ID A0A2Y9KZF1_ENHLU Unreviewed; 1168 AA.
AC A0A2Y9KZF1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Integrin alpha-E isoform X1 {ECO:0000313|RefSeq:XP_022376714.1};
GN Name=LOC111158754 {ECO:0000313|RefSeq:XP_022376714.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022376714.1};
RN [1] {ECO:0000313|RefSeq:XP_022376714.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022376714.1};
RG RefSeq;
RL Submitted (NOV-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 RefSeq; XP_022376714.1; XM_022521006.1.
DR AlphaFoldDB; A0A2Y9KZF1; -.
DR STRING; 391180.A0A2Y9KZF1; -.
DR KEGG; elk:111158754; -.
DR OrthoDB; 3816176at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR000413; Integrin_alpha.
DR InterPro; IPR048285; Integrin_alpha_Ig-like_2.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF79; INTEGRIN ALPHA-E; 1.
DR Pfam; PF01839; FG-GAP; 2.
DR Pfam; PF20805; Integrin_A_Ig_2; 1.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR01185; INTEGRINA.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00191; Int_alpha; 4.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 2.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS51470; FG_GAP; 3.
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 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:UP000248482};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003762};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU003762}.
FT TRANSMEM 1110..1136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT DOMAIN 192..372
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 487..547
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 550..614
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 618..678
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 1168 AA; 130802 MW; BC32F7507F208092 CRC64;
MLLSLYPPTM PVQSLAPLVA FNVDEAQIWV TPEGDTPYVL SSLLHQDPST NKTWLLVTGP
QTKEEGGLLH CCSLIQDKIS CKRVETVPIP KGRYRGVTVV RNHHSVLICM QVRTPQPHSL
SSELTGTCSL LSNNFQNHTQ VHFSNLENLD PSAHVDDRDC YRNKKGNTEK PARWRRALKI
QEEEEEEEAG TEIAIILDGS GSIEPPDFQR AKDFISNMMQ NFYKKCFQCS FALVQYGAVI
QTEFDLRDSQ DVRASLARVQ NITQVGSVTK TASAMQHVLD NIFTPSHGSR KNASKVMVVL
TDGDIFEDPL NLTTVINSPK MQGVERFAIG VGEAFEKNRT YNELKLIASD PDDRYAFKVT
NYTALDGLLS KLQENIIQME GMVGEALHYQ LAQIGFSAQI LDKRQVLLGA VGAFNWSGGA
LLYDMHSRRG RFLNHTAADT ENAQYSYLGY AVALLHKACG LAYVAGAPRY KQRGAVFELQ
KEGRETNFVP VLEGEQMGSY FGSELCPVDI DMDGTTDFLL VAAPFYHIHG EEGRVYVYYL
NEQNGSFSLA YTLSGHPGFT NVRFGFAMAT IGDISQDNLT DVAIGAPLEG FEAADGNSFG
SVYIYNGRQD GLFTSPSQRI KASAMASGLH YFGMSVAGGL DLTGDRLPDI TVGTLGRATV
LRSRPVVNLK VSMTFTPVAL PIGFNRSVNA RLCFEINPMT TVANSGFRET FLNFTMDVDV
VKQRKRLQCS DKSICQSHCR EWDSSMSQLC ESLLLIPTEG ELCEEDCFSN ISISISYQLQ
TSEGQRDHPQ PVLDFYTKPF TIFQLPYEKN CKNKLFCVAE LQMATTISQQ ELVVGLTKEL
TMNINLTNSG EDSYMTTMNL NYPRNLQFKR IQKPPSPDIH CDDPKPNASE LAMNCKIGHP
VLKRSSANFS VVWQLEENAF PNRTADITVT VTNFNDRNSS VKQSHSLQFK HAFIAVLPKP
SVMYMNTSQG LSVYKEFLFN IHGENLFRAV FQLQICVPIK LQGLQFIRVK NLTKIQANTK
CNYSLEKECG KDPVWYVDQW YSVNCTITSN KENVTVAAEL SLNQSQQLPR GVNELQILGE
IYFDKSLYEG LNAENHRTEI TVIFLKEERY LPVFVIIIIS SGCGLLALTL IIIILFQCGF
FKRKYQNLNL DNTRKTQLKS ENLLTEDN
//