AXA2L_HUMAN
ID AXA2L_HUMAN Reviewed; 339 AA.
AC A6NMY6;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Putative annexin A2-like protein;
DE AltName: Full=Annexin A2 pseudogene 2;
DE AltName: Full=Lipocortin II pseudogene;
GN Name=ANXA2P2; Synonyms=ANX2L2, ANX2P2, LPC2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2174397; DOI=10.1016/0378-1119(90)90367-z;
RA Spano F., Raugei G., Palla E., Colella C., Melli M.;
RT "Characterization of the human lipocortin-2-encoding multigene family: its
RT structure suggests the existence of a short amino acid unit undergoing
RT duplication.";
RL Gene 95:243-251(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
CC -!- FUNCTION: Calcium-regulated membrane-binding protein whose affinity for
CC calcium is greatly enhanced by anionic phospholipids. It binds two
CC calcium ions with high affinity. May be involved in heat-stress
CC response. {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11 and 2
CC heavy chains of ANXA2P2/p36. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250}. Melanosome {ECO:0000250}.
CC Note=In the lamina beneath the plasma membrane. In melanosome fractions
CC from stage I to stage IV. Translocated from the cytoplasm to the cell
CC surface through a Golgi-independent mechanism. {ECO:0000250}.
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid. {ECO:0000250}.
CC -!- MISCELLANEOUS: It may cross-link plasma membrane phospholipids with
CC actin and the cytoskeleton and be involved with exocytosis.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. The existence of a
CC transcript at this locus is supported by only one sequence submission
CC (PubMed:2174397). {ECO:0000305|PubMed:2174397}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M62898; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL139008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A6NMY6; -.
DR SMR; A6NMY6; -.
DR IntAct; A6NMY6; 16.
DR MINT; A6NMY6; -.
DR ChEMBL; CHEMBL4295633; -.
DR GlyGen; A6NMY6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A6NMY6; -.
DR PhosphoSitePlus; A6NMY6; -.
DR SwissPalm; A6NMY6; -.
DR BioMuta; HGNC:539; -.
DR EPD; A6NMY6; -.
DR jPOST; A6NMY6; -.
DR MassIVE; A6NMY6; -.
DR MaxQB; A6NMY6; -.
DR PeptideAtlas; A6NMY6; -.
DR PRIDE; A6NMY6; -.
DR ProteomicsDB; 1570; -.
DR TopDownProteomics; A6NMY6; -.
DR GeneCards; ANXA2P2; -.
DR HGNC; HGNC:539; ANXA2P2.
DR neXtProt; NX_A6NMY6; -.
DR InParanoid; A6NMY6; -.
DR PhylomeDB; A6NMY6; -.
DR PathwayCommons; A6NMY6; -.
DR SignaLink; A6NMY6; -.
DR ChiTaRS; ANXA2P2; human.
DR Pharos; A6NMY6; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A6NMY6; protein.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IBA:GO_Central.
DR GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR GO; GO:0046790; F:virion binding; IBA:GO_Central.
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; IPR002389; ANX2.
DR PANTHER; PTHR10502:SF18; PTHR10502:SF18; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR00198; ANNEXINII.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 4.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 5: Uncertain;
KW Acetylation; Annexin; Basement membrane; Calcium;
KW Calcium/phospholipid-binding; Extracellular matrix; Phosphoprotein;
KW Reference proteome; Repeat; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P19620"
FT CHAIN 2..339
FT /note="Putative annexin A2-like protein"
FT /id="PRO_0000343940"
FT REPEAT 33..104
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 105..176
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 189..261
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 265..336
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REGION 2..24
FT /note="S100A10-binding site"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P19620"
FT MOD_RES 24
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250"
FT MOD_RES 49
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07356"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07356"
FT MOD_RES 199
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07356"
FT MOD_RES 227
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07356"
FT CONFLICT 72
FT /note="V -> S (in Ref. 1; M62898)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="D -> A (in Ref. 1; M62898)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 339 AA; 38659 MW; 6A05AB3E19392A15 CRC64;
MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIV
TNRDNAQRQD IVFSYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG
LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA
EDGSVIDYEL IDQDAQDLYD AGVKRKGTDV PKWISIMTER SVPHLQKVFD RYKSYSPYDM
LESIRKEVKG DLENAFLNLV QRIQNKPLYF ADQLYDSMKG KGTRDKVLIR IMVSRSEVDM
LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD
