ANXA9_HUMAN
ID ANXA9_HUMAN Reviewed; 345 AA.
AC O76027; Q5SZF1; Q6FI55; Q9BS00; Q9HBJ6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Annexin A9;
DE AltName: Full=Annexin XXXI;
DE AltName: Full=Annexin-31;
DE AltName: Full=Annexin-9;
DE AltName: Full=Pemphaxin;
GN Name=ANXA9; Synonyms=ANX31;
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], AND VARIANT GLY-166.
RC TISSUE=Liver, and Spleen;
RX PubMed=9742942; DOI=10.1016/s0014-5793(98)00997-1;
RA Morgan R.O., Fernandez M.-P.;
RT "Expression profile and structural divergence of novel human annexin 31.";
RL FEBS Lett. 434:300-304(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-166, TISSUE SPECIFICITY, FUNCTION,
RP SUBUNIT, AND IDENTIFICATION AS AN AUTOANTIGEN IN PV.
RX PubMed=10899159; DOI=10.1074/jbc.m003174200;
RA Nguyen V.T., Ndoye A., Grando S.A.;
RT "Pemphigus vulgaris antibody identifies pemphaxin. A novel keratinocyte
RT annexin-like molecule binding acetylcholine.";
RL J. Biol. Chem. 275:29466-29476(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-345, AND VARIANT GLY-166.
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Low affinity receptor for acetylcholine known to be targeted
CC by disease-causing pemphigus vulgaris antibodies in keratinocytes.
CC {ECO:0000269|PubMed:10899159}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10899159}.
CC -!- INTERACTION:
CC O76027; O60437: PPL; NbExp=6; IntAct=EBI-720960, EBI-368321;
CC -!- TISSUE SPECIFICITY: Expressed in the stratified squamous skin
CC epithelium, but not in epithelia of other types (at protein level).
CC {ECO:0000269|PubMed:10899159}.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05830.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA08933.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ009985; CAA08933.1; ALT_FRAME; mRNA.
DR EMBL; AF230929; AAG16780.1; -; mRNA.
DR EMBL; AL590133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005830; AAH05830.2; ALT_INIT; mRNA.
DR EMBL; CR536481; CAG38720.1; -; mRNA.
DR CCDS; CCDS975.2; -.
DR RefSeq; NP_003559.2; NM_003568.2.
DR AlphaFoldDB; O76027; -.
DR SMR; O76027; -.
DR BioGRID; 114002; 46.
DR IntAct; O76027; 4.
DR MINT; O76027; -.
DR STRING; 9606.ENSP00000357943; -.
DR iPTMnet; O76027; -.
DR PhosphoSitePlus; O76027; -.
DR BioMuta; ANXA9; -.
DR EPD; O76027; -.
DR jPOST; O76027; -.
DR MassIVE; O76027; -.
DR MaxQB; O76027; -.
DR PaxDb; O76027; -.
DR PeptideAtlas; O76027; -.
DR PRIDE; O76027; -.
DR ProteomicsDB; 50350; -.
DR Antibodypedia; 34042; 221 antibodies from 24 providers.
DR DNASU; 8416; -.
DR Ensembl; ENST00000368947.9; ENSP00000357943.4; ENSG00000143412.10.
DR GeneID; 8416; -.
DR KEGG; hsa:8416; -.
DR MANE-Select; ENST00000368947.9; ENSP00000357943.4; NM_003568.3; NP_003559.2.
DR UCSC; uc001ewa.3; human.
DR CTD; 8416; -.
DR DisGeNET; 8416; -.
DR GeneCards; ANXA9; -.
DR HGNC; HGNC:547; ANXA9.
DR HPA; ENSG00000143412; Low tissue specificity.
DR MIM; 603319; gene.
DR neXtProt; NX_O76027; -.
DR OpenTargets; ENSG00000143412; -.
DR PharmGKB; PA24837; -.
DR VEuPathDB; HostDB:ENSG00000143412; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000161835; -.
DR HOGENOM; CLU_025300_0_0_1; -.
DR InParanoid; O76027; -.
DR OMA; HNFQVEA; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; O76027; -.
DR TreeFam; TF105452; -.
DR PathwayCommons; O76027; -.
DR SignaLink; O76027; -.
DR BioGRID-ORCS; 8416; 19 hits in 1071 CRISPR screens.
DR ChiTaRS; ANXA9; human.
DR GeneWiki; ANXA9; -.
DR GenomeRNAi; 8416; -.
DR Pharos; O76027; Tbio.
DR PRO; PR:O76027; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O76027; protein.
DR Bgee; ENSG00000143412; Expressed in lower esophagus mucosa and 126 other tissues.
DR Genevisible; O76027; HS.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0015464; F:acetylcholine receptor activity; IDA:UniProtKB.
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:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0002020; F:protease binding; IBA:GO_Central.
DR GO; GO:0046790; F:virion binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:UniProtKB.
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; IPR009116; ANX9.
DR PANTHER; PTHR10502:SF122; PTHR10502:SF122; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01812; ANNEXINXXXI.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 1.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW Annexin; Reference proteome; Repeat.
FT CHAIN 1..345
FT /note="Annexin A9"
FT /id="PRO_0000067505"
FT REPEAT 41..112
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 113..184
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 197..266
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 270..341
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT VARIANT 28
FT /note="A -> T (in dbSNP:rs16832595)"
FT /id="VAR_048255"
FT VARIANT 114
FT /note="T -> A (in dbSNP:rs7536645)"
FT /id="VAR_048256"
FT VARIANT 119
FT /note="A -> T (in dbSNP:rs16832602)"
FT /id="VAR_048257"
FT VARIANT 166
FT /note="D -> G (in dbSNP:rs267733)"
FT /evidence="ECO:0000269|PubMed:10899159,
FT ECO:0000269|PubMed:9742942, ECO:0000269|Ref.5"
FT /id="VAR_022814"
FT VARIANT 225
FT /note="R -> Q (in dbSNP:rs775255778)"
FT /id="VAR_031212"
FT VARIANT 232
FT /note="R -> Q (in dbSNP:rs7542365)"
FT /id="VAR_048258"
SQ SEQUENCE 345 AA; 38364 MW; DF0FE611CA6D56B9 CRC64;
MSVTGGKMAP SLTQEILSHL GLASKTAAWG TLGTLRTFLN FSVDKDAQRL LRAITGQGVD
RSAIVDVLTN RSREQRQLIS RNFQERTQQD LMKSLQAALS GNLERIVMAL LQPTAQFDAQ
ELRTALKASD SAVDVAIEIL ATRTPPQLQE CLAVYKHNFQ VEAVDDITSE TSGILQDLLL
ALAKGGRDSY SGIIDYNLAE QDVQALQRAE GPSREETWVP VFTQRNPEHL IRVFDQYQRS
TGQELEEAVQ NRFHGDAQVA LLGLASVIKN TPLYFADKLH QALQETEPNY QVLIRILISR
CETDLLSIRA EFRKKFGKSL YSSLQDAVKG DCQSALLALC RAEDM
