ID   Q5TZZ9_HUMAN            Unreviewed;       346 AA.
AC   Q5TZZ9;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Annexin {ECO:0000256|RuleBase:RU003540};
GN   Name=ANXA1 {ECO:0000313|EMBL:ADZ76495.1};
GN   ORFNames=hCG_17305 {ECO:0000313|EMBL:EAW62545.1};
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 {ECO:0000313|EMBL:AAV38719.1};
RN   [1] {ECO:0000313|EMBL:EAW62545.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:CAG28612.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AAV38719.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) System Donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:EAW62545.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:ADO22239.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hoernsten L., Su C., Osbourn A.E., Hellman U., Wernstedt C., Oliw E.H.;
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:ADZ76495.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Perez Solis E.E.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:MOY33937.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Deslattes Mays A., Schmidt M.O., Graham G.T., Tseng E., Baybayan P.,
RA   Sebra R., Sanda M., Mazarati J.-B., Riegel A.T., Wellstein A.;
RT   "Single molecule real time (SMRT) full length RNA-sequencing reveals novel
RT   and dsitinct mRNA isoforms in human bone marrow cell subpopulations.";
RL   J. ISSAAS 1:1-18(2019).
CC   -!- INTERACTION:
CC       Q5TZZ9; O14770: MEIS2; NbExp=3; IntAct=EBI-10181435, EBI-2804934;
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004221}. Basolateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00004187}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004296}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004296}; Extracellular side
CC       {ECO:0000256|ARBA:ARBA00004296}. Cell projection, cilium
CC       {ECO:0000256|ARBA:ARBA00004138}. Cell projection, phagocytic cup
CC       {ECO:0000256|ARBA:ARBA00004231}. Cytoplasmic vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004284}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004284}. Cytoplasmic vesicle, secretory vesicle
CC       lumen {ECO:0000256|ARBA:ARBA00004263}. Early endosome
CC       {ECO:0000256|ARBA:ARBA00004412}. Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004481}. Lateral cell membrane
CC       {ECO:0000256|ARBA:ARBA00004124}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}. Secreted, extracellular exosome
CC       {ECO:0000256|ARBA:ARBA00004550}. Secreted, extracellular space
CC       {ECO:0000256|ARBA:ARBA00004239}.
CC   -!- DOMAIN: The full-length protein can bind eight Ca(2+) ions via the
CC       annexin repeats. Calcium binding causes a major conformation change
CC       that modifies dimer contacts and leads to surface exposure of the N-
CC       terminal phosphorylation sites; in the absence of Ca(2+), these sites
CC       are buried in the interior of the protein core. The N-terminal region
CC       becomes disordered in response to calcium-binding.
CC       {ECO:0000256|RuleBase:RU003540}.
CC   -!- SIMILARITY: Belongs to the annexin family.
CC       {ECO:0000256|ARBA:ARBA00007831, ECO:0000256|RuleBase:RU003540}.
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DR   EMBL; BT019896; AAV38699.1; -; mRNA.
DR   EMBL; BT019916; AAV38719.1; -; mRNA.
DR   EMBL; BT019917; AAV38720.1; -; mRNA.
DR   EMBL; GQ891377; ADO22239.1; -; mRNA.
DR   EMBL; GU997628; ADZ76495.1; -; Genomic_DNA.
DR   EMBL; CR407684; CAG28612.1; -; mRNA.
DR   EMBL; CH471089; EAW62545.1; -; Genomic_DNA.
DR   EMBL; GHIR01000001; MOY33937.1; -; Transcribed_RNA.
DR   EMBL; GHIR01000012; MOY33948.1; -; Transcribed_RNA.
DR   EMBL; GHIR01000018; MOY33953.1; -; Transcribed_RNA.
DR   RefSeq; NP_000691.1; NM_000700.2.
DR   RefSeq; XP_011516911.1; XM_011518609.1.
DR   SMR; Q5TZZ9; -.
DR   IntAct; Q5TZZ9; 1.
DR   Antibodypedia; 2190; 1427 antibodies from 52 providers.
DR   DNASU; 301; -.
DR   GeneID; 301; -.
DR   KEGG; hsa:301; -.
DR   UCSC; uc004ajf.2; human.
DR   CTD; 301; -.
DR   PharmGKB; PA24823; -.
DR   VEuPathDB; HostDB:ENSG00000135046; -.
DR   HOGENOM; CLU_025300_0_0_1; -.
DR   OMA; FMENQEQ; -.
DR   OrthoDB; 1500773at2759; -.
DR   BioGRID-ORCS; 301; 13 hits in 1173 CRISPR screens.
DR   ChiTaRS; ANXA1; human.
DR   GenomeRNAi; 301; -.
DR   ExpressionAtlas; Q5TZZ9; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031514; C:motile cilium; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0042383; C:sarcolemma; 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:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0046632; P:alpha-beta T cell differentiation; IEA:Ensembl.
DR   GO; GO:0050482; P:arachidonic acid secretion; IEA:Ensembl.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; IEA:Ensembl.
DR   GO; GO:0001780; P:neutrophil homeostasis; IEA:Ensembl.
DR   GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
DR   GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; IEA:Ensembl.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0032652; P:regulation of interleukin-1 production; IEA:Ensembl.
DR   GO; GO:0002685; P:regulation of leukocyte migration; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IEA:Ensembl.
DR   Gene3D; 1.10.220.10; Annexin; 4.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR018502; Annexin_repeat.
DR   InterPro; IPR018252; Annexin_repeat_CS.
DR   InterPro; IPR037104; Annexin_sf.
DR   InterPro; IPR002388; ANX1.
DR   PANTHER; PTHR10502; ANNEXIN; 1.
DR   PANTHER; PTHR10502:SF17; ANNEXIN A1; 1.
DR   Pfam; PF00191; Annexin; 4.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR00197; ANNEXINI.
DR   SMART; SM00335; ANX; 4.
DR   SUPFAM; SSF47874; Annexin; 1.
DR   PROSITE; PS00223; ANNEXIN_1; 3.
DR   PROSITE; PS51897; ANNEXIN_2; 4.
PE   1: Evidence at protein level;
KW   Adaptive immunity {ECO:0000256|ARBA:ARBA00023130};
KW   Annexin {ECO:0000256|ARBA:ARBA00023216, ECO:0000256|RuleBase:RU003540};
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU003540};
KW   Calcium/phospholipid-binding {ECO:0000256|ARBA:ARBA00023302,
KW   ECO:0000256|RuleBase:RU003540};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Immunity {ECO:0000256|ARBA:ARBA00023130};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phospholipase A2 inhibitor {ECO:0000256|ARBA:ARBA00023005};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU003540}.
SQ   SEQUENCE   346 AA;  38714 MW;  14B42E1FA4178EC0 CRC64;
     MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV
     DEATIIDILT KRNNAQRQQI KAAYLQETGK PLDETLKKAL TGHLEEVVLA LLKTPAQFDA
     DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL
     LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY
     TKYSKHDMNK VLDLELKGDI EKCLTAIVKC ATSKPAFFAE KLHQAMKGVG TRHKALIRIM
     VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN
//