ID F6XNC0_CIOIN Unreviewed; 1045 AA.
AC F6XNC0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCINP00000024886.2};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000024886.2, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000024886.2}
RP IDENTIFICATION.
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 EMBL; EAAA01001945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6XNC0; -.
DR STRING; 7719.ENSCINP00000024886; -.
DR Ensembl; ENSCINT00000025132.2; ENSCINP00000024886.2; ENSCING00000013582.2.
DR GeneTree; ENSGT00940000167229; -.
DR HOGENOM; CLU_004111_1_0_1; -.
DR InParanoid; F6XNC0; -.
DR OMA; FFNRAKY; -.
DR TreeFam; TF105391; -.
DR Proteomes; UP000008144; Chromosome 4.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 1.20.5.930; Bicelle-embedded integrin alpha(iib) transmembrane segment; 1.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 1.
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:SF122; INTEGRIN ALPHA-PS1; 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; 5.
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:UP000008144};
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..18
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT CHAIN 19..1045
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT /id="PRO_5001424478"
FT TRANSMEM 1014..1036
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003762"
FT REPEAT 23..93
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 292..355
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 356..413
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT REPEAT 419..481
FT /note="FG-GAP"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803"
FT DOMAIN 466..608
FT /note="Integrin alpha first immunoglubulin-like"
FT /evidence="ECO:0000259|Pfam:PF08441"
FT DOMAIN 633..774
FT /note="Integrin alpha second immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20805"
FT DOMAIN 793..998
FT /note="Integrin alpha third immunoglobulin-like"
FT /evidence="ECO:0000259|Pfam:PF20806"
SQ SEQUENCE 1045 AA; 114298 MW; 645C08AD004B1AF8 CRC64;
MELTFLFSIA MLFSCTMGYN LEGRLPLYKS GGTNSTFGFS VALHKLSIDP GSSLEKSLLV
VGSPTAEALP SQTNAVKPGG IYHCPVSTNS EDCTRIAMDL GESSRTNNKT GQWLGVSLKS
QGAGKYLITC AHRHSMRLYS RVNEVERLCG KCFLLNGKYT KNEDLNHTCY SLCKRAPDHD
GADYAQAGTS AAFAGDNEYL IGGPGMWSWT GGMFDIQMAD LEATEALDIF TSSTAIIPLR
RDSYLGFSVA SSNAIKPGET TYVAGAPRGN YTGAIVMYRK ISDGLSKSLA PILTDTILGE
FIGSGFGFSV ATIDVNGDGL DDLLVGAPQY YEYSNEGKHG GAVYVYINQR GVAFSQITPK
KLLGSLDSFF GYSIASVGDI DQDGYIDFAV GAPQEKPNGK VYIFRGSADG NVKQSQVFNG
ANFTDIKPDV KGFGVSLSGA VDIDNNKYPD LLVGTLSDYV VLLRRSRPVI TIESSLSASP
TSLDLRNPNC TLASKTYSCF ELQFCFRYNA RHKEYTEILP IHYSITLDSE LQKERKAARV
AFASPQGPSL MSDVANVPRA GNYFRNSQYI YSMSSEDRLR PIKIDFEFNL ASEINGVKRE
RPDQPVFNMI NDPIMDADFP HARTSVVNLA NNCGDDGCQS NLKLRGSIPP EVVVEENFNY
RSFKSTLTLL LCRDSKMLLS LNVTNDGEEA HQAVVSAKLP AWVYYDNYTV TRSSGAEIVC
TTSDIGGSTF VVCTLGNPYV EGSADTIDIL LDVQQLTADT KQIVIEVTGS TTSINPEIPP
TPLYSDVIIQ MMLSLSGYGK PQQVRYVNAP IKGESAIHYT NEIGPFVEYT FTVKNDGRGL
QLANGVRLIV DFPIEINNGK WLMYLVSAHV RSGGLQIVGE CEQQYQNTLH FKLPVTASVS
AARRTKREAK ASSLYEPRRL SSTQSGSNFV TLDCHGDTAR CVKIGCTLDP IQPGSTTSVN
LQARLWNNTF LEEFVDIDLV NVAASATVSN IDSNVRITGS PTHEVMSVKS SFPWWYILIG
ILIALIIYII IIYLLIKCGF FKRKK
//
