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CASB_HORSE
ID   CASB_HORSE              Reviewed;         241 AA.
AC   Q9GKK3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Beta-casein;
DE   Flags: Precursor;
GN   Name=CSN2 {ECO:0000250|UniProtKB:P39037};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAG43954.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=Warmblood {ECO:0000269|PubMed:12617390};
RC   TISSUE=Lactating mammary gland {ECO:0000312|EMBL:AAG43954.1};
RX   PubMed=12617390; DOI=10.1017/s002202990200599x;
RA   Lenasi T., Rogelj I., Dovc P.;
RT   "Characterization of equine cDNA sequences for alphaS1-, beta- and kappa-
RT   casein.";
RL   J. Dairy Res. 70:29-36(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 16-241 (ISOFORM 1), DEAMIDATION AT ASN-150, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=Haflinger {ECO:0000269|PubMed:16691551};
RC   TISSUE=Milk {ECO:0000269|PubMed:16691551};
RX   PubMed=16691551; DOI=10.1002/pmic.200500728;
RA   Girardet J.-M., Miclo L., Florent S., Molle D., Gaillard J.-L.;
RT   "Determination of the phosphorylation level and deamidation susceptibility
RT   of equine beta-casein.";
RL   Proteomics 6:3707-3717(2006).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 16-241 (ISOFORM 3), AND MASS SPECTROMETRY.
RC   STRAIN=Haflinger {ECO:0000269|PubMed:17366489};
RC   TISSUE=Milk {ECO:0000269|PubMed:17366489};
RX   PubMed=17366489; DOI=10.1002/pmic.200600683;
RA   Miclo L., Girardet J.-M., Egito A.S., Molle D., Martin P., Gaillard J.-L.;
RT   "The primary structure of a low-M(r) multiphosphorylated variant of beta-
RT   casein in equine milk.";
RL   Proteomics 7:1327-1335(2007).
RN   [4] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 16-50 (ISOFORM 1), AND PROTEIN SEQUENCE OF 16-58
RP   (ISOFORM 2).
RC   STRAIN=Welsh pony {ECO:0000269|PubMed:15274143};
RC   TISSUE=Milk {ECO:0000269|PubMed:15274143};
RX   PubMed=15274143; DOI=10.1002/pmic.200300765;
RA   Miranda G., Mahe M.-F., Leroux C., Martin P.;
RT   "Proteomic tools to characterize the protein fraction of Equidae milk.";
RL   Proteomics 4:2496-2509(2004).
RN   [5] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 16-30, AND SUBCELLULAR LOCATION.
RC   STRAIN=Haflinger {ECO:0000269|PubMed:12018413};
RC   TISSUE=Milk {ECO:0000269|PubMed:12018413};
RX   PubMed=12018413; DOI=10.3168/jds.s0022-0302(02)74126-x;
RA   Egito A.S., Miclo L., Lopez C., Adam A., Girardet J.-M., Gaillard J.-L.;
RT   "Separation and characterization of mares' milk alpha(s1)-, beta-, kappa-
RT   caseins, gamma-casein-like, and proteose peptone component 5-like
RT   peptides.";
RL   J. Dairy Sci. 85:697-706(2002).
RN   [6]
RP   PHOSPHORYLATION AT SER-24; SER-25; THR-27; SER-33; SER-38; SER-39 AND
RP   SER-40.
RX   PubMed=20486249; DOI=10.1002/rcm.4552;
RA   Mateos A., Girardet J.M., Molle D., Corbier C., Gaillard J.L., Miclo L.;
RT   "Identification of phosphorylation sites of equine beta-casein isoforms.";
RL   Rapid Commun. Mass Spectrom. 24:1533-1542(2010).
CC   -!- FUNCTION: Important role in determination of the surface properties of
CC       the casein micelles. {ECO:0000250|UniProtKB:P39037}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12018413}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|PubMed:16691551}; Synonyms=B
CC       {ECO:0000269|PubMed:16691551};
CC         IsoId=Q9GKK3-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:12617390};
CC         IsoId=Q9GKK3-2; Sequence=VSP_051779;
CC       Name=3 {ECO:0000269|PubMed:17366489}; Synonyms=low molecular weight
CC       beta-casein {ECO:0000269|PubMed:17366489};
CC         IsoId=Q9GKK3-3; Sequence=VSP_051780;
CC   -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC       {ECO:0000305}.
CC   -!- PTM: There are at least five different forms found in milk, with
CC       varying degrees of phosphorylation. These include form 3-P which is
CC       phosphorylated at three sites that have not been determined, this form
CC       is present in very low amounts, form 4-P which is phosphorylated at
CC       four sites, form 5-P which is phosphorylated at five sites, form 6-P
CC       which is phosphorylated at six sites, and form 7-P which is
CC       phosphorylated at seven sites. {ECO:0000269|PubMed:16691551,
CC       ECO:0000269|PubMed:20486249}.
CC   -!- PTM: Spontaneous deamidation of Asn-150 produces aspartate or
CC       isoaspartate. {ECO:0000269|PubMed:16691551}.
CC   -!- MASS SPECTROMETRY: [Isoform 1]: Mass=25514; Mass_error=3;
CC       Method=Electrospray; Note=Dephosphorylated. The measured range is 16-
CC       241.; Evidence={ECO:0000269|PubMed:16691551};
CC   -!- MASS SPECTROMETRY: [Isoform 3]: Mass=10591; Mass_error=2;
CC       Method=Electrospray; Note=Dephosphorylated. The measured range is 16-
CC       109.; Evidence={ECO:0000269|PubMed:17366489};
CC   -!- MASS SPECTROMETRY: [Isoform 3]: Mass=10911; Method=Electrospray;
CC       Note=Form 4-P. The measured range is 16-109.;
CC       Evidence={ECO:0000269|PubMed:17366489};
CC   -!- MASS SPECTROMETRY: [Isoform 3]: Mass=10991; Method=Electrospray;
CC       Note=Form 5-P. The measured range is 16-109.;
CC       Evidence={ECO:0000269|PubMed:17366489};
CC   -!- MASS SPECTROMETRY: [Isoform 3]: Mass=11071; Method=Electrospray;
CC       Note=Form 6-P. The measured range is 16-109.;
CC       Evidence={ECO:0000269|PubMed:17366489};
CC   -!- MASS SPECTROMETRY: [Isoform 3]: Mass=11150; Method=Electrospray;
CC       Note=Form 7-P. The measured range is 16-109.;
CC       Evidence={ECO:0000269|PubMed:17366489};
CC   -!- MISCELLANEOUS: [Isoform 3]: Accounts for 4% of total casein.
CC       {ECO:0000269|PubMed:17366489}.
CC   -!- SIMILARITY: Belongs to the beta-casein family. {ECO:0000255}.
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DR   EMBL; AF214526; AAG43954.1; -; mRNA.
DR   RefSeq; NP_001075321.1; NM_001081852.1. [Q9GKK3-2]
DR   AlphaFoldDB; Q9GKK3; -.
DR   STRING; 9796.ENSECAP00000042870; -.
DR   iPTMnet; Q9GKK3; -.
DR   PaxDb; Q9GKK3; -.
DR   PeptideAtlas; Q9GKK3; -.
DR   Ensembl; ENSECAT00000010264; ENSECAP00000007906; ENSECAG00000009837. [Q9GKK3-2]
DR   Ensembl; ENSECAT00000064283; ENSECAP00000042870; ENSECAG00000009837. [Q9GKK3-1]
DR   GeneID; 100033903; -.
DR   KEGG; ecb:100033903; -.
DR   CTD; 1447; -.
DR   GeneTree; ENSGT00390000001890; -.
DR   HOGENOM; CLU_106775_0_0_1; -.
DR   InParanoid; Q9GKK3; -.
DR   OMA; LMHQIPQ; -.
DR   OrthoDB; 1336883at2759; -.
DR   TreeFam; TF336929; -.
DR   Proteomes; UP000002281; Chromosome 3.
DR   Bgee; ENSECAG00000009837; Expressed in prefrontal cortex.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:Ensembl.
DR   GO; GO:0007595; P:lactation; IEA:Ensembl.
DR   GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; IEA:Ensembl.
DR   InterPro; IPR001588; Casein.
DR   InterPro; IPR016345; Casein_beta.
DR   InterPro; IPR031305; Casein_CS.
DR   PANTHER; PTHR11500; PTHR11500; 1.
DR   Pfam; PF00363; Casein; 1.
DR   PIRSF; PIRSF002372; Beta-casein; 1.
DR   PROSITE; PS00306; CASEIN_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Milk protein;
KW   Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:12018413"
FT   CHAIN           16..241
FT                   /note="Beta-casein"
FT                   /id="PRO_0000004474"
FT   REGION          21..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            30
FT                   /note="Not phosphorylated"
FT   SITE            32
FT                   /note="Not phosphorylated"
FT   MOD_RES         24
FT                   /note="Phosphoserine; in form 4-P, form 5-P, form 6-P and
FT                   form 7-P"
FT                   /evidence="ECO:0000269|PubMed:20486249"
FT   MOD_RES         25
FT                   /note="Phosphoserine; in form 7-P"
FT                   /evidence="ECO:0000269|PubMed:20486249"
FT   MOD_RES         27
FT                   /note="Phosphothreonine; in form 6-P and form 7-P"
FT                   /evidence="ECO:0000269|PubMed:20486249"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05814"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P05814"
FT   MOD_RES         33
FT                   /note="Phosphoserine; in form 5-P, form 6-P and form 7-P"
FT                   /evidence="ECO:0000269|PubMed:20486249"
FT   MOD_RES         38
FT                   /note="Phosphoserine; in form 4-P, form 5-P, form 6-P and
FT                   form 7-P"
FT                   /evidence="ECO:0000269|PubMed:20486249"
FT   MOD_RES         39
FT                   /note="Phosphoserine; in form 4-P, form 5-P, form 6-P and
FT                   form 7-P"
FT                   /evidence="ECO:0000269|PubMed:20486249"
FT   MOD_RES         40
FT                   /note="Phosphoserine; in form 4-P, form 5-P, form 6-P and
FT                   form 7-P"
FT                   /evidence="ECO:0000269|PubMed:20486249"
FT   MOD_RES         150
FT                   /note="Deamidated asparagine"
FT                   /evidence="ECO:0000269|PubMed:16691551"
FT   VAR_SEQ         42..49
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12617390"
FT                   /id="VSP_051779"
FT   VAR_SEQ         65..196
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17366489"
FT                   /id="VSP_051780"
SQ   SEQUENCE   241 AA;  27049 MW;  140B6EBF3D2323C0 CRC64;
     MKILILACLV ALALAREKEE LNVSSETVES LSSNEPDSSS EESITHINKE KLQKFKHEGQ
     QQREVERQDK ISRFVQPQPV VYPYAEPVPY AVVPQSILPL AQPPILPFLQ PEIMEVSQAK
     ETILPKRKVM PFLKSPIVPF SERQILNPTN GENLRLPVHL IQPFMHQVPQ SLLQTLMLPS
     QPVLSPPQSK VAPFPQPVVP YPQRDTPVQA FLLYQDPRLG PTGELDPATQ PIVAVHNPVI
     V
 
 
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