MNGSRAWRLA AWLLLCLSCS AAVARKDSCE TCTKLVERFH KGLENTAKKN FGGGNTAWEE
KTLSKYESSE IRLVEIIENI CDSSDFECNH MVEEHEEQIE KWWFKMKQKY PDLLKWFCIE
AIKVCCPSGS YGPDCLACLG GSERPCHGNG FCSGDGTRSG DGSCRCKAEY TGSFCLECSD
GYYSSERNDT HAVCIACNQA CKTCNGPSNE DCKECNNGWV KDDGKCVDLN ECASEESPCK
DSQYCLNTEG SFLCKECDGS CSGCSGEGPE SCKDCATGFV MLSGKCTDVD ECDASEKLCL
RENEVCLNTA GSYKCTCSEG FEDKEGNCVK IMETENPEIT EGETGTPASD TNILNTAHED
L