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ANXA4_PIG
ID   ANXA4_PIG               Reviewed;         319 AA.
AC   P08132; Q29306;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Annexin A4;
DE   AltName: Full=35-beta calcimedin;
DE   AltName: Full=Annexin IV;
DE   AltName: Full=Annexin-4;
DE   AltName: Full=Chromobindin-4;
DE   AltName: Full=Endonexin I;
DE   AltName: Full=Lipocortin IV;
DE   AltName: Full=P32.5;
DE   AltName: Full=PP4-X;
DE   AltName: Full=Placental anticoagulant protein II;
DE            Short=PAP-II;
DE   AltName: Full=Protein II;
GN   Name=ANXA4; Synonyms=ANX4;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-319, ACETYLATION AT ALA-2, AND PHOSPHORYLATION AT
RP   THR-7.
RC   TISSUE=Intestinal epithelium;
RX   PubMed=2956093; DOI=10.1002/j.1460-2075.1987.tb02406.x;
RA   Weber K., Johnsson N., Plessmann U., Van P.N., Soling H.-D., Ampe C.,
RA   Vandekerckhove J.;
RT   "The amino acid sequence of protein II and its phosphorylation site for
RT   protein kinase C; the domain structure Ca2+-modulated lipid binding
RT   proteins.";
RL   EMBO J. 6:1599-1604(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-127.
RC   TISSUE=Small intestine;
RX   PubMed=8672129; DOI=10.1007/s003359900153;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA library:
RT   analysis of 839 clones.";
RL   Mamm. Genome 7:509-517(1996).
CC   -!- FUNCTION: Calcium/phospholipid-binding protein which promotes membrane
CC       fusion and is involved in exocytosis. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Zymogen granule membrane
CC       {ECO:0000250|UniProtKB:P50994}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P50994}.
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC       and phospholipid.
CC   -!- MISCELLANEOUS: Seems to bind one calcium ion with high affinity.
CC   -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01245, ECO:0000305}.
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DR   EMBL; F14682; CAA23194.1; -; mRNA.
DR   PIR; A27107; LUPG4.
DR   RefSeq; NP_001161111.1; NM_001167639.1.
DR   AlphaFoldDB; P08132; -.
DR   SMR; P08132; -.
DR   STRING; 9823.ENSSSCP00000008898; -.
DR   iPTMnet; P08132; -.
DR   PaxDb; P08132; -.
DR   PeptideAtlas; P08132; -.
DR   PRIDE; P08132; -.
DR   Ensembl; ENSSSCT00015070189; ENSSSCP00015028063; ENSSSCG00015052361.
DR   Ensembl; ENSSSCT00025064494; ENSSSCP00025027468; ENSSSCG00025047392.
DR   Ensembl; ENSSSCT00040091914; ENSSSCP00040040556; ENSSSCG00040067180.
DR   Ensembl; ENSSSCT00050045379; ENSSSCP00050018645; ENSSSCG00050033836.
DR   Ensembl; ENSSSCT00055038315; ENSSSCP00055030441; ENSSSCG00055019474.
DR   Ensembl; ENSSSCT00055038482; ENSSSCP00055030574; ENSSSCG00055019474.
DR   Ensembl; ENSSSCT00065042016; ENSSSCP00065017812; ENSSSCG00065031077.
DR   Ensembl; ENSSSCT00065042020; ENSSSCP00065017813; ENSSSCG00065031077.
DR   Ensembl; ENSSSCT00065042027; ENSSSCP00065017816; ENSSSCG00065031077.
DR   Ensembl; ENSSSCT00065042031; ENSSSCP00065017817; ENSSSCG00065031077.
DR   Ensembl; ENSSSCT00065042040; ENSSSCP00065017821; ENSSSCG00065031077.
DR   Ensembl; ENSSSCT00065042049; ENSSSCP00065017826; ENSSSCG00065031077.
DR   Ensembl; ENSSSCT00070059960; ENSSSCP00070051085; ENSSSCG00070029818.
DR   Ensembl; ENSSSCT00070059961; ENSSSCP00070051086; ENSSSCG00070029818.
DR   Ensembl; ENSSSCT00070059962; ENSSSCP00070051087; ENSSSCG00070029818.
DR   GeneID; 100312960; -.
DR   KEGG; ssc:100312960; -.
DR   CTD; 307; -.
DR   eggNOG; KOG0819; Eukaryota.
DR   InParanoid; P08132; -.
DR   OrthoDB; 856254at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 3.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.220.10; -; 4.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR018502; Annexin_repeat.
DR   InterPro; IPR018252; Annexin_repeat_CS.
DR   InterPro; IPR037104; Annexin_sf.
DR   InterPro; IPR002391; ANX4.
DR   PANTHER; PTHR10502:SF28; PTHR10502:SF28; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; SSF47874; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 4.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW   Cytoplasmic vesicle; Direct protein sequencing; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2956093"
FT   CHAIN           2..319
FT                   /note="Annexin A4"
FT                   /id="PRO_0000067484"
FT   REPEAT          14..85
FT                   /note="Annexin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          86..157
FT                   /note="Annexin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          169..241
FT                   /note="Annexin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   REPEAT          245..316
FT                   /note="Annexin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:2956093"
FT   MOD_RES         7
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000269|PubMed:2956093"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P09525"
FT   MOD_RES         213
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09525"
FT   MOD_RES         293
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09525"
FT   MOD_RES         300
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P09525"
SQ   SEQUENCE   319 AA;  35829 MW;  DB55FC634EFFD30A CRC64;
     MAAKGGTVKA ASGFNAAEDA QTLRKAMKGL GTDEDAIISV LAYRSTAQRQ EIRTAYKSTI
     GRDLLDDLKS ELSGNFEQVI LGMMTPTVLY DVQELRRAMK GAGTDEGCLI EILASRTPEE
     IRRINQTYQL QYGRSLEDDI RSDTSFMFQR VLVSLSAGGR DEGNYLDDAL VRQDAQDLYE
     AGEKKWGTDE VKFLTVLCSR NRNHLLHVFD EYKRISQKDI EQSIKSETSG SFEDALLAIV
     KCMRNKSAYF AERLYKSMKG LGTDDNTLIR VMVSRAEIDM MDIRANFKRL YGKSLYSFIK
     GDTSGDYRKV LLILCGGDD
 
 
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