GenomeNet

Database: UniProt
Entry: A0A452QNN0_URSAM
LinkDB: A0A452QNN0_URSAM
Original site: A0A452QNN0_URSAM 
ID   A0A452QNN0_URSAM        Unreviewed;      1011 AA.
AC   A0A452QNN0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Integrin subunit alpha 2b {ECO:0000313|Ensembl:ENSUAMP00000006957.1};
GN   Name=ITGA2B {ECO:0000313|Ensembl:ENSUAMP00000006957.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000006957.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000006957.1}
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; A0A452QNN0; -.
DR   Ensembl; ENSUAMT00000007887.1; ENSUAMP00000006957.1; ENSUAMG00000004666.1.
DR   GeneTree; ENSGT00940000160724; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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; IPR013649; Integrin_alpha_Ig-like_1.
DR   InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR   InterPro; IPR048286; Integrin_alpha_Ig-like_3.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR   PANTHER; PTHR23220:SF73; INTEGRIN ALPHA-IIB; 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; PF20806; Integrin_A_Ig_3; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 4.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR   SUPFAM; SSF69179; Integrin domains; 3.
DR   PROSITE; PS51470; FG_GAP; 4.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW   ECO:0000256|RuleBase:RU003762};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291022};
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..31
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   CHAIN           32..1011
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT                   /id="PRO_5018809408"
FT   TRANSMEM        977..999
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003762"
FT   REPEAT          38..96
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          287..352
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          354..413
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   REPEAT          416..477
FT                   /note="FG-GAP"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT   DOMAIN          462..613
FT                   /note="Integrin alpha first immunoglubulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF08441"
FT   DOMAIN          614..754
FT                   /note="Integrin alpha second immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20805"
FT   DOMAIN          760..967
FT                   /note="Integrin alpha third immunoglobulin-like"
FT                   /evidence="ECO:0000259|Pfam:PF20806"
FT   REGION          835..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..860
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1011 AA;  109836 MW;  A76ECE38C3525405 CRC64;
     MARAVCPLHA LWLLEWVQLL LGPGAIPAAW ALNLDPVQLT LYTGPNGSHF GFALDFYKDN
     HGRVAIVVGA PRTLGPSQEE TGGVFLCPWK AEGSQCTLLP FDLNDETRHV GSHTFQTFKS
     RQGLGASVVS WNDNIVACAP WQHWNALEKT EEAEKTPVGG CFVAQLQNGH RAEYSPCRAN
     TMSQVYVKNG FNDRRYCEAG FSSAVTQAGE LVLGAPGGYF FLGTCPIVSS YRPGTLLWHV
     PFQSFTFDYS KPEYYDGYRG NPGTSLLGLP ALSPPTPPVR SCPCGSAPTP TRGPTPMASY
     FGHSVTVTDV NGDGRHDLLV GAPLYMESRA DRKLAEVGRV YLFLQPRGHH VLGAPSLLLT
     GTQLYGRFGS AIAPLGDLDR DGYNDVAVAA PYGGPSGRGQ VLVFLGQSEG LSSRPSQILD
     SPFPAGSGFG FSLRGATDID DNGYPDLLVG AYGANKVAVY RAQPVVMASV QLLVQDSLNP
     AVKNCVLPQT QTLVSCFNIQ MCVGATGHNI PQQLPLSAEL QLDRQKPRQG RRVLLLNSQL
     AGTTLHLDLG GRQSPICHTT VAFLRDEADF RDKLSPIVLS FNVSLQPRKD GVAPGLVLHG
     DTHVQEQTRI ILDCGEDDLC VPQLQLTASV AGSPLLIGAD NVLELQMDAA NEGEGAYEAE
     LAVHLPPGAH YMRAVSNVEG FERLICNQKK ENETKMVLCE LGNPMKRNAR IGITMLVSVE
     NLEEAGEHVS FWLQTRSKNS QNPNSEAVLL DVPVRAEAHV ELRGNSFPAS LVVVAEEDNR
     ENSSDIWGPK VEHTYELHNN GPSTISGIHL SLCLPGQSQR SDLLYILDIE PQGGLQCSPQ
     PTPNPDKMNW RLPTPSPSPT SPGHHKRERR QASLPGSNQP AGLQDPILLS CDSGPHTVVQ
     CELREMARGQ RAMVRVLAFL QLPSLQQRPL DQFVLQSQAW FNVSSLPYAV PALSLPSGET
     QVQTRLLRAL EERDIPIWWV LVGVLGGLLL LMLLVLAMWK VRHEGESGVP R
//
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