ID A0A7N4PTY6_SARHA Unreviewed; 442 AA. AC A0A7N4PTY6; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 14-DEC-2022, entry version 5. DE RecName: Full=Annexin {ECO:0000256|RuleBase:RU003540}; GN Name=ANXA2 {ECO:0000313|Ensembl:ENSSHAP00000043545.1}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000043545.1, ECO:0000313|Proteomes:UP000007648}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000043545.1, ECO:0000313|Proteomes:UP000007648} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J., RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C., RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P., RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M., RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M., RA Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered marsupial RT Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000043545.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}. CC Secreted, extracellular space, extracellular matrix, basement membrane CC {ECO:0000256|ARBA:ARBA00004302}. CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium CC and phospholipid. {ECO:0000256|RuleBase:RU003540}. CC -!- SIMILARITY: Belongs to the annexin family. CC {ECO:0000256|ARBA:ARBA00007831, ECO:0000256|RuleBase:RU003540}. 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 AlphaFoldDB; A0A7N4PTY6; -. DR Ensembl; ENSSHAT00000032872.1; ENSSHAP00000043545.1; ENSSHAG00000015232.2. DR GeneTree; ENSGT00940000154257; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:1990665; C:AnxA2-p11 complex; IEA:Ensembl. DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0001533; C:cornified envelope; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0031902; C:late endosome membrane; IEA:Ensembl. DR GO; GO:0005811; C:lipid droplet; IEA:Ensembl. DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl. DR GO; GO:0045121; C:membrane raft; IEA:Ensembl. DR GO; GO:0030496; C:midbody; IEA:Ensembl. DR GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl. DR GO; GO:1990667; C:PCSK9-AnxA2 complex; IEA:Ensembl. DR GO; GO:0098797; C:plasma membrane protein complex; IEA:Ensembl. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl. DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl. DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW. DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl. DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl. DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:Ensembl. DR GO; GO:0002020; F:protease binding; IEA:Ensembl. DR GO; GO:0044548; F:S100 protein binding; IEA:Ensembl. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:Ensembl. DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl. DR GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl. DR GO; GO:0042730; P:fibrinolysis; IEA:Ensembl. DR GO; GO:0001765; P:membrane raft assembly; IEA:Ensembl. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IEA:Ensembl. DR GO; GO:0002091; P:negative regulation of receptor internalization; IEA:Ensembl. DR GO; GO:0036035; P:osteoclast development; IEA:Ensembl. DR GO; GO:1905581; P:positive regulation of low-density lipoprotein particle clearance; IEA:Ensembl. DR GO; GO:1905597; P:positive regulation of low-density lipoprotein particle receptor binding; IEA:Ensembl. DR GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IEA:Ensembl. DR GO; GO:0010756; P:positive regulation of plasminogen activation; IEA:Ensembl. DR GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl. DR GO; GO:1905602; P:positive regulation of receptor-mediated endocytosis involved in cholesterol transport; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0044090; P:positive regulation of vacuole organization; IEA:Ensembl. DR GO; GO:0031340; P:positive regulation of vesicle fusion; IEA:Ensembl. DR GO; GO:0050767; P:regulation of neurogenesis; IEA:Ensembl. DR GO; GO:0006900; P:vesicle budding from membrane; IEA:Ensembl. 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; ANNEXIN A2-RELATED; 1. DR Pfam; PF00191; Annexin; 4. DR PRINTS; PR00196; ANNEXIN. DR PRINTS; PR00198; ANNEXINII. DR SMART; SM00335; ANX; 4. DR SUPFAM; SSF47874; Annexin; 1. DR PROSITE; PS00223; ANNEXIN_1; 2. DR PROSITE; PS51897; ANNEXIN_2; 4. PE 3: Inferred from homology; KW Annexin {ECO:0000256|ARBA:ARBA00023216, ECO:0000256|RuleBase:RU003540}; KW Basement membrane {ECO:0000256|ARBA:ARBA00022869}; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU003540}; KW Calcium/phospholipid-binding {ECO:0000256|ARBA:ARBA00023302, KW ECO:0000256|RuleBase:RU003540}; KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}; KW Repeat {ECO:0000256|RuleBase:RU003540}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}. SQ SEQUENCE 442 AA; 49978 MW; A0624289098E090C CRC64; MFPATVCVCV WVSHYESGEV LGSGRRGEGK GGGPGRGGAG TLLLLRMWQS IKTPPKTSRL CLKPDKLPAL SVLGAASFKM STVHEILCKL NLEGDHSTPA SAYGSVKAYN NFDAERDAIN IEAAIKTKDL KFEAIRKDEI VKEMDWIRKY MKGVDEVTIV NILTNRSNEQ RQDIAFAYQR RTKKELASAL KSALSGHLET VILGLLKTPA QYDASELKAS MKGLGTDEDS LIEIICSRTN QELYEINKVY REMYKTELEK DIISDTSGDF RKLMVALAKG KRAEDGSVID YELIDQDARE LYDAGVKRKG TDVPKWISIM TERSVCHLQK VFERYKSYSP YDMLESIKKE VKGDLENAFL NLVQCIQNKP LYFADRLYDS MKGKGTRDKV LIRIMVSRSE VDMLKIRSEF KRKYGKSLYY FIQQDTKGDY QKALLYLCGG DD //