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CALU_RAT
ID   CALU_RAT                Reviewed;         315 AA.
AC   O35783;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Calumenin;
DE   AltName: Full=CBP-50;
DE   AltName: Full=Crocalbin;
DE   Flags: Precursor;
GN   Name=Calu;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=10094503; DOI=10.1016/s0014-5793(99)00177-5;
RA   Hseu M.-J., Yen C.-H., Tzeng M.-C.;
RT   "Crocalbin: a new calcium-binding protein that is also a binding protein
RT   for crotoxin, a neurotoxic phospholipase A2.";
RL   FEBS Lett. 445:440-444(1999).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH GGCX.
RX   PubMed=15075329; DOI=10.1074/jbc.m401645200;
RA   Wajih N., Sane D.C., Hutson S.M., Wallin R.;
RT   "The inhibitory effect of calumenin on the vitamin K-dependent gamma-
RT   carboxylation system. Characterization of the system in normal and
RT   warfarin-resistant rats.";
RL   J. Biol. Chem. 279:25276-25283(2004).
CC   -!- FUNCTION: Involved in regulation of vitamin K-dependent carboxylation
CC       of multiple N-terminal glutamate residues. Seems to inhibit gamma-
CC       carboxylase GGCX. Binds 7 calcium ions with a low affinity (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:15075329}.
CC   -!- SUBUNIT: Binds crotoxin. Interacts with GGCX.
CC       {ECO:0000269|PubMed:15075329}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:O43852}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:O43852}. Secreted
CC       {ECO:0000250|UniProtKB:O43852}. Melanosome
CC       {ECO:0000250|UniProtKB:O43852}. Sarcoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:O43852}.
CC   -!- SIMILARITY: Belongs to the CREC family. {ECO:0000305}.
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DR   EMBL; AJ001929; CAA05100.1; -; mRNA.
DR   AlphaFoldDB; O35783; -.
DR   GlyGen; O35783; 1 site.
DR   iPTMnet; O35783; -.
DR   PhosphoSitePlus; O35783; -.
DR   jPOST; O35783; -.
DR   PaxDb; O35783; -.
DR   PRIDE; O35783; -.
DR   UCSC; RGD:620383; rat.
DR   RGD; 620383; Calu.
DR   InParanoid; O35783; -.
DR   PhylomeDB; O35783; -.
DR   Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR   PRO; PR:O35783; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR   GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IDA:RGD.
DR   GO; GO:0014012; P:peripheral nervous system axon regeneration; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   InterPro; IPR027239; Calumenin.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR10827:SF76; PTHR10827:SF76; 1.
DR   Pfam; PF13202; EF-hand_5; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF13833; EF-hand_8; 1.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; SSF47473; 2.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 6.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW   Golgi apparatus; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Sarcoplasmic reticulum; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..315
FT                   /note="Calumenin"
FT                   /id="PRO_0000004155"
FT   DOMAIN          68..103
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          104..139
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          151..186
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          188..223
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          229..264
FT                   /note="EF-hand 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          265..300
FT                   /note="EF-hand 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOTIF           312..315
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000250"
FT   BINDING         81
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         83
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         85
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         92
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         117
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         119
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         121
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         128
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         164
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         166
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         168
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         175
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305"
FT   BINDING         201
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         203
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         205
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         212
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         242
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000305"
FT   BINDING         244
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000305"
FT   BINDING         246
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000305"
FT   BINDING         248
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000305"
FT   BINDING         253
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000305"
FT   BINDING         278
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         280
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         282
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         284
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         289
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         47
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O43852"
FT   MOD_RES         65
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O43852"
FT   MOD_RES         69
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43852"
FT   MOD_RES         254
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O43852"
FT   MOD_RES         261
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43852"
FT   MOD_RES         277
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43852"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   315 AA;  36997 MW;  06B7FED579929E98 CRC64;
     MDLRQFLMCL SLCTAFALSK PTEKKDRVHH EPQLSDKVHN DAQNFDYDHD AFLGAEEAKS
     FGQLTPEESK EKLGMIVDKI DTDKDGFVTE GELKSRIKHA QKKYIYDNVE NQWQEFDMNQ
     DGLISWDEYR NVTYGTYLDD PDPDDGFNYK PIMVRDERRF KMADQDGDLI ATKEEFTAFL
     HPEEYDYMKD IVLQETMEDI DQNADGFIDL EEYIGDMYSH DGNADEPQWV KTEREQFVEF
     RDKNRDGKMD KEETKDWILP SDYDHAEAEA RHLVYESDQD KDGKLTKEEI VDKYDLFVGS
     QATDFGEALV RHDEF
 
 
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