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Database: UniProt
Entry: A0A096NHY7_PAPAN
LinkDB: A0A096NHY7_PAPAN
Original site: A0A096NHY7_PAPAN 
ID   A0A096NHY7_PAPAN        Unreviewed;      1152 AA.
AC   A0A096NHY7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   27-MAR-2024, entry version 59.
DE   SubName: Full=Integrin subunit alpha M {ECO:0000313|Ensembl:ENSPANP00000012585.3};
GN   Name=ITGAM {ECO:0000313|Ensembl:ENSPANP00000012585.3};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000012585.3, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000012585.3, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000012585.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC       ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC       {ECO:0000256|ARBA:ARBA00008054, ECO:0000256|RuleBase:RU003762}.
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DR   AlphaFoldDB; A0A096NHY7; -.
DR   STRING; 9555.ENSPANP00000012585; -.
DR   Ensembl; ENSPANT00000018729.4; ENSPANP00000012585.3; ENSPANG00000017008.4.
DR   eggNOG; KOG3637; Eukaryota.
DR   GeneTree; ENSGT00940000161282; -.
DR   OMA; CQRIKCD; -.
DR   Proteomes; UP000028761; Chromosome 18.
DR   Bgee; ENSPANG00000017008; Expressed in bone marrow and 52 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0010668; P:ectodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0043315; P:positive regulation of neutrophil degranulation; IEA:Ensembl.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR   CDD; cd01469; vWA_integrins_alpha_subunit; 1.
DR   Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 2.
DR   Gene3D; 2.60.40.1460; Integrin domains. Chain A, domain 2; 1.
DR   Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR   Gene3D; 2.60.40.1530; ntegrin, alpha v. Chain A, domain 4; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   InterPro; IPR013649; Integrin_alpha_Ig-like_1.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR048633; ITGAX-like_Ig_3.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF130; INTEGRIN ALPHA-M; 1.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF08441; Integrin_A_Ig_1; 1.
DR   Pfam; PF20805; Integrin_A_Ig_2; 1.
DR   Pfam; PF00357; Integrin_alpha; 1.
DR   Pfam; PF21520; ITGAX-like_Ig_3; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00191; Int_alpha; 5.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF69179; Integrin domains; 3.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS51470; FG_GAP; 4.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW   ECO:0000256|RuleBase:RU003762};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU003762};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003762};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003762}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   CHAIN           17..1152
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT                   /id="PRO_5035340069"
FT   TRANSMEM        1106..1128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   REPEAT          18..75
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   DOMAIN          148..326
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   REPEAT          441..501
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          505..563
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          568..628
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ   SEQUENCE   1152 AA;  127396 MW;  89BF6E5F63E4A09E CRC64;
     MALRVLLLTA LTLCHGFNLD TENVMTFQEN AKGFGQSVVQ LQGSRVVVGA PQEIVAANQT
     GSLYQCDYSI GSCEPIRLQI PEEAVNMSLG LSLAATTSPP QLLACGPTMH QTCSENTYVK
     GLCFLFGSNL RQQPQKFPGT LRGCPEQDIA FLIDGSGSIN PREFQQMKDF VSIMMEQLKK
     SKTLFSLMQY SEEFWTHFTF KEFQRNPKPR SLVNSITQLY GRTHTATAIR KVVRELFNVN
     QGARKYARKI LVVITDGEKF GDPLGYEDVI PEADREGVIR YVIGVGDAFR SSKSRQELNT
     IASKPARDHV FQVNNFEALK TIQNQLQEKI FAIEGTQTGS ASSFEHEMSQ EGFSAAITSN
     GPLLSTVGSY DWAGGAFLYT SNEKSTFINM TRVDSDMNDA YLGYAATVIL RNRVQNLVLG
     APRYQHIGLV AMFRQNTGMW ESNANVKGTQ IGAYFGASLC SVDVDSNGST DLVLIGAPYY
     YEQTRGGQVS VCPLPRAQRG RWQCDAVLYG EQGQPWGRFG AALTVLGDVN GDKLTDVAIG
     APGEEDNQGA VYLFHGTSGF GISPSHSQRI AGSKLPSRLQ YFGQSLSGGQ DLTMDGLVDL
     SVGAQGHVLL VRSQPVLRVE ATMEFNPREV ARNVFECNDQ MVKGKEAGEV RVCLRVQKST
     RDRLREGQIQ SVVTYDLALD SGRPRSRAVF GETKNSTRRQ TKTLGLTQTC ETLKLQLPDC
     IEDPVSPIVL RLNFSLVGTP LSAFGNLRPV LAEDAQRLFI ALFPFEKNCG NDNICQDDLS
     ITFSFMSLDC LVVGGPREFN VTVTVRNDGE DSYRTQVTFF FPLGLSYRKV SRLQNQRSQR
     SWRLACESAS STEVPGALKS TSCSINHPIF PENSEVTFNI TFDVDSKASL GNKLLLKANV
     TSENNMSRTN KTEFQRELPV KYAVYMVVTS HEVSTKYINF TASENTSRVM QHQYQVKNLG
     QRSLPISLVF LVPVQLNQTI IWDRPQVTFS ESLSSTCHTE EILPTPYTDF LAKLQKDPVV
     NCSIAVCQRI KCDIPFFGIQ EEFNATLKGN LSFGWYIKTS HNHLLVVSTA EIMFNNSTFT
     LLAGQGAFVR AQTETKVELF EVPNPLPLIV GSSVGGLLLL AVITAVLYKL GFFKRQYKDM
     MSEGGPPGAE PQ
//
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