ID M3XIF0_LATCH Unreviewed; 1189 AA.
AC M3XIF0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Laminin subunit gamma 2 {ECO:0008006|Google:ProtNLM};
GN Name=LAMC2 {ECO:0000313|Ensembl:ENSLACP00000022506.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000022506.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000022506.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {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 EMBL; AFYH01189957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01189958; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01189959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006008025.1; XM_006007963.2.
DR AlphaFoldDB; M3XIF0; -.
DR STRING; 7897.ENSLACP00000022506; -.
DR Ensembl; ENSLACT00000025713.1; ENSLACP00000022506.1; ENSLACG00000006588.2.
DR GeneID; 102359091; -.
DR KEGG; lcm:102359091; -.
DR CTD; 3918; -.
DR eggNOG; KOG1836; Eukaryota.
DR GeneTree; ENSGT00940000158069; -.
DR HOGENOM; CLU_002471_0_0_1; -.
DR OMA; NCKSAIM; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000006588; Expressed in pelvic fin and 5 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00055; EGF_Lam; 7.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF313; LAMININ SUBUNIT GAMMA-2; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 6.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00180; EGF_Lam; 8.
DR SMART; SM00281; LamB; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50027; EGF_LAM_2; 3.
DR PROSITE; PS51115; LAMININ_IVA; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Secreted {ECO:0000256|ARBA:ARBA00022869}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1189
FT /note="Laminin subunit gamma 2"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004043728"
FT DOMAIN 89..135
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 144..193
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 220..388
FT /note="Laminin IV type A"
FT /evidence="ECO:0000259|PROSITE:PS51115"
FT DOMAIN 522..577
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 649..676
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 705..830
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 874..908
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1035..1073
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1138..1172
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 89..101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 109..118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 164..173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 546..555
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1189 AA; 130994 MW; 4DC77BCA7D5892C6 CRC64;
MHLNAMWSVL ILWGYFFVLD PPQVSATFRW HSCNCNGKST RCVFDVNLYK QTGNGYRCIN
CIDNTDGPSC ERCKAGFYRQ QAGDRCFPCS CNAQGSKTSQ CDNNGRCTCK PGVMGDKCDR
CQPGYRSLSE VGCQRRDAQS LSDCRCNPAG SAGPCDPSTG RCNCKSAIMG QNCDRCKPGY
YNLHQANPAG CMQCFCYGHS TDCTSTNRYS IHRISSAFNR GAEGWRALCR DGAQDQLKWS
PKYNDVYFIS RANGPVYFVA PSQFLGNQML SYGKNLSFAF RVDRGGRQPS PEDLVLEGAG
MRVTAPLPTL TKTLPCGITK TYTFRLDEHP SSNWSPQLSA ADFHRLLQNL TAIKIRATYG
LYSTGYLDDV TLVSAQPTPG ELAPWVESCT CPSGYEGQFC EKCAPGYKRE SLALGPFSQC
VPCNCLGGGT CDSETGECYL GDGPGISNCL SCQPGFYSLP EDPCNCRRCP CANSCSFNPE
TRTVICDGCP IGRTGDRCEL CSDGYYGDPH GVNGPAQPCR PCQCSNNVDP NAVGNCNRLT
GECLKCLYNT AGFYCDRCKD GFYGNALVGN PADRCKPCNC NPAGSQSPQC RNDGHCVCQQ
GFEGLKCEGT PCPTCYDQVR YKVDQHLGKL REMEAAFSRI STSQPPVNSQ ELEYKLNEAE
RTIQAMLRDA QATEASDYAF RDHLFDLKNT QSQQFSRLQT VGNTVKRAED LAGRYNDKIQ
NTQRLIEKTR KDLEQAKTNM RKVALPSLDL PGDSNTLTVL AQEATALADR HKQQADEIEQ
TAKSASAISD QAYELVRSTV QGEKGTADSI ERLNDLYNTI QTTTKDLETQ ADQAHSQSEI
VNQDALRIYN DMSTLKKFDP MLIQKELKKV KQDVADKTRQ VNKRQTQFED LQNNMKNSQM
EVKDLLKDGE DAQMVADGLL ARANAARTLA EKALKSGNAS FYEVEDILNS LEGFHDKINN
NKAEAEKALK KLPAISSAIA EANNKRKQAE ASLGNAMRDA AVAKDTAKEA QATTDYVKME
AEELKADASD SFKHALDLEE DTDKLRKQLK AVEKDFEKKN KDADQDVENI QETSGAVEGA
QGKAESTRTA VRNALTTINN VLEQLGKPEG IDSQRLQSLE DALKAAKSQF NNKLSPKLED
LEQAAVGQNT RILTLEENIV NIMADIANLE DIERSLPLGC YNTAPLERP
//
