CLGN_CANLF
ID CLGN_CANLF Reviewed; 620 AA.
AC E2RA18; D9N169;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Calmegin;
DE Flags: Precursor;
GN Name=CLGN;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer;
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 327-360 IN COMPLEX WITH PPIB.
RX PubMed=20801878; DOI=10.1074/jbc.m110.160101;
RA Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F.,
RA Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.;
RT "Structural basis of cyclophilin B binding by the calnexin/calreticulin P-
RT domain.";
RL J. Biol. Chem. 285:35551-35557(2010).
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 PDILT. Interacts with ADAM2 (By similarity).
CC Interacts with PPIB. {ECO:0000250, ECO:0000269|PubMed:20801878}.
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; AAEX03011717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_533285.3; XM_533285.5.
DR PDB; 3ICI; X-ray; 1.70 A; C=327-360.
DR PDB; 5V8Z; X-ray; 2.10 A; B/D=327-360.
DR PDBsum; 3ICI; -.
DR PDBsum; 5V8Z; -.
DR AlphaFoldDB; E2RA18; -.
DR SMR; E2RA18; -.
DR STRING; 9615.ENSCAFP00000057942; -.
DR PaxDb; E2RA18; -.
DR GeneID; 476076; -.
DR CTD; 1047; -.
DR eggNOG; KOG0675; Eukaryota.
DR HOGENOM; CLU_018224_2_0_1; -.
DR InParanoid; E2RA18; -.
DR OMA; RVGCGEW; -.
DR OrthoDB; 775337at2759; -.
DR TreeFam; TF300618; -.
DR Proteomes; UP000002254; Chromosome 19.
DR Bgee; ENSCAFG00000003696; Expressed in testis and 24 other tissues.
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:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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; 1.
DR SUPFAM; SSF63887; SSF63887; 1.
DR PROSITE; PS00803; CALRETICULIN_1; 1.
DR PROSITE; PS00804; CALRETICULIN_2; 1.
DR PROSITE; PS00805; CALRETICULIN_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Chaperone; Disulfide bond;
KW Endoplasmic reticulum; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..620
FT /note="Calmegin"
FT /id="PRO_0000428628"
FT TOPO_DOM 30..480
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 277..290
FT /note="1-1"
FT REPEAT 294..307
FT /note="1-2"
FT REPEAT 313..326
FT /note="1-3"
FT REPEAT 332..345
FT /note="1-4"
FT REPEAT 349..362
FT /note="2-1"
FT REPEAT 366..379
FT /note="2-2"
FT REPEAT 380..393
FT /note="2-3"
FT REPEAT 394..407
FT /note="2-4"
FT REGION 267..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..360
FT /note="Interaction with PPIB"
FT REGION 526..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..578
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 138
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27824"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14967"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14967"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52194"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52194"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52194"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52194"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27824"
FT DISULFID 161..195
FT /evidence="ECO:0000250"
FT DISULFID 361..365
FT /evidence="ECO:0000250"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:3ICI"
SQ SEQUENCE 620 AA; 70900 MW; A1481CDA17B91E05 CRC64;
MSSPWSTVIS MHFQSFWLCL GLLFISVNAE FMDDDVEMED FDENSEEIDV NEGELPSEIN
YKTPQPMGEV YFTETFDSGR LAGWVLSKAK KDDTDAEISI YDGRWEIEEL KENRVPGDRG
LVLKSRAKHH AIAAVLAKPF IFADKPLIVQ YEVNFQDGID CGGAYIKLLA DTDGLNLENF
YDKTSYTIMF GPDKCGEDYK LHFIFRHKHP KTGVFEEKHA KPPDVDLKKF FTDRKTHLYT
LVMNPDDTFE VLIDQVVVNQ GSLLEDVVPP INPPKEIEDP SDKKPDEWDE RAKIPDPSAV
KPEDWDESEP AQIEDLSVVK PDGWLDDEPK FIPDPNAEKP DDWNEDMDGE WEAPRISNPA
CRIGCGEWSP PMIDNPKYKG VWRPPMIDNP NYQGIWSPRK IPNPDYFEDD HPFLLTSFRA
LGLELWSMTS NIYFDNFIIC SEKETADRWA ADGWGVKILV ANANEPGIFK QLMAAAEERP
WLWLIYFVTA GLPIALIASF CWPRKVKKKY EDSEYKKTDI CKPQTKGALE QEVKEKKAAL
EKPVDLEEEK KQSDGETVEK EEEAEPEEKS EEEIEIIEGQ EEGNKSNKSG SEDEMKEADE
STGSGDGPVK SVRKRRVRKE
