ID M3ZRT1_XIPMA Unreviewed; 1178 AA.
AC M3ZRT1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Integrin subunit alpha 1 {ECO:0000313|Ensembl:ENSXMAP00000004924.2};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000004924.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000004924.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000004924.2};
RG Ensembl;
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_014324128.1; XM_014468642.1.
DR AlphaFoldDB; M3ZRT1; -.
DR STRING; 8083.ENSXMAP00000004924; -.
DR Ensembl; ENSXMAT00000004929.2; ENSXMAP00000004924.2; ENSXMAG00000004890.2.
DR GeneID; 102222514; -.
DR KEGG; xma:102222514; -.
DR CTD; 3672; -.
DR eggNOG; KOG3637; Eukaryota.
DR GeneTree; ENSGT00940000157646; -.
DR HOGENOM; CLU_004111_2_1_1; -.
DR InParanoid; M3ZRT1; -.
DR OMA; THTFLAI; -.
DR OrthoDB; 3816176at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:UniProt.
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 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 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; IPR018184; Integrin_alpha_C_CS.
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 InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR23220; INTEGRIN ALPHA; 1.
DR PANTHER; PTHR23220:SF22; INTEGRIN ALPHA-1; 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 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; 5.
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 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:UP000002852};
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..24
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 25..1178
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5017103047"
FT TRANSMEM 1135..1159
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 29..87
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 168..354
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REPEAT 365..416
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 476..538
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 554..613
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 617..677
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
SQ SEQUENCE 1178 AA; 131238 MW; 2771426ADCDDDF13 CRC64;
MLRLSQISTL TAAAVVVLLT CVLSFNVDQK NAMSFSGPLD DMFGYTVQQF ENSEGKWVLI
GSPHSGQPAK RTGDVYKCPV GRGDNTCIKL ELPKNTTVPN LHEVKENMTM GTTLVTNPTG
GFMACGPQYG YMCGQQQYIS GVCANVSPSF QILNSIAPGV QNCTSNLDIV FVLDGSNSIY
PWGRIVDFLV RFLERVQVGP KLSQVGIVSY GQDVKHHVNL SQFNNNKDLL KFVRRIPQHT
GTKTHTFLAI DTARKEAFTQ ERGARTDAKK VMVILTDGES HDNHMQNKVI GECDQDHIER
FGIAVLGYYK RENKSEEDVQ KFIDEIKSIS SKPIQDHFFN VSDELFLVNL ADTLGRKIFA
LEATSGNFTS SFEMEMSQAG FSAHASKDGL LLGAVGAYDW NGTVVMQTAE STITPEKDEF
YDPKDNKTGR GLAEYLGYDV QSASTPKGVL YITGAPRYNH TGRVVIYQLT KESRVETVQI
LRGEQIGSYF GSVLQTVDVN NDSYTDLLLV GAPMYMGPER NEQGKVYVYK LNEKGKFVHK
FNLKPVNQSC CSVNSDGCTM KNEPCGARFG TAIAAVSDLN LDGFNDVVIG APFENDHRGA
VYIYHGHKSN PYLNLVQHIP AGGDGEKVKF FGQSIHGIMD LNGDGIVDVT IGGLGGASLF
WSRDVAQVTS SMTFEPTKIN LQHSQYQCEH RGHKSVCVDT TVCFQYQVKS EKRHASATEI
RYNVTLDVLR SKARASFIDQ DLDKSDRKVT KTFLISNGQR ICKTERFIMS AQLDFKDPFN
VTLEFGLTNE DQGPVLDANL PRSITKTIPL VDCGDQLKCI TDLSLTAVPS EKSMLIPVKS
KDKLDVKIDI INKKDNAYNT KVILNFTPNI NYVKVEPEKE CTPDHMKVEC AVGYPFLGSN
AKESFKVRFE TDSTHIYENI HINVTTISDS EENPNTLHDN NVEISLPVKY EAGVIFSVSH
AEKHIIIKDG EQYSLKDSDF GRMTEEVNIS YTVEKAGSTL TPPLDLKVMY PYRSPLDNVL
LFWTSVVSST GVKCKEPPAP KHNKPKKETL TRFLLECGQT QCDSFSCFIP ETNKSQVNVT
FKVWKPTFIE GEFSSLKMMV NATLTFKQSH LFELGSNAKN RNVTIPISKE TVGGIPIWII
IISILIGLLI LALIIFIFWK LGFFKRKTRD YSKEEMSD
//
