LAMC2_HORSE
ID LAMC2_HORSE Reviewed; 1190 AA.
AC Q8HZI9;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Laminin subunit gamma-2;
DE AltName: Full=Epiligrin subunit gamma;
DE AltName: Full=Kalinin subunit gamma;
DE AltName: Full=Laminin-5 subunit gamma;
DE AltName: Full=Nicein subunit gamma;
DE Flags: Precursor;
GN Name=LAMC2;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12230513; DOI=10.1046/j.1523-1747.2002.01852.x;
RA Spirito F., Charlesworth A., Linder K., Ortonne J.-P., Baird J.,
RA Meneguzzi G.;
RT "Animal models for skin blistering conditions: absence of laminin 5 causes
RT hereditary junctional mechanobullous disease in the Belgian horse.";
RL J. Invest. Dermatol. 119:684-691(2002).
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components. Ladsin exerts cell-scattering activity
CC toward a wide variety of cells, including epithelial, endothelial, and
CC fibroblastic cells.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end. Gamma-2 is a
CC subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=Major component.
CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC other laminin chains to form a coiled coil structure.
CC -!- DOMAIN: Domain IV is globular.
CC -!- MISCELLANEOUS: Binds heparin. {ECO:0000250}.
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DR EMBL; AY082802; AAM03454.1; -; mRNA.
DR RefSeq; NP_001075237.1; NM_001081768.1.
DR AlphaFoldDB; Q8HZI9; -.
DR SMR; Q8HZI9; -.
DR STRING; 9796.ENSECAP00000031292; -.
DR PaxDb; Q8HZI9; -.
DR GeneID; 791245; -.
DR KEGG; ecb:791245; -.
DR CTD; 3918; -.
DR InParanoid; Q8HZI9; -.
DR OrthoDB; 156553at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 6.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 7.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00180; EGF_Lam; 6.
DR SMART; SM00281; LamB; 1.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01248; EGF_LAM_1; 6.
DR PROSITE; PS50027; EGF_LAM_2; 6.
DR PROSITE; PS51115; LAMININ_IVA; 1.
PE 2: Evidence at transcript level;
KW Basement membrane; Cell adhesion; Coiled coil; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Heparin-binding;
KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1190
FT /note="Laminin subunit gamma-2"
FT /id="PRO_0000017076"
FT DOMAIN 28..83
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 84..130
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 139..186
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 187..196
FT /note="Laminin EGF-like 4; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 213..381
FT /note="Laminin IV type A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00458"
FT DOMAIN 382..415
FT /note="Laminin EGF-like 4; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 416..462
FT /note="Laminin EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 463..517
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 518..573
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 574..603
FT /note="Laminin EGF-like 8; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 604..1190
FT /note="Domain II and I"
FT /evidence="ECO:0000250"
FT COILED 613..718
FT /evidence="ECO:0000255"
FT COILED 809..1073
FT /evidence="ECO:0000255"
FT COILED 1114..1190
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1030
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..37
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 30..53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 56..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 68..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 84..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 86..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 104..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 116..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 139..150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 141..155
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 157..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 169..184
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 463..471
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 465..482
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 485..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 497..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 518..532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 520..539
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 542..551
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 554..571
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 574..586
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 576..592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 594..603
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 611
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 614
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1181
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1190 AA; 130846 MW; 5F8C8BAC3E93A595 CRC64;
MPALWLRCGL CLALLLPAAR ASSGSQVCDC NGKSRQCIFD QELHKQTGNG FRCLNCNDNT
DGIHCERCKA GFYRQRERDR CLPCNCNSKG SLSARCDNSG RCSCKPGVTG DRCDRCLPGF
HTLTDAGCAQ DQRLLDSKCD CDPAGISGPC DSGRCVCKPA VTGERCDRCR PGYYHLDGGN
PQGCTQCFCY GHSASCHSSG DYSVHKIISA FHQDVDGWKA VQRNGSPAKL QWSQRHRDIF
SSARRSDPVY FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR HPSAHDVILE GAGLRITAPL
MPLSKTLPCG ITKTYTFRLN EHPSSNWSPQ LSYFEYRRLL RNLTALRIRA TYGEYSTGYI
DNVTLISARP VSGAPAPWVE QCVCPVGYKG QFCQDCASGY KRDSARLGPF GTCIPCNCQG
GGACDPDTGD CYSGDENPDI PECADCPIGF YNDPQDPRSC KPCPCRNGFS CSVMPETEEV
VCNNCPQGVT GARCELCADG YFGDPFGERG PVRPCQPCQC NNNVDPSASG NCDRLTGRCL
KCIHNTAGVH CDQCKAGYYG DPLAPNPADK CRACNCNPVG SEPVECRSDG SCVCKPGFGG
LSCEHAALTS CPACYNQVKV QMDQFMQQLQ ILEALISKAQ GGAVPNAELE GRMQQAEQAL
RDILREAQIS QDAVRSFNLR VAKARTQENS YRDRLDDLKM TVERVRALGS QYQNQVQDTR
RLITQMRLSL EESEASLQNT NIPPSEHYVG PNGFKSLAQE ATRLADSHVQ SASNMEQLAK
ETQEYSKELM SLVREALQEG GGSGSLDGAV VQRLVGKLQK TKSLAQELSR EATQTDMEAD
RSYQHSLHLL NSVSQIQGVN DQSLQVEAKR LRQKADSLSN RVTKHMDEFK HVQSNLGNWE
EETRQLLQNG KNGRQTSDQL LSRANLAKSR AQEALSMGNA TFYEVENILK NLREFDLQVG
DKRAEAEEAM KRLSYISQKV AGASDKTKQA EAALGSAAAD AQRAKNAARE ALEISGKIEQ
EIGGLNLEAN VTADGALAME KGLATLKSEM REVEGELSRK EQEFDMDMDA VQMVIAEAQR
VENRAKNAGV TIQDTLNTLD GILHLIDQPG SVDEERLILL EQKLFRAKTQ INSQLRPLMS
ELEERAHRQK GHLRFLETSI DGILADVKNL ENIRDNLPPG CYNTQALEQQ
