ID A0A8C8BB20_9STRI Unreviewed; 1827 AA.
AC A0A8C8BB20;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Laminin subunit alpha-4 {ECO:0000256|ARBA:ARBA00072601};
DE AltName: Full=Laminin-14 subunit alpha {ECO:0000256|ARBA:ARBA00082518};
DE AltName: Full=Laminin-8 subunit alpha {ECO:0000256|ARBA:ARBA00080104};
DE AltName: Full=Laminin-9 subunit alpha {ECO:0000256|ARBA:ARBA00077984};
OS Otus sunia (Oriental scops-owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Strigiformes;
OC Strigidae; Otus.
OX NCBI_TaxID=257818 {ECO:0000313|Ensembl:ENSOSUP00000018125.1, ECO:0000313|Proteomes:UP000694552};
RN [1] {ECO:0000313|Ensembl:ENSOSUP00000018125.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSOSUP00000018125.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00002418}.
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. Alpha-4 is a
CC subunit of laminin-8 (laminin-411), laminin-9 (laminin-421) and
CC laminin-14 (laminin-423). {ECO:0000256|ARBA:ARBA00062601}.
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 Ensembl; ENSOSUT00000018729.1; ENSOSUP00000018125.1; ENSOSUG00000012831.1.
DR Proteomes; UP000694552; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-ARBA.
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:UniProtKB-KW.
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 FunFam; 2.10.25.10:FF:000051; Laminin subunit alpha 4; 1.
DR FunFam; 2.10.25.10:FF:000491; Laminin subunit alpha 4; 1.
DR FunFam; 2.10.25.10:FF:000569; Laminin subunit alpha 4; 1.
DR FunFam; 2.60.120.200:FF:000053; Laminin subunit alpha 4; 1.
DR FunFam; 2.60.120.200:FF:000058; Laminin subunit alpha 4; 1.
DR FunFam; 2.60.120.200:FF:000064; Laminin subunit alpha 4; 1.
DR FunFam; 2.60.120.200:FF:000066; Laminin subunit alpha 4; 1.
DR FunFam; 2.60.120.200:FF:000087; Laminin subunit alpha 4; 1.
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.
DR InterPro; IPR009254; Laminin_aI.
DR InterPro; IPR010307; Laminin_dom_II.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR056863; LMN_ATRN_NET-like_EGF.
DR InterPro; IPR050372; Neurexin-related_CASP.
DR PANTHER; PTHR15036:SF47; LAMININ SUBUNIT ALPHA-4; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 1.
DR Pfam; PF00053; EGF_laminin; 2.
DR Pfam; PF24973; EGF_LMN_ATRN; 1.
DR Pfam; PF02210; Laminin_G_2; 5.
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; 5.
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; 5.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000694552};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1827
FT /note="Laminin subunit alpha-4"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5034943893"
FT DOMAIN 84..133
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 134..188
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 189..242
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 837..1038
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1050..1229
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1236..1404
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1473..1644
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1651..1824
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1329..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 341..403
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 438..472
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1415..1431
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 103..112
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 159..168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 214..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 226..240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 1827 AA; 202443 MW; 50E5915E15C189B8 CRC64;
MALIFAWPLV SPILFFLRCF SSSTASSEGG VFQFDIEGSS AVSVQEATVI RGQQQAVATG
SWVPFAEGCQ EGFYRTSSGK CSPCNCNGNA NRCLDGSGIC LDCQRNTTGQ HCEQCPDGYI
GDVVRGVPTF CQPCPCPLPT LANFAVSCYR KSGGVRCVCK ENYAGPNCER CAPGYYGNPL
LIGSTCKKCD CSGNSDPNLI FEDCDEVTGQ CRNCLRNTTG FKCERCAPGY YGDARFAKNC
TECNCGGRMC DSQTGECLAD SPEVSTGTDC PTISCDKCIW DLTDDIRLAV LAIDESKSTL
LSISTGVAAQ KRLNDLNLTT THLQAAMSKK KNHAVLWTIQ ADDAADEMND LLREAATLDE
QGNEASSKGL LIQKETMETN NRATQLVQQL SNMRDNIQEI SSKMKYYAIQ QELSPEEIAQ
KLSAAEEMLK EIKRRKPFTN QRQLADEEEN AAEELLQQVE EFHERYNDTR SLVSDVLEQL
SEQDVKLSDL EEALDQALDY VIQTEDINKE NTASLQRREK QHEKIKEQID EVNGILLSAT
TILAGPQKVN SELSEVIKNV SGFYAEIDGA KKELQEKLAN LSLFDDDLVE KAMHHAHNLR
RLADELDRNL YGVDTNGLVQ RAINASNVYE NIASYIEEAN KAALLALNTT NRVNDAAVGI
DTQIIYHKGK SEELLNRAME LQRAADDSND LTIADTSQHV NGTLARMNAL RSQLMRAITK
MQSAEPVEAR ERLEQAKVKT AEAVSATMTV TQATTPMDEN VRLWSQNLQD FQHSSAAYDS
AVHSAGDAVK KLTEVFPQLL DKLRRVEQKA PANNISSSIQ RIRELIAQTR SVASKVQVSM
MFGGQSAVEV NPKINVEELK SFTSMSLYIK FQKDNPQLAA SPDRFILYLG NKNAKNYIGL
AIKNDNLVYI YNLGGQDVEI PLDAKPVSTW PSYFSIIKIE RIGRHGKMFL TVPSLSSTAE
EKFIKKGEVP GPDSLLNLEP ENAVFYVGGV PPDFKLPPSL NLPGFIGCLE LATLNDDVIS
LYNFKQVYNI DTTTSPPCAR NKLAFTQSRA VSYFFDGSGY ALARNIERRG RFSQVTRFDI
EVRTPTDNGL ILLMINGSMF FSLEMHNGFL YLRYDFGFST GPVLLEDSMK KAQINDAKFH
EISIIYHNSK KMILVVDRRH IKSVDNERTA MPFTDIYIGG APAEILHSSI SSHLAGSIGF
KGCMKGFQFQ KKDFNLLEEP GTLGISYGCP EDSLISRKAY FNGESFIASS QKVSLFSEFE
GGFNFRTLQP NGLLFYYSEG SDVLSISMDR GAVVLNASGI KIQSPDRNYN DGKNHFIITS
VTPERYELTV DDKKQSKKNP SKDRAGKSPD SVKKFYFGGS PLRTQQANFT GCISNAYFTR
LDREVEVEDF QQYSEKVQTS LYGCPVESPP VALLHKKGKN SSKAKGNRNK KVGRDKDKIS
QPSTGLKKTY QEVNMQRDPQ CHLPMNPKAT KHAYQFGGTA NSRQEFDHIP KDFSQRAHFS
ISLKTHSSHG MIFYVSDQKE TNFMALFVAH GRLIFVFNVG HQKIRIKSQE KYNDGLWHNV
IFIRGKNIGR LIIDGLRVLE EPFSGDANSW QVTEPLYIGG VAPGKAVKNI QINSVYSFSG
CLSNLQLNGR SVTSASQTFS VTPCFEGPSE AGTYFSSEGG YVVLDESFSL GLKFEVVFEI
RPRSSSGILL HGHSVNGEYL NMHMRNGQVT VKLNNGIRDF STSVTLKQSL CDGRWHRIAV
IRDANVVQLD VDSEVNHVVG PLNPKATDHR EPVFIGGVPE SLLTSSLTTR NSFIGCIRNF
MIDEKPVSFS KAALVSGAVS INTCPAA
//
