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Database: UniProt
Entry: H2ZIA7_CIOSA
LinkDB: H2ZIA7_CIOSA
Original site: H2ZIA7_CIOSA 
ID   H2ZIA7_CIOSA            Unreviewed;      3032 AA.
AC   H2ZIA7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Laminin subunit alpha-2 {ECO:0008006|Google:ProtNLM};
OS   Ciona savignyi (Pacific transparent sea squirt).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC   Cionidae; Ciona.
OX   NCBI_TaxID=51511 {ECO:0000313|Ensembl:ENSCSAVP00000017323.1, ECO:0000313|Proteomes:UP000007875};
RN   [1] {ECO:0000313|Proteomes:UP000007875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Birren B., Nusbaum C., Abebe A., Abouelleil A., Adekoya E., Ait-zahra M.,
RA   Allen N., Allen T., An P., Anderson M., Anderson S., Arachchi H.,
RA   Armbruster J., Bachantsang P., Baldwin J., Barry A., Bayul T.,
RA   Blitshsteyn B., Bloom T., Blye J., Boguslavskiy L., Borowsky M.,
RA   Boukhgalter B., Brunache A., Butler J., Calixte N., Calvo S., Camarata J.,
RA   Campo K., Chang J., Cheshatsang Y., Citroen M., Collymore A., Considine T.,
RA   Cook A., Cooke P., Corum B., Cuomo C., David R., Dawoe T., Degray S.,
RA   Dodge S., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A.,
RA   Elkins T., Engels R., Erickson J., Farina A., Faro S., Ferreira P.,
RA   Fischer H., Fitzgerald M., Foley K., Gage D., Galagan J., Gearin G.,
RA   Gnerre S., Gnirke A., Goyette A., Graham J., Grandbois E., Gyaltsen K.,
RA   Hafez N., Hagopian D., Hagos B., Hall J., Hatcher B., Heller A.,
RA   Higgins H., Honan T., Horn A., Houde N., Hughes L., Hulme W., Husby E.,
RA   Iliev I., Jaffe D., Jones C., Kamal M., Kamat A., Kamvysselis M.,
RA   Karlsson E., Kells C., Kieu A., Kisner P., Kodira C., Kulbokas E.,
RA   Labutti K., Lama D., Landers T., Leger J., Levine S., Lewis D., Lewis T.,
RA   Lindblad-toh K., Liu X., Lokyitsang T., Lokyitsang Y., Lucien O., Lui A.,
RA   Ma L.J., Mabbitt R., Macdonald J., Maclean C., Major J., Manning J.,
RA   Marabella R., Maru K., Matthews C., Mauceli E., Mccarthy M., Mcdonough S.,
RA   Mcghee T., Meldrim J., Meneus L., Mesirov J., Mihalev A., Mihova T.,
RA   Mikkelsen T., Mlenga V., Moru K., Mozes J., Mulrain L., Munson G.,
RA   Naylor J., Newes C., Nguyen C., Nguyen N., Nguyen T., Nicol R., Nielsen C.,
RA   Nizzari M., Norbu C., Norbu N., O'donnell P., Okoawo O., O'leary S.,
RA   Omotosho B., O'neill K., Osman S., Parker S., Perrin D., Phunkhang P.,
RA   Piqani B., Purcell S., Rachupka T., Ramasamy U., Rameau R., Ray V.,
RA   Raymond C., Retta R., Richardson S., Rise C., Rodriguez J., Rogers J.,
RA   Rogov P., Rutman M., Schupbach R., Seaman C., Settipalli S., Sharpe T.,
RA   Sheridan J., Sherpa N., Shi J., Smirnov S., Smith C., Sougnez C.,
RA   Spencer B., Stalker J., Stange-thomann N., Stavropoulos S., Stetson K.,
RA   Stone C., Stone S., Stubbs M., Talamas J., Tchuinga P., Tenzing P.,
RA   Tesfaye S., Theodore J., Thoulutsang Y., Topham K., Towey S., Tsamla T.,
RA   Tsomo N., Vallee D., Vassiliev H., Venkataraman V., Vinson J., Vo A.,
RA   Wade C., Wang S., Wangchuk T., Wangdi T., Whittaker C., Wilkinson J.,
RA   Wu Y., Wyman D., Yadav S., Yang S., Yang X., Yeager S., Yee E., Young G.,
RA   Zainoun J., Zembeck L., Zimmer A., Zody M., Lander E.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAVP00000017323.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Secreted, extracellular space, extracellular matrix, basement membrane
CC       {ECO:0000256|ARBA:ARBA00004302}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR   Ensembl; ENSCSAVT00000017512.1; ENSCSAVP00000017323.1; ENSCSAVG00000010201.1.
DR   GeneTree; ENSGT00940000161177; -.
DR   Proteomes; UP000007875; Unassembled WGS sequence.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   CDD; cd00055; EGF_Lam; 14.
DR   CDD; cd00110; LamG; 5.
DR   Gene3D; 2.60.120.200; -; 5.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.10.25.10; Laminin; 11.
DR   Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR010307; Laminin_dom_II.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR000034; Laminin_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   InterPro; IPR002049; LE_dom.
DR   PANTHER; PTHR10574:SF436; -; 1.
DR   PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR   Pfam; PF00052; Laminin_B; 2.
DR   Pfam; PF00053; Laminin_EGF; 16.
DR   Pfam; PF00054; Laminin_G_1; 4.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   Pfam; PF06009; Laminin_II; 1.
DR   Pfam; PF00055; Laminin_N; 1.
DR   PRINTS; PR00011; EGFLAMININ.
DR   SMART; SM00181; EGF; 8.
DR   SMART; SM00180; EGF_Lam; 16.
DR   SMART; SM00281; LamB; 2.
DR   SMART; SM00282; LamG; 5.
DR   SMART; SM00136; LamNT; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 10.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 5.
DR   PROSITE; PS50027; EGF_LAM_2; 9.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 5.
DR   PROSITE; PS51115; LAMININ_IVA; 2.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   4: Predicted;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW   ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007875};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          1..250
FT                   /note="Laminin N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51117"
FT   DOMAIN          439..487
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          508..696
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          725..774
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          833..880
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          881..929
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          930..976
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1023..1068
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1069..1126
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1148..1333
FT                   /note="Laminin IV type A"
FT                   /evidence="ECO:0000259|PROSITE:PS51115"
FT   DOMAIN          1412..1472
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1473..1519
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          2064..2246
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2260..2440
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2445..2629
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2691..2863
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          2868..3032
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          517..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2641..2671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2641..2657
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        458..467
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        744..753
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        852..861
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        864..878
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        881..893
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        883..900
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        902..911
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        930..942
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        950..959
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1023..1035
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1025..1042
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1044..1053
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1069..1081
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1097..1106
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1443..1452
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1473..1485
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1475..1492
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1494..1503
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   3032 AA;  334676 MW;  B4639FFE97D27BF6 CRC64;
     GLFPSVVNLA SHAEITSNAT CGERGPDKFC KLVQHVDRRT DRGQQCGICD QFSRNPSERH
     AVENAIDGRG DRWWQSPTID QGYQYHRVTL TLDLKQVFQV AYVIIKAANS PRPGNWILEK
     STDGVTWSPW QYFATSDREC LLKYGKVASQ LGAPNYKTDS EVMCTTYFSR LNPFQNGEIH
     VSLINGRPSA ENPSFELVDF TSARYIRLRL QKIRTLHGDL MTLSIGSTQN DPSVTRRYYY
     SIKDISIGGM CICYGHASTC PTNTQNGLFH CACEHNTVGF NCERCAPGFH QYKWMPGNNG
     FQCEECNCHG HATECYYDPA VNERGDSLNT RGEYIGGGVC VGCRDGTAGI NCQSCVDGMY
     RPLDVEADSS HPCLPCNCNA YGGTRISDSG PYNCVKDIDH IDAENDLFPG SCYCKVGYTG
     QQCDKCAFGY TGFPYCEPCP CNTSGSLNID PCIGDCACKE HVTGDNCNQC KVGFYNLQRN
     NPMGCDECFC NGATQSCVSS NLRWSTIHTN EGWEVRDQRG RRRTRPQIDP DLHEPYVEHG
     PTARELGTTM YYWSAPARYL GNKLNSYGGT LRYTVSYDIL QGAQPMPIQA NDIILDGNGR
     TVIYNHRGML ISPEIETEVA LKLASSVFGS RDGWVNAESL QPVSKADMIA VLSNLRRILI
     RAVYSRNIGA VYRIHDVYMD SATPEGKGLP ASSVEICHCP PGYTGYSCQD CATGYWRNGE
     QCFPCNCNHH SNICNKLNGA CENCQHSTIG IHCERCKPGY YGNALNGTSE DCQRCSCPLA
     TTSNNFSPTC RLDKTGDMMC LECAVGNSGK RCETCSDGYF GNPFAPGGSC QPCSCNGNSG
     ACNQLNGVCK FCKGHTAGDH CERCEAAYYG DAILRKNCGP CECNPIGSLS RQCDFVTGQC
     PCRQDVYGRK CDACASNNYL SIEEKMCVPC DCNPIGSIMM QCRSDGSCVC RTGVVGKTCG
     ICSTGYHSFG DGGCIECDCT HTNGHCNPAT GECVCPANTH GEGCMNCVDG SYQWSLNNGC
     TLCNCSKAGS TSFTCDNITG QCPCKFEYTD KTCNRCRPGY YGYPNCKACN CLVDGTQAST
     CLNDGTCECS DDGQCLCKAN VQGLHCDRCV AGAFGLSNEN EVGCTTCFCG VTNQCQQATY
     YWGNPISLSL APVEVTNEIA SRSTVGVADD IALLDSNTAV RAMRSGPYYW RLPPQFNGDR
     RLSYGGKLRY TIYFVSEFST PPGMRPEASV IIQGGNLQTI KYSMEDPHIK QTRAYVVPMQ
     EFGWAHLDSN KNVTRDEFSL ILQNVNSILI KASYGFLMDQ SRLSEVYLDV AVAGVTGRGD
     SATDLPPAYG IEECICPPGY SGLSCQNCMA GYMRVQREPN LGMCELCNCF NRSDSCDIFT
     GKCLNCIDKF VGHNCETCET GYYFSGNSCH KCECPGAGAI NNFSPTCHSD GSDGIASYTC
     DACQIGYEGK HCERCADGYF GDPTVPGGFC AKCGCNVAGS LDGACDKVTG QCNCDEGIKG
     RICDRCSDKH VITTEGCREC NDECAGKLLL EIEEMVNRTN DVDIRDMFPP PWNRLIGARN
     VTAQLQNVFA PSFLYTLTDS STSCITVSSN ASGKVNATRE HVKQQILQTA ELNNTVEIFF
     LNKGPKSIFI TAVSNMATRL LHGLQNGTAQ DAADIYSKVD IKMNEMRARN INQYKEMADT
     ELEFAKDMLE LVYTNFTARA NQTEPQAHLF NEELIKQVGE IETKFRHLQM ELSNASTDIR
     VATTKNVLNS QTLRQTMGNI ERINNMATMT NVTLDEAQKI VNAAIDLYKS GLQNMEAVTL
     HNNNILGSDL QGLQMSSVKS AVEHSAQLQE DARMMLEVYK NVSAFSYNQT EAASRWTNII
     RLLVRANKTS KTAIKQGKAA LSTATTDLGI RANESLLRNM AILNEVAELR NTVNGDRDLL
     RSLEDHLRSS NHSALNLTDQ HNRLLSRIDK INAAPSLTSN ELFTITRSSN KVLGEINKQL
     EGAQENVRLL GETELQVLQR SQIAKEVADN LDAVSEGMRS VSEAKERTTS KLERVQLASE
     SVRANISNIR QLIEDARRKA GSIRVSVSSK GKCAMAYKPT ITPGKTTEIV LTIQNSEPNN
     ALLYLARPRQ DYIVVELRDY KVTVTWDLGG GPGFVQNPLI IKADTENLRS SPDWRNQELN
     VTAYRESDKI ATMTNVGGVS PGSYSMLDIN NDDILFVGGI LNTTEVHEAV MYRTFNGCMG
     EAFLQGRTVG LWNFREINNP EDCKGCIEIE VATDKEQTNL YSYYGRSYSV LRFNNHDSKR
     TQISIRLQSF SSEGLIVYTG SATHPDFYSI ELNKGRIMLK LDLGNGVHNA STENQYNTGE
     WVQVTFRRFA GNSLLSIKTV NQSQENIWLR IQGSDESLNF TSGDVTCVGG FPSDRTIKAD
     VTKISFVGCL KEFSQNNLLR SLKSTVVEDV ARDSGVQTAC PAEITRDIGI SNKGFVELKP
     INLQPTSSIS ITFNTRNEDA VLLFATSDNR QLRRRRRQTD EAYYSMYVYD GFVHTALKLP
     GSPHIRLTSK FNIYNDGRDH TATLHRRREN ITLQMNEDGD YVSEYLPRGA DQTITVRRVF
     VGGIPAEFNS TKAVGTEKSL NGCVRDLMSN LLVNFKEAVQ AKNSYFGTCA FVEFEPQPTL
     TSATPPNTFT SNSMNPPKPP RATTPNTQPP LSNDPAMVPK QPNMVMIGNF SAHFGLSRNS
     HVTFKLKKNI AKNFMSFRFT FDLKVRTLGR NGILVYAGHK TQVDFFALKV KEGIPIFQFD
     NGRGRGEADG SIRINDGKWH RKIKEKRIHI RGWCKNKKTT SPKGANIMGV DNILYVGGLP
     ESFNSKKIGQ LSSMDACIKD LVLNRKRKLN LSKPRSAHKV DQCYKKMESG AFFNGKGYAI
     YSEKYRVGPR MLIEMEFRTW NPSGILLSIN NRRSDGLGIE LVNGSIYFRT DNGAGPFEAV
     YSDASTQHNT GRKVKFNLCD GRWHSLIANK DMNSLSLVVD GNAVPTVVSR ATTNSADTKD
     PLYVGGIPDG TTNQQQVRTN QNLQGCIRNV RL
//
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