ID A0A1S3K4C5_LINUN Unreviewed; 1842 AA.
AC A0A1S3K4C5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Protocadherin Fat 4 {ECO:0000313|RefSeq:XP_013417101.1};
GN Name=LOC106178461 {ECO:0000313|RefSeq:XP_013417101.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013417101.1};
RN [1] {ECO:0000313|RefSeq:XP_013417101.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013417101.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR RefSeq; XP_013417101.1; XM_013561647.1.
DR EnsemblMetazoa; XM_013561647.1; XP_013417101.1; LOC106178461.
DR GeneID; 106178461; -.
DR KEGG; lak:106178461; -.
DR InParanoid; A0A1S3K4C5; -.
DR OrthoDB; 2969991at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 10.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00054; EGF_CA; 6.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.60.40.60; Cadherins; 8.
DR Gene3D; 2.10.25.10; Laminin; 8.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR24028:SF146; CADHERIN FAMILY; 1.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR Pfam; PF00028; Cadherin; 1.
DR Pfam; PF07645; EGF_CA; 3.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF12661; hEGF; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 10.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF49313; Cadherin-like; 8.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 3.
DR PROSITE; PS50268; CADHERIN_2; 8.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50923; SUSHI; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PROSITE-ProRule:PRU00043};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1842
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010306435"
FT TRANSMEM 1736..1761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..119
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 221..269
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 312..381
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 386..476
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 498..584
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 788..885
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 894..989
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 989..1094
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1121..1249
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1350..1471
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1486..1528
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1530..1568
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1570..1606
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1608..1646
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1672..1709
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 1518..1527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1539..1556
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1558..1567
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1596..1605
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1699..1708
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1842 AA; 200454 MW; F14154FB7F3712C5 CRC64;
MAWISSLFRS WWLCFIVVVV IGSAKGGNLL QVQHVVDSSR VRRNSDPCQN NNGGCSYMCV
ATVPSYRCTC PTGYRLMADG KACQDKDECL EPNACPELGQ CVNTPGSYRC VCPSGFACDS
RDSSCVDIDE CLLGTIACSQ GCHNTQGSYR CVCSTGFALQ EDGATCEDID ECIEYSPCNV
SCINFPGSYT CSCGEGQYYS SRSSTCVPAS CAALYMEKLV THCTIQEKVE YDYGEVCTLQ
CKQGVTVGST TVECTGSGEW SPVMADCVEE KPPSPPPHIY LSSNTIQEHS HRMTAIGWLR
TMYVRDSPDR VYTLHNHTDI FGVYGSGHDA KLVVTGNLDF ELQPTYWLNI SASSDIPPNT
INNIITVHIS DINEPPSIPL LNSSILAETA SVGTQVTSVQ AVDPDRGQNL TYRIVSGAHD
DFEFKDNLLL VKSSLDFETR ELYDIEIEVR DDGIPSLATR GTLRVFVTNI NEAPTSILLN
SSDVQEYVTG KRTGTRNGTV ISTLTAVDED RNDIHTFTVL DPRQNGLECF SIYESYLVVG
NENCFDYETN RVLTVQLQVQ DSGFLTYTKT KSISILDQNE APNRVVLSSD QIFSLSPAGT
VVGTLSAVDP DNGDRHNFTL TGPSQQFILE GNKLKVKTDL SLLTSPTVQV TIQATDLGGL
PCQQSLTIGL IPVSSSIMYG SADYEVTLSP SSVLENSAAG TEVGAVSIVH HGNGEVTEQF
TCVLRDDGGG MFIVQDRNRI AVSGSTLIDF ESGHQIQIQV ECFSSSEVLH QTFVITILNV
NEPPTDIKSE TGKFEVMENK MPGELIAYLS AEDPDQGDQF RFMLESSFTM VPFAIGANHL
ITHNLINFEL TPSFDITIFV TDNGGLRFSK AITVTVVDQN DPPTQILMAD GTCIIESAAI
NSVVTTLRTV DEDVEQLHTY TIQDQNPPGA LAIHNRNKLV VADASKIDYE KYHSVEVTIV
TQDNGLPLAL SYTQTLTIPV LDANESPTRI SLDNYTVAEN SPPGTLVANI HVEDPDTFHQ
VFYCTLMQDA IGRFQIQFVP LVEQNLLVVA DGSLLNYEQS DTHLIEIMCK DCGGLNVSSS
FSVQVLDIND APLKVIFVDS KGDTMTAPYP PSETQQQISH LPSSYVVVVN ETMDPSSIGN
EIVAYFSVMD DDSLQAGKQK HTCHLVSEAD YINNNLEGPA SEMSSRFQLM TLNGSVWNAV
VVREKLDYEE VVAVFYLYLR CTDDGIPTPL AVMASLKVVV ADVPEAPYNI SLSNNNILEN
SAPESTVGLL TIHDEDPPLS GYIITVTTSG TPFYVRGQEL KVLNNRLNYE LKSVFTVQVE
AKEVETGLSL TKNFTINIIN VDEPPCCLQI NGQTELELPD NMAVGTEIGT LTVVDQDVGD
THTFSFQPDR KRRDLDDHVS YFRLEGNKLY LSKALDPLSY AMLGISILAV DSTGLQLLEQ
LYFKVLMINC GGVKCSSANG LCDKGQLPPS CRCKLGFEGN GINCTNIDEC SPISPCHPEN
SLGCIDGYGG VNNYTCMCKD GWMPPNCEQR VDQCDTAMCS RNGTSSCVHQ STGTQCVCKA
GYTGRSCDID VDDCVPGVCG NGGQCQDGIS GYSCVCPPGY EGRHCEIDRT ACLTVQCPFN
GSCIVLSGPG GGHVCQCQAP YSLDCRGCAY GYGGPQCKPC DSQHTGYDCK IKTAVCSSSP
CEHNSTCVDL DNSRFGCICA GGWTGPTCSK LSIKSNTFYV HSQPSQASGT EGEISMVIYV
IIGILAFLLT VLVVIVTFYM VRRKRKKRSA RGRVRYASSN QDPFVFGPPR SICADSERRH
SWEAETQQFV NPVYSSMESA LAANVEVSSG ECVAKVADQD AS
//
