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
//