CLGN_BOVIN
ID CLGN_BOVIN Reviewed; 606 AA.
AC Q3SYT6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Calmegin;
DE Flags: Precursor;
GN Name=CLGN;
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=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions during spermatogenesis as a chaperone for a range
CC of client proteins that are important for sperm adhesion onto the egg
CC zona pellucida and for subsequent penetration of the zona pellucida.
CC Required for normal sperm migration from the uterus into the oviduct.
CC Required for normal male fertility. Binds calcium ions (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPIB and PDILT. Interacts with ADAM2 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR EMBL; BC103401; AAI03402.1; -; mRNA.
DR RefSeq; NP_001029377.1; NM_001034205.2.
DR AlphaFoldDB; Q3SYT6; -.
DR SMR; Q3SYT6; -.
DR STRING; 9913.ENSBTAP00000002071; -.
DR PaxDb; Q3SYT6; -.
DR PRIDE; Q3SYT6; -.
DR Ensembl; ENSBTAT00000002071; ENSBTAP00000002071; ENSBTAG00000001580.
DR GeneID; 504256; -.
DR KEGG; bta:504256; -.
DR CTD; 1047; -.
DR VEuPathDB; HostDB:ENSBTAG00000001580; -.
DR VGNC; VGNC:27437; CLGN.
DR eggNOG; KOG0675; Eukaryota.
DR GeneTree; ENSGT00950000182915; -.
DR HOGENOM; CLU_018224_2_0_1; -.
DR InParanoid; Q3SYT6; -.
DR OMA; RVGCGEW; -.
DR OrthoDB; 775337at2759; -.
DR TreeFam; TF300618; -.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000001580; Expressed in spermatid and 99 other tissues.
DR ExpressionAtlas; Q3SYT6; baseline.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 2.10.250.10; -; 1.
DR InterPro; IPR001580; Calret/calnex.
DR InterPro; IPR018124; Calret/calnex_CS.
DR InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR11073; PTHR11073; 1.
DR Pfam; PF00262; Calreticulin; 1.
DR PRINTS; PR00626; CALRETICULIN.
DR SUPFAM; SSF49899; SSF49899; 2.
DR SUPFAM; SSF63887; SSF63887; 1.
DR PROSITE; PS00803; CALRETICULIN_1; 1.
DR PROSITE; PS00804; CALRETICULIN_2; 1.
DR PROSITE; PS00805; CALRETICULIN_REPEAT; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..606
FT /note="Calmegin"
FT /id="PRO_0000236245"
FT TOPO_DOM 20..466
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..606
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 263..276
FT /note="1-1"
FT REPEAT 280..293
FT /note="1-2"
FT REPEAT 299..312
FT /note="1-3"
FT REPEAT 318..331
FT /note="1-4"
FT REPEAT 335..348
FT /note="2-1"
FT REPEAT 352..365
FT /note="2-2"
FT REPEAT 366..379
FT /note="2-3"
FT REPEAT 380..393
FT /note="2-4"
FT REGION 255..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..346
FT /note="Interaction with PPIB"
FT /evidence="ECO:0000250"
FT REGION 518..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..564
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27824"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14967"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14967"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52194"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52194"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52194"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52194"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27824"
FT DISULFID 147..181
FT /evidence="ECO:0000250"
FT DISULFID 347..351
FT /evidence="ECO:0000250"
SQ SEQUENCE 606 AA; 69515 MW; 4FAE7CE2EBF8EB4D CRC64;
MRFQGFWLCL GLLFISVNAE FMDDSVEMED FDENSEETDE LSSEIKYKTP QPVGEVYFTE
TFDSGRLAGW VLSKAKKDDI DAEISIYDGR WEIEELKENR IPGDRGLVLK SRAKHHAISA
VLAKPFIFAD KPLVVQYEVN FQDGIDCGGA YIKLLADTDG LNLENFYDKT SYTIMFGPDK
CGEDYKLHFI FRHKHPKTGV FEEKHAKPPD VDLKRFFTDR KTHLYTLVMN PDDTFEVLID
QIVVNKGSLL EDVVPPINPP KEIEDPTDEK PDDWDERAKI PDASAVKPED WDESEPPQIV
DSSAVKPDGW LDNEPEFIPD PNAEKPFDWN EDMDGEWEAP HISNPACRIG CGEWSPPMID
NPKYKGIWRP PMIDNPNYQG IWSPRKIPNP DYFEDNHPFL LTSFRALGLE LWSMTSDIYF
DNFIICSEKE VADRWAADGW GMKILIENAN EPSIFKQLMS ATEQRPWLWF IYLLTAALPI
ALIGSFCWPR KVKKKYEDVA FEKLDICKPQ TKGALEQEVK EEKAALEKPV DLEEEKKQSD
GEIVEKEEEG EPEEKSEEEI EIIEGQEEGN KSNKSGSEDE MKEADESTGS GDGPIKSVRK
RRVRKE
