ID M3W293_FELCA Unreviewed; 1747 AA.
AC M3W293;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 4.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Laminin subunit beta 4 {ECO:0000313|Ensembl:ENSFCAP00000004135.6};
GN Name=LAMB4 {ECO:0000313|Ensembl:ENSFCAP00000004135.6,
GN ECO:0000313|VGNC:VGNC:68010};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000004135.6, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000004135.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004135.6,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000004135.6, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004135.6,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000004135.6}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000004135.6};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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; AANG04003224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9685.ENSFCAP00000004135; -.
DR PaxDb; 9685-ENSFCAP00000004135; -.
DR Ensembl; ENSFCAT00000004480.6; ENSFCAP00000004135.6; ENSFCAG00000004479.6.
DR VGNC; VGNC:68010; LAMB4.
DR eggNOG; KOG0994; Eukaryota.
DR GeneTree; ENSGT00940000162514; -.
DR HOGENOM; CLU_001560_1_0_1; -.
DR InParanoid; M3W293; -.
DR OMA; RRCSCHP; -.
DR Proteomes; UP000011712; Chromosome A2.
DR Bgee; ENSFCAG00000004479; Expressed in zone of skin and 5 other cell types or tissues.
DR GO; GO:0043256; C:laminin complex; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd22301; cc_LAMB4_C; 1.
DR CDD; cd00055; EGF_Lam; 13.
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; 1.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 12.
DR Pfam; PF21199; LAMININ_IV_B; 1.
DR Pfam; PF00055; Laminin_N; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 13.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 11.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1747
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023903287"
FT DOMAIN 24..264
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 265..331
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 332..394
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 395..454
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 455..505
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 545..763
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 769..816
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 817..862
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 863..910
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 970..1021
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1022..1079
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1080..1127
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1128..1174
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1408..1470
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1528..1741
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 297..306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 362..371
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 425..434
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 477..486
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 489..503
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 769..781
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 771..788
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 790..799
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 817..829
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 819..836
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 838..847
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 882..891
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 894..908
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 994..1003
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1052..1061
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1080..1092
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1082..1099
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1101..1110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1128..1140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1130..1147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1149..1158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1747 AA; 191326 MW; 244AF8FA681501DC CRC64;
MQLPLTFLLH LGLLSFTKAQ DKCHRSACHP TTGDLLVGRS AQLTASSTCG LDGAQKYCIL
SYLEGEQKCF ICDSRFPYDP YTQSQSHTIE NVITSFEPGR DKKWWQAENG LDHVSIRLDL
EALFQFSHLI LTFKTFRPAA MLVERSTDYG HTWKVLKYFA KDCAASFPNI TSGQAQGVGD
LVCDSKYSDI EPSSGGEVVL KVLDPRFEIE NPYSPYIQDL VTLTNLRINF TKLHTLGDTL
LGRRENGSLD NYYYALSNMV VGGSCFCHGH ASECGPVQKV RGDVFSPPGM VHGQCVCQHH
TDGPNCERCK GFFQDVPWRP AAGLQDSACR ACRCNGHSDR CHFDMTAYLA SGGRSGGVCE
DCQHHTEGQH CDRCRPLFYR DPLRAMSDPY ACIPCECDPD GTLSGGICVS HSDPALGSVA
GQCLCKENVE GAKCDQCKPN HHGLSAADPL GCQPCNCNPL GSLPLSACDV ETGQCACQSF
ATGPHCEECT VGYWGLENHL HGCSPCDCDI GGAYSNVCSP KDGQCECRPH ITGRSCTESA
PGYFFAPLNF YLYEAEEATP LQGLAPLGSV TFGQVPAVHG VFREPVPGSP TAWTGPGFAR
VLPGAGLRFA VDHIALPMDF TIAIRYEIQP AADWAVQILV NPLGKSKHCP RETPWPRPQS
FPLPATSRIV LLPTPICLEP DVQYSIDVYF SQALEGGAHA HSHILVDSLS LIPQINSLEN
FCSKQDLDEY HLHNCVDIAL KAGPQMLPGA CERLIVSMSA RLNNGAVACK CHPQGSVGPN
CSRLGGQCQC KPHVAGRCCD RCSTGSYGLG HHGCHPCHCH PQGSKSAVCD QITGQCACQG
EVAGLRCDRC LASYFGFPNC RPCLCNGFAE LCDPETGSCF NCGGFTTGRN CERCIDGYYG
DPPSGRSCRP CPCPDVPSSN QYFAHSCYQD PWSSDVICNC LQGYAGKQCG ECSAGFYGNP
RISGAPCRPC ACNNNIDVTD PESCSRVTGE CLRCLHDTQG PNCQFCKPGH FGSAINQTCR
RCSCHPSGVT PAACPPGQGA CLCDPNTGAC PCLPNVTGQT CDRCADRYWN LVPGRGCQPC
NCDPRTSHSG HCDQLTGQCP CKLGYDGQHC SECKENYYGD PLGRCLPCDC NTEGTQKPVC
DQNTGMCRCR EGVSGPRCDR CARGHGQEFP ACLPCHRCFD QWDRAAASLS KAVQGLIGLA
ANTEDKTETL LVCEADFKGL RENMSEIERI LKHPVFSSGE FLKAKDYQDS VREQIMQLSL
QLKAVHEFQD LKETMVRMKS EADLLFEDLR KEIDLRSRAH TANIMDPSET IKKHYQRSSS
AEKKITETTS IIKNSEKTRN DLHSMFDTLS SKENLSLEKL KQITVPDMQI LIEKVCGVPG
DMPCVLPSCG DPSCRGSRTL SGHALQQAQE AETVIHNLSD QVQGWKNQLK NVSKLAEVSK
SNALQLSEKL RNMKNQSESE EEKMSLLIKR LKKFLSEENV PPEDIEKVAN RVLDIHLPMA
SQNLTRELDK IRKLTQLCED NGTDAGRLNK AADEARKVLA KAKGAEKAAN VLLNLDKTLN
RLQQVQTTQG RINSAITQLT AEITKIKKNT VQAEKEAKDT ENKLDSAKQQ SVLEAGLSQL
RTTLQRNRGR AARLRAQAAS AQRQAGGLEQ EFAELNNQYA VLQHKTSATG LTKVTLDKVE
QLKEAAEKLA TDTEDKIRRI ADLEKKTQDL NLSRQEKADQ LKELEDQVVA LKNEIVEREN
KYAACYR
//
