ID A0A452FAH5_CAPHI Unreviewed; 1792 AA.
AC A0A452FAH5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Laminin subunit alpha 4 {ECO:0000313|Ensembl:ENSCHIP00000021328.1};
GN Name=LAMA4 {ECO:0000313|Ensembl:ENSCHIP00000021328.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000021328.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000021328.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000021328.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
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; LWLT01000012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSCHIT00000029172.1; ENSCHIP00000021328.1; ENSCHIG00000019560.1.
DR GeneTree; ENSGT00940000159970; -.
DR Proteomes; UP000291000; Chromosome 9.
DR Bgee; ENSCHIG00000019560; Expressed in descending colon and 17 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
DR GO; GO:0030334; P:regulation of cell migration; IEA:InterPro.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:InterPro.
DR CDD; cd00055; EGF_Lam; 3.
DR CDD; cd00110; LamG; 5.
DR Gene3D; 2.60.120.200; -; 5.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009254; Laminin_aI.
DR InterPro; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR15036:SF49; AXOTACTIN; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00053; Laminin_EGF; 3.
DR Pfam; PF02210; Laminin_G_2; 4.
DR Pfam; PF06008; Laminin_I; 1.
DR Pfam; PF06009; Laminin_II; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00180; EGF_Lam; 3.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1792
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019553552"
FT DOMAIN 82..131
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 132..186
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 187..240
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1016..1196
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1203..1371
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1438..1609
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1616..1789
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 510..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 339..505
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 562..614
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 510..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 101..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 157..166
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 212..221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 224..238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1792 AA; 198705 MW; 4C2C228D482ADEA2 CRC64;
MALSSAWCAV LPLWLLCGAA CSRAASGDGS AFPFDMEGSS AFGRLDPPET SEPRAAPGSL
PPAAKKCDAG FFFAYSEECL PCDCNGNSNE CLDGSGLCVH CQRNTTGEHC EKCLDGYIGD
AIRGPPRFCQ PCPCPLPHVA NFAESCYRKN GAVRCICKEN YAGPNCERCA PGYYGNPLLI
GSTCKKCDCS GNSDPNLIFE DCDEVTGQCR NCLRNTTGFK CERCAPGYYG DARRAKNCAA
CNCGGGPCDS VTGECLEEGF EPPTGTDCPT ISCDKCIWDL TDDLRLAALS IEESKSGLLS
VSSGAAAHRH VNEINSTIYL LKTKLSEREN QYVLRKIQIN NAENTMKSLQ SDVEELAERE
SQASRKVQLA QKESMDTINH ATQLAEQAHN MRDKIQEISS KMLYYGEEQE LSSEEISEKL
VLAQKMLEEI RRRQPFLTQR ELVDEEADEA HELLSQAESW QRQYNDTRSL FPVVLEQLDD
YNAKLSDLQE SLDQALNHVR DAEDMNRATA ARQRDHEKQH ERVREQTEGV NVSLRTSSDS
LMMPRLTLSE LDNIIKNASG IYAEIDGAKN ELQRKLSNLS NLSHDLVQEA VDHARNLQQE
ADELSRNLHS SDMNGLVQKA LDASNVYENI ANYVSEANET AEQALNITDR IYDVKISRHT
PPHPHLCPTC ASFGFFSAGS DEAVVDTSRR VGGALARKSA LRNRLNDAIK RLQAAERGDA
QQRLGQSQLI TAEANKTTME VQEATAPMAS NLTNWSQNLQ SFDSSAYNTA VDSARDAVGN
LTEVVPQLLD QLRTVEQKRP ASNVSASIQR IRELIAQTRS VASKIQVSMM FDGQSAVEVH
PRASMDDLKT YTSLSLYMKP PPVKQSELAV TADQFILYLG SKNVRASDKC FSLASKKTTL
KILYLNRVGK HGKVFLTVPS LSSTAEEKFI KKGEFAGDDS LLDLDPEDTV FYVGGVPSNF
KLPASLNLPG FVGCLELATL NNDVISLYNF KHIYNMDPSK SVPCARDKLA FTQSRAASYF
FDGSSYAIVR DITRRGKFGQ VTRFDIEVRT PTDNGLVLLM VNGSMFFSLE MRNGYLHVFY
DFGFSNGPVH LEDTLKKAQI NDAKYHEISI IYHNDKKMIL VVDRRHVKSM DNEKMKIPFT
DIYIGGAPPE ILQSRTLRAH LPLDINFRGC MKGFQFQKKD FNLLEQTETL GVGYGCPEDS
LISRRAYFNG QSYIASSQKI SFFDGFEGGF NFRTLQPNGL LFYYASGSDM FSISLNNGTV
IMDVKGIKVQ SADKQYNDGL SHFIVTSVSP ARYELIVDKS RLGSKNPTKG KVEQTQAGEK
KFYFGGSPIT PQYANFTGCI SNAYFTRLDR DVEVEDFQRY SEKVHTSLYE CPIESSPLFL
LHKKGRNSSK PKTNQNKKGG KSKDAPSWDP VGLKFLERNI PRDSHCQLSN SPRAIEHAYQ
YGGTANSRQE FEHLKGDFGE KSQFSIRLKT RSSHGMIFYV SDQEENNFMT LFLAHGRLVF
MFNVGHKKLK IRSQEKYNDG LWHDVIFIRE KSSGRMIIDG LRILEESLPP AGADWKIRGP
IYLGGVAPGR AVKNVQINSV YSFSGCLGNL QLNGASITSA AQTFSVTPCF EGPMETGTYF
STEGGYVVLD ESFNIGLKFE IAFEVRPRSS SGTLVHGHSV NGEYLNVHMK NGQVIVKVNN
GIRDFSTSVT PKQSLCDGRW HRITVIRDSN VVQLDVDSEV NHVVGPLNPK PVDHREPVFV
GGVPESLLTP RLAPGRPFTG CIRHFVIDGR PVSFSKAALV SGAVSINSCP AA
//
